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Escherichia coli K-12 substr. MG1655 Protein: 50S ribosomal subunit

Synonyms: ribosome, large subunit

Component of: ribosome (summary available)

Subunit composition of 50S ribosomal subunit = [RrlA][RrfA][RplA][RplB][RplC][RplD][RplE][RplF][(RplJ)([RplL]2)2][RplI][RplK][RplM][RplN][RplO][RplP][RplQ][RplR][RplS][RplT][RplU][RplV][RplW][RplX][RplY][RpmA][RpmB][RpmC][RpmD][RpmE][RpmF][RpmG][RpmH][RpmI][RpmJ]
         23S ribosomal RNA (rrlA) = RrlA (extended summary available)
         5S ribosomal RNA (rrfA) = RrfA (extended summary available)
         50S ribosomal subunit protein L1 = RplA (extended summary available)
         50S ribosomal subunit protein L2 = RplB (summary available)
         50S ribosomal subunit protein L3 = RplC (summary available)
         50S ribosomal subunit protein L4 = RplD (extended summary available)
         50S ribosomal subunit protein L5 = RplE (extended summary available)
         50S ribosomal subunit protein L6 = RplF (summary available)
         50S ribosomal protein complex L8 = (RplJ)([RplL]2)2 (summary available)
                 50S ribosomal subunit protein L10 = RplJ (extended summary available)
                 50S ribosomal subunit protein L7/L12 dimer = (RplL)2
                         50S ribosomal subunit protein L12 = RplL
         50S ribosomal subunit protein L9 = RplI (extended summary available)
         50S ribosomal subunit protein L11 = RplK (extended summary available)
         50S ribosomal subunit protein L13 = RplM (extended summary available)
         50S ribosomal subunit protein L14 = RplN (extended summary available)
         50S ribosomal subunit protein L15 = RplO (summary available)
         50S ribosomal subunit protein L16 = RplP (extended summary available)
         50S ribosomal subunit protein L17 = RplQ (summary available)
         50S ribosomal subunit protein L18 = RplR (extended summary available)
         50S ribosomal subunit protein L19 = RplS (extended summary available)
         50S ribosomal subunit protein L20 = RplT (extended summary available)
         50S ribosomal subunit protein L21 = RplU (summary available)
         50S ribosomal subunit protein L22 = RplV (extended summary available)
         50S ribosomal subunit protein L23 = RplW (extended summary available)
         50S ribosomal subunit protein L24 = RplX (summary available)
         50S ribosomal subunit protein L25 = RplY (extended summary available)
         50S ribosomal subunit protein L27 = RpmA (extended summary available)
         50S ribosomal subunit protein L28 = RpmB (summary available)
         50S ribosomal subunit protein L29 = RpmC (summary available)
         50S ribosomal subunit protein L30 = RpmD (summary available)
         50S ribosomal subunit protein L31 = RpmE (summary available)
         50S ribosomal subunit protein L32 = RpmF (summary available)
         50S ribosomal subunit protein L33 = RpmG (summary available)
         50S ribosomal subunit protein L34 = RpmH (summary available)
         50S ribosomal subunit protein L35 = RpmI (summary available)
         50S ribosomal subunit protein L36 = RpmJ (summary available)

Relationship Links: PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:2AW4 , PDB:Structure:2AWB

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Credits:
Created 02-Jun-2006 by Keseler I , SRI International


Subunit of: ribosome

Subunit composition of ribosome = [(RrsA)(RpsA)(RpsB)(RpsC)(RpsD)(RpsE)(RpsF)(RpsG)(RpsH)(RpsI)(RpsJ)(RpsK)(RpsL)(RpsM)(RpsN)(RpsO)(RpsP)(RpsQ)(RpsR)(RpsS)(RpsT)(RpsU)(Sra)][(RrlA)(RrfA)(RplA)(RplB)(RplC)(RplD)(RplE)(RplF)([RplJ][(RplL)2]2)(RplI)(RplK)(RplM)(RplN)(RplO)(RplP)(RplQ)(RplR)(RplS)(RplT)(RplU)(RplV)(RplW)(RplX)(RplY)(RpmA)(RpmB)(RpmC)(RpmD)(RpmE)(RpmF)(RpmG)(RpmH)(RpmI)(RpmJ)]
         30S ribosomal subunit = (RrsA)(RpsA)(RpsB)(RpsC)(RpsD)(RpsE)(RpsF)(RpsG)(RpsH)(RpsI)(RpsJ)(RpsK)(RpsL)(RpsM)(RpsN)(RpsO)(RpsP)(RpsQ)(RpsR)(RpsS)(RpsT)(RpsU)(Sra) (summary available)
                 16S ribosomal RNA (rrsA) = RrsA (extended summary available)
                 30S ribosomal subunit protein S1 = RpsA (extended summary available)
                 30S ribosomal subunit protein S2 = RpsB (summary available)
                 30S ribosomal subunit protein S3 = RpsC (summary available)
                 30S ribosomal subunit protein S4 = RpsD (extended summary available)
                 30S ribosomal subunit protein S5 = RpsE (extended summary available)
                 30S ribosomal subunit protein S6 = RpsF (extended summary available)
                 30S ribosomal subunit protein S7 = RpsG (extended summary available)
                 30S ribosomal subunit protein S8 = RpsH (extended summary available)
                 30S ribosomal subunit protein S9 = RpsI (extended summary available)
                 30S ribosomal subunit protein S10 = RpsJ (extended summary available)
                 30S ribosomal subunit protein S11 = RpsK (summary available)
                 30S ribosomal subunit protein S12 = RpsL (extended summary available)
                 30S ribosomal subunit protein S13 = RpsM (extended summary available)
                 30S ribosomal subunit protein S14 = RpsN (summary available)
                 30S ribosomal subunit protein S15 = RpsO (extended summary available)
                 30S ribosomal subunit protein S16 = RpsP (summary available)
                 30S ribosomal subunit protein S17 = RpsQ (summary available)
                 30S ribosomal subunit protein S18 = RpsR (extended summary available)
                 30S ribosomal subunit protein S19 = RpsS (summary available)
                 30S ribosomal subunit protein S20 = RpsT (extended summary available)
                 30S ribosomal subunit protein S21 = RpsU (summary available)
                 30S ribosomal subunit protein S22 = Sra (summary available)
         50S ribosomal subunit = (RrlA)(RrfA)(RplA)(RplB)(RplC)(RplD)(RplE)(RplF)([RplJ][(RplL)2]2)(RplI)(RplK)(RplM)(RplN)(RplO)(RplP)(RplQ)(RplR)(RplS)(RplT)(RplU)(RplV)(RplW)(RplX)(RplY)(RpmA)(RpmB)(RpmC)(RpmD)(RpmE)(RpmF)(RpmG)(RpmH)(RpmI)(RpmJ)
                 23S ribosomal RNA (rrlA) = RrlA (extended summary available)
                 5S ribosomal RNA (rrfA) = RrfA (extended summary available)
                 50S ribosomal subunit protein L1 = RplA (extended summary available)
                 50S ribosomal subunit protein L2 = RplB (summary available)
                 50S ribosomal subunit protein L3 = RplC (summary available)
                 50S ribosomal subunit protein L4 = RplD (extended summary available)
                 50S ribosomal subunit protein L5 = RplE (extended summary available)
                 50S ribosomal subunit protein L6 = RplF (summary available)
                 50S ribosomal protein complex L8 = (RplJ)([RplL]2)2 (summary available)
                         50S ribosomal subunit protein L10 = RplJ (extended summary available)
                         50S ribosomal subunit protein L7/L12 dimer = (RplL)2
                                 50S ribosomal subunit protein L12 = RplL
                 50S ribosomal subunit protein L9 = RplI (extended summary available)
                 50S ribosomal subunit protein L11 = RplK (extended summary available)
                 50S ribosomal subunit protein L13 = RplM (extended summary available)
                 50S ribosomal subunit protein L14 = RplN (extended summary available)
                 50S ribosomal subunit protein L15 = RplO (summary available)
                 50S ribosomal subunit protein L16 = RplP (extended summary available)
                 50S ribosomal subunit protein L17 = RplQ (summary available)
                 50S ribosomal subunit protein L18 = RplR (extended summary available)
                 50S ribosomal subunit protein L19 = RplS (extended summary available)
                 50S ribosomal subunit protein L20 = RplT (extended summary available)
                 50S ribosomal subunit protein L21 = RplU (summary available)
                 50S ribosomal subunit protein L22 = RplV (extended summary available)
                 50S ribosomal subunit protein L23 = RplW (extended summary available)
                 50S ribosomal subunit protein L24 = RplX (summary available)
                 50S ribosomal subunit protein L25 = RplY (extended summary available)
                 50S ribosomal subunit protein L27 = RpmA (extended summary available)
                 50S ribosomal subunit protein L28 = RpmB (summary available)
                 50S ribosomal subunit protein L29 = RpmC (summary available)
                 50S ribosomal subunit protein L30 = RpmD (summary available)
                 50S ribosomal subunit protein L31 = RpmE (summary available)
                 50S ribosomal subunit protein L32 = RpmF (summary available)
                 50S ribosomal subunit protein L33 = RpmG (summary available)
                 50S ribosomal subunit protein L34 = RpmH (summary available)
                 50S ribosomal subunit protein L35 = RpmI (summary available)
                 50S ribosomal subunit protein L36 = RpmJ (summary available)

Summary:
The ribosome is a complex machinery that translates the genetic code.

A crystal structure of the E. coli ribosome has been determined at 3.5 Å resolution [Schuwirth05]. Additional crystal structures of the ribosome with tRNA bound in two functionally distinct states reveal how a ratchet-like motion of the small and large subunits contributes to translocation, termination of translation, and ribosome recycling [Zhang09, Dunkle11].

Approximately eight molecules of Zn2+ are bound to the ribosome; therefore, it appears that a large fraction of intracellular Zn2+ is ribosome-associated [Hensley11].

Selected reviews: [Ramakrishnan02, Yonath05, Ogle05, Kaczanowska07]

Citations: [Kuhlenkoetter11]

Relationship Links: PDB:Structure:3R8N , PDB:Structure:3R8O , PDB:Structure:3R8S , PDB:Structure:3R8T

Credits:
Created 15-Jun-2006 by Keseler I , SRI International


Subunit of 50S ribosomal subunit: 23S ribosomal RNA (rrlA)

Synonyms: rrlA

Gene: rrlA Accession Numbers: EG30077 (EcoCyc), b3854, ECK3846

Sequence Length: 2902/3 AAs

MultiFun Terms: cell structure ribosomes
information transfer protein related translation
information transfer RNA related rRNA, stable RNA

Unification Links: EcoliWiki:b3854

Reactions known to consume the compound:

Not in pathways:
23S rRNA[periplasmic space] + H2O[periplasmic space] → 2 a single-stranded RNA[periplasmic space]

Not in pathways:
rRNA + S-adenosyl-L-methionine → rRNA containing N6,N6-dimethyladenine + S-adenosyl-L-homocysteine

Not in pathways:
23S rRNA[periplasmic space] + H2O[periplasmic space] → 2 a single-stranded RNA[periplasmic space]

Reactions known to produce the compound:

tRNA processing :
a tRNA precursor with a 5' extension and a short 3' extension + H2O → a tRNA precursor with a short 3' extension + a single-stranded RNA
a tRNA precursor with a 5' extension + H2O → an uncharged tRNA + a single-stranded RNA

Not in pathways:
YhaV endonuclease degradation substrate mRNA + H2O → 2 a single-stranded RNA
an mRNA + H2O → a single-stranded RNA + a single-stranded RNA
an mRNA + H2O → a single-stranded RNA + a single-stranded RNA
RNase E degradation substrate mRNA + n H2O → n a single-stranded RNA
YhaV endonuclease degradation substrate rRNA + H2O → 2 a single-stranded RNA
RNase III mRNA processing substrate + 2 H2O → RNase III processing product mRNA + 2 a single-stranded RNA
an mRNA[periplasmic space] + H2O[periplasmic space] → 2 a single-stranded RNA[periplasmic space]
RNase G degradation substrate mRNA + H2O → 2 a single-stranded RNA
9S rRNA + 2 H2O → 5S rRNA + 2 a single-stranded RNA
RNase E mRNA processing substrate + n H2O → RNase E processing product mRNA + n a single-stranded RNA

Reactions known to both consume and produce the compound:

Not in pathways:
a single-stranded RNA + phosphate ↔ a single-stranded RNA + a nucleoside diphosphate

In Reactions of unknown directionality:

Not in pathways:
rRNA[periplasmic space] = 2 a single-stranded RNA[periplasmic space]

Not in pathways:
rRNA[periplasmic space] = 2 a single-stranded RNA[periplasmic space]

Summary:
The 23S and 5S rRNAs are the RNA components of the large subunit (50S subunit) of the E. coli ribosome.

There are seven ribosomal RNA (rRNA) operons, called rrnA, rrnB, rrnC, rrnD, rrnE, rrnG, and rrnH. Each operon contains a 16S rRNA gene, a 23S rRNA gene, and a 5S rRNA gene (except the rrnD operon, which contains two 5S rRNA genes) interspersed with various tRNA genes. Regarding nomenclature, "rrs" genes encode 16S rRNAs, "rrl" genes encode 23S rRNAs, and "rrf" genes encode 5S rRNAs [Neidhardt96].

The sequence and structure of the 23S rRNA has been described, and the relationship of the 23S rRNA to ribosome assembly, structure, and function has been characterized. Interactions between the 23S rRNA and ribosomal proteins have been described.

The relationship of the 23S rRNA to sensitivity to multiple antibiotics is discussed. 23S rRNA also encodes a short peptide that plays a role in erythromycin resistance.

Analysis of mutations in 23S rRNA has been conducted.

The 23S rRNA is subject to pseudouridylation, dihydrouridylation, and methylation. Processing and modification of the 23S rRNA has been characterized. Possible roles for the modified nucleotides have been proposed [Sergiev07]; their location has been visualized in a cryo-EM structure of the ribosome [Fischer15].

Reviews describing these results are available.

Regulation has been described in detail; for a review see [Schneider03].

Reviews: [Arthur87a, BrissonNoel88, Dahlberg89, Srivastava91, Brimacombe91, Brimacombe92, Lane92, Mueller95, Wower95, Tenson95, Liebman95, Douthwalte95, Triman96a, Triman97, Triman98, Triman99, Charette00, Nakajima99, Stark02, Kim01g].


Subunit of 50S ribosomal subunit: 5S ribosomal RNA (rrfA)

Synonyms: rrfA

Gene: rrfA Accession Numbers: EG30070 (EcoCyc), b3855, ECK3847

Sequence Length: 39 AAs

MultiFun Terms: cell structure ribosomes
information transfer protein related translation
information transfer RNA related rRNA, stable RNA

Unification Links: EcoliWiki:b3855

Reactions known to consume the compound:

Not in pathways:
rRNA + S-adenosyl-L-methionine → rRNA containing N6,N6-dimethyladenine + S-adenosyl-L-homocysteine

Reactions known to produce the compound:

Not in pathways:
9S rRNA + 2 H2O → 5S rRNA + 2 a single-stranded RNA

tRNA processing :
a tRNA precursor with a 5' extension and a short 3' extension + H2O → a tRNA precursor with a short 3' extension + a single-stranded RNA
a tRNA precursor with a 5' extension + H2O → an uncharged tRNA + a single-stranded RNA

Not in pathways:
YhaV endonuclease degradation substrate mRNA + H2O → 2 a single-stranded RNA
an mRNA + H2O → a single-stranded RNA + a single-stranded RNA
an mRNA + H2O → a single-stranded RNA + a single-stranded RNA
RNase E degradation substrate mRNA + n H2O → n a single-stranded RNA
YhaV endonuclease degradation substrate rRNA + H2O → 2 a single-stranded RNA
RNase III mRNA processing substrate + 2 H2O → RNase III processing product mRNA + 2 a single-stranded RNA
23S rRNA[periplasmic space] + H2O[periplasmic space] → 2 a single-stranded RNA[periplasmic space]
an mRNA[periplasmic space] + H2O[periplasmic space] → 2 a single-stranded RNA[periplasmic space]
RNase G degradation substrate mRNA + H2O → 2 a single-stranded RNA
9S rRNA + 2 H2O → 5S rRNA + 2 a single-stranded RNA
RNase E mRNA processing substrate + n H2O → RNase E processing product mRNA + n a single-stranded RNA

Reactions known to both consume and produce the compound:

Not in pathways:
a single-stranded RNA + phosphate ↔ a single-stranded RNA + a nucleoside diphosphate

In Reactions of unknown directionality:

Not in pathways:
rRNA[periplasmic space] = 2 a single-stranded RNA[periplasmic space]

Not in pathways:
rRNA[periplasmic space] = 2 a single-stranded RNA[periplasmic space]

Summary:
The 5S and 23S rRNAs are the RNA components of the large subunit (50S subunit) of the E. coli ribosome.

There are seven ribosomal RNA (rRNA) operons, called rrnA, rrnB, rrnC, rrnD, rrnE, rrnG, and rrnH. Each operon contains a 16S rRNA gene, a 23S rRNA gene, and a 5S rRNA gene (except the rrnD operon, which contains two 5S rRNA genes) interspersed with various tRNA genes. Regarding nomenclature, "rrs" genes encode 16S rRNAs, "rrl" genes encode 23S rRNAs, and "rrf" genes encode 5S rRNAs [Neidhardt96].

The sequence and structure of the 5S rRNA has been described, and the relationship of the 5S rRNA to ribosome assembly, structure, and function has been characterized. Interactions between the 5S rRNA and 23S rRNA as well as ribosomal proteins have been described. Mutations in 5S rRNA have been analyzed, and the post-transcriptional processing of the 5S rRNA has been characterized.

Reviews describing these results are available.

Regulation has been described in detail; for a review see [Schneider03].

Reviews: [Lind78, Azad79, Tanaka85, Nowotny88, Moore88a, Vester88, Goringer88, Srivastava91, Barciszewska96, Barciszewska97]

Citations: [Pieler82]


Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L1

Synonyms: Rpy, RplA

Gene: rplA Accession Numbers: EG10864 (EcoCyc), b3984, ECK3975

Locations: cytosol, ribosome

Sequence Length: 234 AAs

Molecular Weight: 24.73 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0045947 - negative regulation of translational initiation Inferred from experiment [Baughman83]
GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
GO:0006417 - regulation of translation Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Arifuzzaman06, Butland05]
GO:0000049 - tRNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a]
GO:0015934 - large ribosomal subunit Inferred by computational analysis [GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation
regulation type of regulation posttranscriptional

Unification Links: DIP:DIP-35746N , EcoliWiki:b3984 , Mint:MINT-1268287 , ModBase:P0A7L0 , PR:PRO_000023809 , Pride:P0A7L0 , Protein Model Portal:P0A7L0 , RefSeq:NP_418411 , SMR:P0A7L0 , String:511145.b3984 , Swiss-Model:P0A7L0 , UniProt:P0A7L0

Relationship Links: InterPro:IN-FAMILY:IPR002143 , InterPro:IN-FAMILY:IPR005878 , InterPro:IN-FAMILY:IPR016094 , InterPro:IN-FAMILY:IPR016095 , InterPro:IN-FAMILY:IPR023673 , InterPro:IN-FAMILY:IPR023674 , InterPro:IN-FAMILY:IPR028364 , PDB:Structure:1EG0 , PDB:Structure:1ML5 , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2RDO , PDB:Structure:2WWQ , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J37 , PDB:Structure:3J46 , PDB:Structure:3J4X , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5S , PDB:Structure:3KCR , PDB:Structure:487D , PDB:Structure:4CSU , Pfam:IN-FAMILY:PF00687 , Prosite:IN-FAMILY:PS01199

Summary:
The L1 protein is a component of the 50S subunit of the ribosome and also functions in the post-transcriptional regulation of the ribosomal protein genes encoded in the L11 operon. Ribosomes lacking L1 show a lower translation activity than wild type [Subramanian80] and are defective in binding of aminoacylated tRNA [Sander83]. L1 has been identified within a 3-D map of the 70S ribosome constructed by cryo-electron microscopy [Malhotra98].

L1 interacts with a region in the 5' end of 23S rRNA [Branlant76a, Branlant80, Egebjerg91]. It also can be crosslinked to a region near the central fold of aminoacylated tRNA in the P and E site [Podkowinski89, Rosen93, Osswald95]. L1 is located within 21 Å of nucleotide C2475 of 23S rRNA, near the peptidyltransferase center [Muralikrishna95].

L1 is a translational repressor of the synthesis of L11 and L1, the proteins encoded by the L11 operon [Brot81, Thomas87, Stoffler81, Yates80, Dabbs81]. Synthesis of L1 is regulated by translational coupling to the synthesis of L11 [Yates81, Baughman83]. The target site for L1 binding to the mRNA is near the translation initiation site of L11 [Yates81, Baughman83, Thomas87a], and the presence of 23S rRNA relieves translational inhibition by L1 [Yates81]. The predicted secondary structure of the L1 binding region within 23S rRNA and rplKA mRNA is similar [Branlant80, Gourse81] and has been studied experimentally [Baughman84, Kearney87, Said88, Drygin00].

Both the growth rate control and stringent control of the synthesis of ribosomal proteins L11 and L1 are resulting from translational regulation by L1 [Cole86].

Essentiality data for rplA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L2

Synonyms: RplB

Gene: rplB Accession Numbers: EG10865 (EcoCyc), b3317, ECK3304

Locations: cytosol, ribosome

Sequence Length: 273 AAs

Molecular Weight: 29.86 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Chodavarapu11, Rippa10a, Arifuzzaman06, Butland05]
GO:0008270 - zinc ion binding Inferred from experiment [Katayama02]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ishihama08, Zhang07]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0015934 - large ribosomal subunit Inferred by computational analysis [GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35747N , EcoliWiki:b3317 , Mint:MINT-1322809 , ModBase:P60422 , PR:PRO_000023810 , Pride:P60422 , Protein Model Portal:P60422 , RefSeq:NP_417776 , SMR:P60422 , String:511145.b3317 , UniProt:P60422

Relationship Links: InterPro:IN-FAMILY:IPR002171 , InterPro:IN-FAMILY:IPR005880 , InterPro:IN-FAMILY:IPR008991 , InterPro:IN-FAMILY:IPR012340 , InterPro:IN-FAMILY:IPR014722 , InterPro:IN-FAMILY:IPR014726 , InterPro:IN-FAMILY:IPR022666 , InterPro:IN-FAMILY:IPR022669 , InterPro:IN-FAMILY:IPR022671 , Panther:IN-FAMILY:PTHR13691 , Panther:IN-FAMILY:PTHR13691:SF5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:487D , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00181 , Pfam:IN-FAMILY:PF03947 , Prosite:IN-FAMILY:PS00467

Summary:
The L2 protein is a component of the 50S subunit of the ribosome and is part of the peptidyltransferase center. L2 is highly evolutionarily conserved [Schmid84, Uhlein98].

L2 is required for the association of the 30S and 50S subunits [Diedrich00]; one end of the elongated L2 protein is located at the intersubunit interface of the 50S subunit [Willumeit01]. L2 is involved in binding of tRNA to both the A and P sites, and the His229 residue appears to be important for peptidyl-transferase activity of the ribosome [Diedrich00]. A conserved region within L2 is required for assembly of L16 into the 50S ribosomal subunit [Romero90]. Ribosome modulation factor binds near L2, L13, and S13 [Yoshida02b].

L2 interacts with domains II and IV of 23S rRNA [Egebjerg91, Beauclerk88, Thiede98, Ostergaard98] and with 5S rRNA [Okada00b]. L2 also interacts with aminoacyl-tRNA [Metspalu81, Remme85, Sumpter90].

Essentiality data for rplB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L3

Synonyms: RplC

Gene: rplC Accession Numbers: EG10866 (EcoCyc), b3320, ECK3307

Locations: cytosol, ribosome

Sequence Length: 209 AAs

Molecular Weight: 22.243 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Zheng11]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-10744N , EcoliWiki:b3320 , Mint:MINT-1302843 , ModBase:P60438 , PR:PRO_000023811 , Pride:P60438 , Protein Model Portal:P60438 , RefSeq:NP_417779 , SMR:P60438 , String:511145.b3320 , UniProt:P60438

Relationship Links: InterPro:IN-FAMILY:IPR000597 , InterPro:IN-FAMILY:IPR009000 , InterPro:IN-FAMILY:IPR019926 , InterPro:IN-FAMILY:IPR019927 , Panther:IN-FAMILY:PTHR11229 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00297 , Prosite:IN-FAMILY:PS00474

Summary:
The L3 protein is a component of the 50S subunit of the ribosome. L3 and L24 are the two proteins that initiate assembly of the 50S subunit [Nowotny82].

The L3 protein is methylated at the glutamine residue in position 150 [Lhoest77, Arnold99]. A prmB mutant which lacks methylation of L3 has a cold-sensitive growth phenotype and accumulates abnormal ribosomal particles; however, lack of L3 methylation does not appear to affect ribosome function once the ribosome is assembled [Lhoest81].

L3 interacts with 23S rRNA [Uchiumi99]; this interaction appears to be cooperative with L6 [Uchiumi99].

An L3 mutant strain is resistant to the antibiotics tiamulin (a peptidyl transferase inhibitor) and pleuromutilin, but not valnemulin [Bosling03, Long06]. An amber mutation in rplC exerts a polar effect on the genes distal to the rplC gene in the S10 operon [Cabezon80].

Essentiality data for rplC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L4

Synonyms: EryA, RplD

Gene: rplD Accession Numbers: EG10867 (EcoCyc), b3319, ECK3306

Locations: cytosol, ribosome

Sequence Length: 201 AAs

Molecular Weight: 22.086 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0017148 - negative regulation of translation Inferred from experiment [Yates80a]
GO:0060702 - negative regulation of endoribonuclease activity Inferred from experiment [Singh09a]
GO:0006351 - transcription, DNA-templated Inferred by computational analysis [UniProtGOA11a]
GO:0006353 - DNA-templated transcription, termination Inferred by computational analysis [UniProtGOA11a]
GO:0006355 - regulation of transcription, DNA-templated Inferred by computational analysis [UniProtGOA11a]
GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a, Gaudet10]
GO:0006417 - regulation of translation Inferred by computational analysis [UniProtGOA11a]
GO:0046677 - response to antibiotic Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Singh09a]
GO:0030371 - translation repressor activity Inferred from experiment [Yates80a]
GO:0060698 - endoribonuclease inhibitor activity Inferred from experiment [Singh09a]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a, Gaudet10]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a, Gaudet10]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation
regulation genetic unit regulated operon
regulation type of regulation posttranscriptional translation attenuation and efficiency
regulation type of regulation transcriptional level

Unification Links: DIP:DIP-35791N , DisProt:DP00600 , EcoliWiki:b3319 , Mint:MINT-1219709 , ModBase:P60723 , PR:PRO_000023812 , Pride:P60723 , Protein Model Portal:P60723 , RefSeq:NP_417778 , SMR:P60723 , String:511145.b3319 , UniProt:P60723

Relationship Links: InterPro:IN-FAMILY:IPR002136 , InterPro:IN-FAMILY:IPR013005 , InterPro:IN-FAMILY:IPR023574 , Panther:IN-FAMILY:PTHR10746 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00573

Summary:
The L4 protein is a component of the 50S subunit of the ribosome and also regulates the expression of S10 operon at both the transcriptional and posttranscriptional level. The functions of L4 in ribosome assembly, attenuation, and translational regulation of the operon are separable [Freedman87, Li96e].

Addition of L4 to an in vitro protein synthesis reaction inhibits the synthesis of the promoter-proximal proteins in the S10 operon, suggesting that L4 may be an inhibitor of translation [Yates80a]. In vivo, overproduction of L4 was found to reduce the synthesis of S10 operon mRNA [Zengel80]. The steady-state growth rate-dependent control of the S10 operon expression requires additional factors [Lindahl90].

L4 stimulates premature termination (transcription attenuation) at a NusA-dependent terminator site 30 bases upstream of the first structural gene of the S10 operon, and termination requires the function of NusA [Lindahl83, Zengel90]. The attenuator hairpin region is sufficient for NusA-dependent pausing, and a second hairpin region immediately upstream of the attenuator hairpin is necessary for L4 to prolong the pause [Zengel92, Sha95, Zengel96]. Structural and sequence requirements for L4-mediated transcription termination within the S10 leader region have been determined [Zengel02]; the first 150 bases of the S10 leader region are sufficient for L4-mediated attenuation control [Zengel90a], and a 64-nucleotide sequence is required for L4 interaction with the S10 leader mRNA [Stelzl03]. Binding of L4 to the leader region induces structural changes in the mRNA [Stelzl03]. A region of 110 bases within domain I of 23S rRNA competes with paused transcription complex for binding of L4 [Zengel91, Zengel93].

L4 interacts with the 5' segment of 23S rRNA [Spierer75, Gulle88, Maly80, Urlaub95, Thiede98]. The L4 and L24 binding sites in 23S rRNA localize to a small fragment [Stelzl00] and may be a key element for rRNA folding in the early assembly pathway for the ribosome [Stelzl01]. The L4 binding region within domain I of 23S rRNA has three-dimensional structural similarity to its binding region on the S10 operon leader mRNA where it inhibits its own translation [Ostergaard98, Stelzl03].

L4 is a component of the binding site for erythromycin on the ribosome [Arevalo88]. An L4 K63E mutant is resistant to erythromycin, has a cold-sensitive growth defect, and shows a defect in 50S subunit assembly [Apirion67, Wittmann73, Chittum94]. The mutation reduces the rate of erythromycin association as well as equilibrium binding [Lovmar09]. Additional L4 mutants that confer erythromycin resistance have been isolated; all map to the extended loop region of L4 [Zaman07]. A large number of additional alleles was isolated by recombineering [Diner09]. L4, L5, and L21 bind to erythromycin cooperatively [Pye90]. The extended loop region of L4 (amino acids 40-88) contributes to the lining of the peptide exit tunnel in the ribosome and is contacted by the growing peptide chain [Houben05]. While deletions of this region of L4 do not appear to affect function of L4 [Zengel03], the K63E point mutation that results in erythromycin resistance alters the decoding accuracy of the ribosome [OConnor04]. Various mutations in L4 affect peptide-induced pausing of translation [Lawrence08a].

L4 directly interacts with the C-terminal domain of RNase E and inhibits its activity. A number of mRNAs are stabilized by ectopic expression of L4 [Singh09a].

Citations: [Gagnon10, Dunkle10, Kostopoulou12, Fu13]

Essentiality data for rplD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L5

Synonyms: RplE

Gene: rplE Accession Numbers: EG10868 (EcoCyc), b3308, ECK3295

Locations: cytosol, ribosome

Sequence Length: 179 AAs

Molecular Weight: 20.302 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0000027 - ribosomal large subunit assembly Inferred from experiment [Korepanov12]
GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0008097 - 5S rRNA binding Inferred from experiment [Spierer78]
GO:0000049 - tRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35914N , EcoliWiki:b3308 , Mint:MINT-1238892 , PR:PRO_000023813 , Pride:P62399 , Protein Model Portal:P62399 , RefSeq:NP_417767 , SMR:P62399 , String:511145.b3308 , UniProt:P62399

Relationship Links: InterPro:IN-FAMILY:IPR002132 , InterPro:IN-FAMILY:IPR020929 , InterPro:IN-FAMILY:IPR020930 , InterPro:IN-FAMILY:IPR022803 , Panther:IN-FAMILY:PTHR11994 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5S , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00281 , Pfam:IN-FAMILY:PF00673 , Prosite:IN-FAMILY:PS00358

Summary:
The L5 protein is a component of the 50S subunit of the ribosome. The crystal structure of the ribosome [Schuwirth05], cryo-EM reconstructions [Gao03a], and crosslinking experiments [Lambert81] show that the L5 protein contacts the S13 protein of the small subunit of the ribosome, forming the only protein-protein bridge between the subunits. During the ratchet-like motion of the ribosome, L5 and S13 reorganize in different constellations [Shasmal10]. L5, L15 and L18 are required for 5S RNA incorporation into the 50S subunit of the ribosome [Rohl82], and L5 was shown to be required for the assembly of the central protuberance of the 50S subunit [Korepanov12].

L5 binds to 5S rRNA [Branlant76, ChenSchmeisser77, Zimmermann78, Spierer78, Spierer78a, Pieler82, Huber84]. The association of L5 with 5S rRNA is cooperatively stimulated by L18 [Spierer78], and the binding regions of the 5S rRNA-L5-L18 complex were mapped [Ostergaard98]. Both L5 and L18 are essential for viability [Korepanov07]. A crystal structure of the Thermus thermophilus L5 in complex with a fragment of 5S RNA has been solved [Perederina02]. L5 also crosslinks to IF-3 [Chaires82] and uncharged tRNA in the P site of the ribosome [Abdurashidova90, Podkowinski91, Osswald95]. Molecular dynamics simulations suggest that L5 facilitates tRNA translocation [Bock13].

L5 is altered in a thiopeptin-resistant mutant [Liou75]. L4, L5, and L21 bind to erythromycin cooperatively [Pye90]. Inhibition of the EF-G-ribosome complex by thiostrepton involves destabilization of 5S RNA-protein (L5 and L18) interactions [Hanson03].

Expression of L5 is regulated at the translational level by S8 [Yates80, Olins81a, Mattheakis88, Cerretti88, Merianos04].

Overexpression of rplE suppresses the growth defect of a ΔrsgA mutant [Campbell08].

Citations: [Chang74, Chang75a, Sander75, Kenny75, Bernabeu76, Chen76, Morrison77, Dabbs77, Isono77, Jaskunas77, Jaskunas77a, Branlant77, Fox78, Spierer79, Garrett79, Larrinua79, Newberry80, Shen80, Maimets81, Metspalu82, Cerretti83, Maly83, Tewari83, Suryanarayana83, Traut83, Andrieux84, Siegrist84, Siegrist85, Yusupov86, Goringer86, Kakegawa86, Kashiwagi87, Herold87, Nag87, Lotti89, Redl89, RandolphAnderso89, Dontsova90, Osswald90, Abdurashidova91, Herfurth95, Traut95, Shpanchenko96, Dey98, Agrawal04, Soung09, Meng12]

Essentiality data for rplE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 4]
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L6

Synonyms: RplF

Gene: rplF Accession Numbers: EG10869 (EcoCyc), b3305, ECK3292

Locations: cytosol, ribosome

Sequence Length: 177 AAs

Molecular Weight: 18.904 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
GO:0046677 - response to antibiotic Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35860N , EcoliWiki:b3305 , Mint:MINT-1244940 , PR:PRO_000023814 , Pride:P0AG55 , Protein Model Portal:P0AG55 , RefSeq:NP_417764 , SMR:P0AG55 , String:511145.b3305 , Swiss-Model:P0AG55 , UniProt:P0AG55

Relationship Links: InterPro:IN-FAMILY:IPR000702 , InterPro:IN-FAMILY:IPR002358 , InterPro:IN-FAMILY:IPR019906 , InterPro:IN-FAMILY:IPR020040 , Panther:IN-FAMILY:PTHR11655 , PDB:Structure:1EG0 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:487D , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00347 , Prints:IN-FAMILY:PR00059 , Prosite:IN-FAMILY:PS00525

Summary:
The L6 protein is a component of the 50S subunit of the ribosome.

L6 interacts with 23S rRNA [Urlaub95, Osswald90, Uchiumi99]. Interaction appears to be cooperative with L3 [Uchiumi99]. L6 crosslinks to the stem-loop structure in domain V of 23S rRNA [Wower81], but assembles to domain VI [Leffers88]. The L6 binding site within domain VI has been identified [Stelzl00].

L6 is altered in a gentamicin-resistant mutant [Buckel77]. Ribosomes of gentamicin-resistant L6 mutants have altered misreading properties; the L6 alteration is thought to change a parameter of the ribosome function involved in codon recognition [Kuhberger79]. L6 also participates in the binding of dibekacin to ribosomes [Akiyama81].

Mutations in L6 cause a cold-sensitive growth defect as well as defective assembly and maturation of the 30S and 50S subunits of the ribosome at low temperature [Bosl81].

Essentiality data for rplF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal protein complex L8

Summary:
The ribosomal proteins L10 and L7/L12 form a complex of two L7/L12 dimers and one L10 monomer; the complex can be isolated both in solution and from intact ribosomes and was previously identified as L8 [Pettersson76, Chu76, Osterberg77, Gudkov78]. The conformation of the L8 complex and changes in L7/L12 dimer conformation upon binding to the ribosome or L10 has been studied [Makarov93, Hamman96, Bocharov98].

The binding site within 23S rRNA of the L8 complex has been determined [Beauclerk84, Rosendahl93].


Subunit of 50S ribosomal protein complex L8: 50S ribosomal subunit protein L10

Synonyms: RplJ

Gene: rplJ Accession Numbers: EG10871 (EcoCyc), b3985, ECK3976

Locations: cytosol, ribosome

Sequence Length: 165 AAs

Molecular Weight: 17.712 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
GO:0006417 - regulation of translation Inferred by computational analysis [UniProtGOA11a]
GO:0042254 - ribosome biogenesis Inferred by computational analysis [GOA01a]
Molecular Function: GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0070180 - large ribosomal subunit rRNA binding Inferred by computational analysis [GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07, LopezCampistrou05]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation
regulation type of regulation posttranscriptional translation attenuation and efficiency

Unification Links: DIP:DIP-35816N , EcoliWiki:b3985 , Mint:MINT-1264502 , PR:PRO_000023816 , Pride:P0A7J3 , Protein Model Portal:P0A7J3 , RefSeq:NP_418412 , SMR:P0A7J3 , String:511145.b3985 , UniProt:P0A7J3

Relationship Links: InterPro:IN-FAMILY:IPR001790 , InterPro:IN-FAMILY:IPR002363 , InterPro:IN-FAMILY:IPR022973 , Panther:IN-FAMILY:PTHR11560:SF8 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J37 , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ5 , PDB:Structure:4KJ9 , Pfam:IN-FAMILY:PF00466 , Prosite:IN-FAMILY:PS01109

Summary:
The L10 protein is a component of the 50S subunit of the ribosome and also regulates the expression of the L10 (β) operon at the posttranscriptional level.

L10 forms a complex with L7/L12; this complex was originally identified as the L8 subunit [Pettersson76, Chu76, Osterberg77, Gudkov78]. L10 and L7/L12 bind to the 23S rRNA early during assembly of the 50S subunit [deNarvaez79]. Binding of L10 to 23S rRNA can be separated from binding to L7/L12 [Pettersson79]; two binding sites in the C terminus of L10 are required for the binding of two L7/L12 dimers, but not for assembly of L10 into the ribosome [Griaznova00].

Synthesis of L10 and L7/L12 is regulated at the level of translation initiation [Little81a, Robakis81]. Expression of L12 is closely linked to expression of L10 [Hui82], and a region within the leader sequence of the L10 operon mRNA regulates the translation efficiency of L10 and L7/L12 [Hui82, Fiil80]. The L10 protein acts at a single site in the leader mRNA [Yates81a]. It has been shown that the region within the leader sequence that is essential for both translational feedback regulation and efficient translation lies between 70 and195 bases upstream of the rplJ translation start [Friesen83], and that secondary structure within that region is required for feedback regulation [Christensen84, Climie87, Climie88]. A complex containing L10 and L12 can bind directly to the leader sequence of the L10 operon mRNA and prevent translation [Johnsen82, Christensen84, Climie88], and added 23S rRNA prevents binding of L10/L12 to the mRNA [Johnsen82]. There is sequence similarity between 23S rRNA and the L10 leader region, and the L10/L12 binding site includes part of the homologous sequences [Johnsen82].

The abundance of L10 is also regulated at the post-translational level. L10 alone is subject to rapid proteolytic decay (half life of 1.5 minutes), but is stable if it is in a complex with L7/L12 [Petersen90a].

Essentiality data for rplJ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal protein complex L8: 50S ribosomal subunit protein L7/L12 dimer

Gene: rplL Accession Numbers: EG10873 (EcoCyc), b3986, ECK3977

Locations: cytosol, ribosome

Subunit composition of 50S ribosomal subunit protein L7/L12 dimer = [RplL]2
         50S ribosomal subunit protein L12 = RplL

Map Position: [4,178,583 -> 4,178,948] (90.06 centisomes, 324°)
Length: 366 bp / 121 aa

Molecular Weight of Polypeptide: 12.295 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a, WittmannLiebold73]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-36009N , EcoliWiki:b3986 , Mint:MINT-1277405 , PR:PRO_000023818 , Pride:P0A7K2 , Protein Model Portal:P0A7K2 , RefSeq:NP_418413 , SMR:P0A7K2 , String:511145.b3986 , UniProt:P0A7K2

Relationship Links: InterPro:IN-FAMILY:IPR000206 , InterPro:IN-FAMILY:IPR008932 , InterPro:IN-FAMILY:IPR013823 , InterPro:IN-FAMILY:IPR014719 , Panther:IN-FAMILY:PTHR11809 , PDB:Structure:1CTF , PDB:Structure:1RQS , PDB:Structure:1RQT , PDB:Structure:1RQU , PDB:Structure:1RQV , PDB:Structure:2BCW , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2XTG , PDB:Structure:2XUX , PDB:Structure:3J5O , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4KIX , Pfam:IN-FAMILY:PF00542 , ProDom:IN-FAMILY:PD001326

Reactions known to consume the compound:

Not in pathways:
50S ribosomal subunit protein L12 + acetyl-CoA → 50S ribosomal subunit protein L7 + coenzyme A

Summary:
50S ribosomal subunit protein L7 is the N-acetylated form of 50S ribosomal subunit protein L12 [Terhorst73].

Gene Citations: [Ralling84, Steward91, Barry80]

Essentiality data for rplL knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L9

Synonyms: RplI

Gene: rplI Accession Numbers: EG10870 (EcoCyc), b4203, ECK4199

Locations: cytosol, ribosome

Sequence Length: 149 AAs

Molecular Weight: 15.769 kD (from nucleotide sequence)

Molecular Weight: 15.7 kD (experimental) [Giri79]

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [Gaudet10, GOA06, GOA01a]
Molecular Function: GO:0070180 - large ribosomal subunit rRNA binding Inferred from experiment [Marquardt79, Adamski96]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0044822 - poly(A) RNA binding Inferred by computational analysis [Gaudet10]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35748N , EcoliWiki:b4203 , Mint:MINT-1228834 , ModBase:P0A7R1 , PR:PRO_000023815 , Pride:P0A7R1 , Protein Model Portal:P0A7R1 , RefSeq:NP_418624 , SMR:P0A7R1 , String:511145.b4203 , UniProt:P0A7R1

Relationship Links: InterPro:IN-FAMILY:IPR000244 , InterPro:IN-FAMILY:IPR009027 , InterPro:IN-FAMILY:IPR020069 , InterPro:IN-FAMILY:IPR020070 , InterPro:IN-FAMILY:IPR020594 , Panther:IN-FAMILY:PTHR21368 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:487D , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF01281 , Pfam:IN-FAMILY:PF03948 , Prosite:IN-FAMILY:PS00651

Summary:
The L9 protein is a component of the 50S subunit of the ribosome. L9 is universally conserved in eubacteria, but not in other domains of life; surprisingly, it is not essential. L9 appears to be involved in maintenance of the reading frame during translational pauses [Atkins09]. A model for the physiological function of L9 has been proposed [Naganathan15].

L9 is part of the first reconstitution intermediate of the 50S subunit [Herold87, Tumminia94]. L9 can be crosslinked to L2 and L28 [Kakegawa86, Redl89, Walleczek89] and is exposed on the ribosome surface [Agafonov97]. A solution structure determined by cryo-EM showed that the L9 protein consists of N-terminal and C-terminal domains connected by a long α helical domain that is wrapped around the L1 stalk [Matadeen99]. An atomic model of L9 within the ribosome was obtained in a cryo-EM structure, revealing contacts with the 30S subunit [Fischer15].

The binding region of L9 on domain V of 23S rRNA was mapped [Ostergaard98, Vladimirov00]. The N- and C-terminal domains of L9 interact with two separate sites in domain V of 23S rRNA [Adamski96, Lieberman00]. Crosslinking of tRNA in the A site of the ribosome to L9 depends on the state of the tRNA [Graifer89].

L9 may normally be involved to limit "ribosomal hopping" during translation of bacteriophage T4 gene 60 [Herbst94, Adamski96, Herr00, Herr01]. In a strain lacking rplI, frameshifting, stop-hopping [Herr01], as well as recoding at stalled ribosomes [Seidman11] is increased.

Strains that contain certain mutations in the essential ribosomal stability factor Der are dependent on L9 for survival. The N-terminal domain of L9 is both necessary and sufficient for complementation of the derT57I mutant allele [Naganathan13]. A second class of mutations causing synthetic phenotypes map to EF-P and enzymes responsible for its post-translational modification. L9 improves subunit maturation in der and efp mutant backgrounds [Naganathan15].

An rplI mutant with a temperature-sensitive growth defect has been isolated [Isono78, Isono78a]. An rplI deletion shows only a slight growth defect [Naganathan13].

Review: [Atkins09]

Citations: [Branlant76, Morrison77, Robertson77, Branlant77, Subramanian77, Kitakawa80, Kamp83, Moureau83, StofflerMeilick83, Traut83, Vladimirov85, Abdurashidova85, Schnier86, Osswald90, Nag91, Kuroda01, Sato01, Schuwirth05, Hwang06, Gordiyenko08, Dunkle11, AlMajdoub13]

Essentiality data for rplI knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 4]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L11

Synonyms: RelC, RplK

Gene: rplK Accession Numbers: EG10872 (EcoCyc), b3983, ECK3974

Locations: cytosol, ribosome

Sequence Length: 142 AAs

Molecular Weight: 14.875 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006415 - translational termination Inferred from experiment [Sato06]
GO:0015968 - stringent response Inferred from experiment [Jenvert07]
GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Arifuzzaman06, Butland05]
GO:0019843 - rRNA binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Schmidt81a]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0070180 - large ribosomal subunit rRNA binding Inferred by computational analysis [GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a, Dognin80a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35882N , EcoliWiki:b3983 , Mint:MINT-1232893 , ModBase:P0A7J7 , PR:PRO_000023817 , Pride:P0A7J7 , Protein Model Portal:P0A7J7 , RefSeq:NP_418410 , SMR:P0A7J7 , String:511145.b3983 , UniProt:P0A7J7

Relationship Links: InterPro:IN-FAMILY:IPR000911 , InterPro:IN-FAMILY:IPR006519 , InterPro:IN-FAMILY:IPR020783 , InterPro:IN-FAMILY:IPR020784 , InterPro:IN-FAMILY:IPR020785 , Panther:IN-FAMILY:PTHR11661 , PDB:Structure:1EG0 , PDB:Structure:1MJ1 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3DEG , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3EP2 , PDB:Structure:3EQ3 , PDB:Structure:3EQ4 , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0D , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:487D , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00298 , Pfam:IN-FAMILY:PF03946 , Prosite:IN-FAMILY:PS00359 , Smart:IN-FAMILY:SM00649

Reactions known to consume the compound:

Not in pathways:
a non-methylated ribosomal protein L11 + S-adenosyl-L-methionine → a methylated ribosomal protein L11 + S-adenosyl-L-homocysteine

Summary:
The L11 protein is a component of the 50S subunit of the ribosome.

L11 is posttranslationally modified by methylation [Chang75a]. The N-terminal alanine residue is methylated to N-trimethylalanine [Lederer77, Dognin80], and two lysine residues are methylated to Nε, Nε, Nε-trimethyllysine [Dognin80a, Jerez80, Dognin80, Arnold99]. Methylation of L11 does not appear to be essential for its function [Vanet94].

Ribosome core particles lacking L11 do not display EF-G-dependent GTPase activity [Schrier75]. L11 participates in joining the 30S initiation complex to the 50S subunit [Naaktgeboren76, Gotz89]. The N-terminal domain of L11 participates in the formation of the arc-like connection between EF-G and L7/L12 during tRNA translocation [Datta05].

L11 directly interacts with 23S rRNA [Littlechild77]. Its binding site has been identified [Schmidt81a] and is adjacent to the L8 complex binding site in 23S rRNA [Beauclerk84, Egebjerg90]. Binding of the L8 complex and L11 appears to be cooperative [Rosendahl93, Rosendahl95]. L11 recognizes and stabilizes the three-dimensional structure of its binding site in 23S rRNA [Ryan91, Blyn00, Bowen05, Maeder06]. A crystal structure of L11 bound to a 58 nucleotide fragment of 23S rRNA has been determined; the C-terminal domain of L11 binds RNA tightly, while the N-terminal domain makes only limited contacts with RNA [Wimberly99].

The L11 binding region of 23S rRNA appears to be important for translation termination [Van02a]. The N-terminal domain of L11 is critical for modulation of release factor binding [Tate83a, McCaughan84, Tate84, Tate86, Van03b]. Deletion of the amino terminus reduces the termination efficiency of RF1, but not RF2, thus increasing nonsense suppression at UAG codons, while changes in L11 reduce dissociation of RF2 from ribosome, causing a decrease in nonsense suppression at UGA codons [Bouakaz06]. Strains lacking L11 exhibit UAG stop codon suppression, defective growth, and high-temperature lethality; strains lacking only the N-terminal domain of L11 are only defective in UAG-dependent termination [Van03b]. However, later experiments show that L11 affects RF1 and RF2 activity similarly [Sato06].

L11 is required for binding of the thiazole antibiotic thiostrepton to the ribosome [Highland75a].

L11 plays a role in regulating the stringent response; an rplK (relC) mutant has a relaxed phenotype [Friesen74, Parker76]. Both a proline-rich helix in the N-terminal domain of L11 and the linker region between the N- and C-terminal domains are required for regulating the activity of (p)ppGpp synthetase I (RelA) [Yang01c, Jenvert07], although no direct interaction between the two proteins has been detected [Yang01c]. ppGpp synthesis by RelA requires both uncharged tRNA at the A site of the ribosome and the presence of L11 [Wendrich02]. The L11 N-terminal domain alone can activate RelA in the presence of ribosomes and uncharged tRNA [Jenvert07].

Essentiality data for rplK knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Yamamoto09]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L13

Synonyms: RplM

Gene: rplM Accession Numbers: EG10874 (EcoCyc), b3231, ECK3220

Locations: cytosol, ribosome

Sequence Length: 142 AAs

Molecular Weight: 16.019 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0008270 - zinc ion binding Inferred from experiment [Katayama02]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-47837N , EcoliWiki:b3231 , Mint:MINT-1269598 , ModBase:P0AA10 , PR:PRO_000023819 , Pride:P0AA10 , Protein Model Portal:P0AA10 , RefSeq:NP_417698 , SMR:P0AA10 , String:511145.b3231 , UniProt:P0AA10

Relationship Links: InterPro:IN-FAMILY:IPR005822 , InterPro:IN-FAMILY:IPR005823 , InterPro:IN-FAMILY:IPR023563 , InterPro:IN-FAMILY:IPR023564 , Panther:IN-FAMILY:PTHR11545 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IY9 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00572 , Prosite:IN-FAMILY:PS00783

Summary:
The L13 protein is an early assembly component of the 50S subunit of the ribosome. The RNA helicase SrmB is necessary for the assembly of L13 into the ribosome [Charollais03].

L13 interacts with 23S rRNA [Spierer75, Spierer76, Skold81, Osswald90, Tumminia94] and crosslinks to it in both free ribosomes and the initiation complex [Chistyakov89]. L13 is located within 21 Å of nucleotide C2475 of 23S rRNA, near the peptidyltransferase center [Muralikrishna95]. L13 binds to 5S rRNA [Kargel87] and can be crosslinked to L2 [Barritault75], L3 [Walleczek89], L20 [Barritault75, Redl89, Walleczek89] and L21 [Schonfeld87, Walleczek89a, Walleczek89]. L13 interacts with tRNA in the P site [Graifer89].

Ribosome modulation factor binds near L2, L13, and S13 [Yoshida02b]. A puromycin analog [Krassnigg78], a tobramycin analog [Tangy83], and a pactamycin analog [Tejedor85] can be crosslinked to L13.

L13 has RNA chaperone-like activity in an in vitro trans splicing assay [Semrad04] and binds zinc [Katayama02].

Essentiality data for rplM knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L14

Synonyms: RplN

Gene: rplN Accession Numbers: EG10875 (EcoCyc), b3310, ECK3297

Locations: cytosol, ribosome

Sequence Length: 123 AAs

Molecular Weight: 13.541 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Hauser12]
GO:0070180 - large ribosomal subunit rRNA binding Inferred from experiment [Urlaub95]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a, Kaltschmidt70]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0015934 - large ribosomal subunit Inferred by computational analysis [GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35798N , EcoliWiki:b3310 , Mint:MINT-1304553 , ModBase:P0ADY3 , PR:PRO_000023820 , Pride:P0ADY3 , Protein Model Portal:P0ADY3 , RefSeq:NP_417769 , SMR:P0ADY3 , String:511145.b3310 , Swiss-Model:P0ADY3 , UniProt:P0ADY3

Relationship Links: InterPro:IN-FAMILY:IPR000218 , InterPro:IN-FAMILY:IPR005745 , InterPro:IN-FAMILY:IPR019972 , InterPro:IN-FAMILY:IPR023571 , Panther:IN-FAMILY:PTHR11761 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IY9 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3IZZ , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:487D , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00238 , Prosite:IN-FAMILY:PS00049

Summary:
The L14 protein is a component of the 50S subunit of the ribosome.

L14 crosslinks to 23S rRNA [Osswald90, Urlaub95]. In the cryo-EM reconstruction of the ribosome, L14 was modelled to be located at the 30S-50S subunit interface, at bridges B5 and B8 [Gao03a]. In all-atom molecular dynamics simulations of the ribosome, a structural gate between helices 71 and 92 of 23S rRNA restricts tRNA motion and together with L14 acts as a steric filter for the cognate tRNA [Caulfield12].

L14 interacts directly with ribosomal silencing factor. Amino acid residues in L14 that are essential for this interaction have been identified by mutagenesis [Hauser12].

Based on amino-terminal sequencing of the purified protein, L14 may be identical to Rep helicase stimulatory protein (RHSP) [Smith89b, Yancey91]. RHSP forms aggregates on DNA and interacts with rRNA [Yancey91].

Retroregulation of L14 expression by mRNA processing and decay has been studied in E. coli B/r [Liang99].

Essentiality data for rplN knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L15

Synonyms: RplO

Gene: rplO Accession Numbers: EG10876 (EcoCyc), b3301, ECK3288

Locations: ribosome

Sequence Length: 144 AAs

Molecular Weight: 14.98 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Butland05]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a, Gaudet10]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0015934 - large ribosomal subunit Inferred by computational analysis [GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-10752N , EcoliWiki:b3301 , Mint:MINT-1260355 , ModBase:P02413 , PR:PRO_000023821 , Pride:P02413 , Protein Model Portal:P02413 , RefSeq:NP_417760 , SMR:P02413 , String:511145.b3301 , UniProt:P02413

Relationship Links: InterPro:IN-FAMILY:IPR001196 , InterPro:IN-FAMILY:IPR005749 , InterPro:IN-FAMILY:IPR021131 , Panther:IN-FAMILY:PTHR12934 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IY9 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4UY8 , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00828 , Prosite:IN-FAMILY:PS00475

Summary:
The L15 protein is a component of the 50S subunit of the ribosome.

L15 is a late assembly protein [Franceschi90] that appears to be required for 5S rRNA incorporation [Rohl82]. L15 interacts with domain II of 23S rRNA in a partially assembled ribosomal particle [Littlechild77, Lieberman98]. L15 appears to be dispensible for protein synthesis and cell growth [Ito84], and ribosomes lacking L15 are translationally active [Franceschi90].

L15 is a component of the binding site for erythromycin on the ribosome [Arevalo88].

L15 has RNA chaperone-like activity in an in vitro trans splicing assay [Semrad04].

Essentiality data for rplO knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L16

Synonyms: RplP

Gene: rplP Accession Numbers: EG10877 (EcoCyc), b3313, ECK3300

Locations: cytosol, ribosome

Sequence Length: 136 AAs

Molecular Weight: 15.281 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0000049 - tRNA binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Remme83]
GO:0019843 - rRNA binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Stoffler71]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a, Gaudet10]
Cellular Component: GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35976N , EcoliWiki:b3313 , Mint:MINT-1302401 , ModBase:P0ADY7 , PR:PRO_000023822 , Pride:P0ADY7 , Protein Model Portal:P0ADY7 , RefSeq:NP_417772 , SMR:P0ADY7 , String:511145.b3313 , UniProt:P0ADY7

Relationship Links: InterPro:IN-FAMILY:IPR000114 , InterPro:IN-FAMILY:IPR016180 , InterPro:IN-FAMILY:IPR020798 , Panther:IN-FAMILY:PTHR12220 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00252 , Prints:IN-FAMILY:PR00060 , Prosite:IN-FAMILY:PS00586 , Prosite:IN-FAMILY:PS00701

Summary:
The L16 protein is a late assembly component of the 50S subunit of the ribosome; ribosomes lacking L16 are translationally active [Franceschi90]. L2 is required for assembly of L16 into the 50S subunit [Romero90].

L16 interacts with tRNA [Remme83, Maimets84, Sumpter90] and can be crosslinked to aminoacylated tRNA in the A and P site [Abdurashidova79, Osswald95]. Conserved residues within L16 were shown to be involved in the translocation of tRNA from the A to the P site [Bock13]. L16 is located within 21 Å of nucleotide C2475 of 23S rRNA, near the peptidyltransferase center [Muralikrishna95]. L16 and a histidine residue within the N-terminal domain of L16 may be important for the correct conformation of the peptidyltransferase center [Baxter80, Baxter87, Tate87]. L16 is important for release factor 2-dependent peptidyl-tRNA hydrolysis [Tate83]. The antibiotics chloramphenicol [Nierhaus73, Pongs73] and virginiamycin S [deBethune78] interact with L16 within the ribosome.

L16 is one of six ribosomal proteins that is completely lost from ribosomes in post-stationary cells [Ramagopal84].

The N-terminal methionine of L16 appears to be methylated [Brosius76, Chen77], and additional posttranslational modifications of the protein are present [Arnold99, Nesterchuk11]. These include phosphorylation [Macek08, Soung09] as well as hydroxylation of the Arg81 residue by ribosomal protein-arginine oxygenase [Ge12].

L16 has RNA chaperone-like activity in an in vitro trans-splicing assay [Semrad04] as well as protein chaperone activity [Kovacs09].

Citations: [Czernilofsky74, Maassen74, Kazemie75, Kazemie76, Dzionara77, Pichon77, Morrison77, Hernandez77, Bernabeu77, Jaskunas77, Teraoka78, Bernabeu78, Baxter78, Spierer79, Adachi79, Marquardt79, Skold81, Guerin81, Schulze82, Moureau83, Maimets, Ganoza85, Yusupov86, Kakegawa86, Walleczek89a, Chistyakov89, Redl89, Walleczek89, RandolphAnderso89, Wower89, Vladimirov90, Sumpter91, Nag91a, Agafonov97, Vladimirov00, Lancaster08]

Essentiality data for rplP knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 4]
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L17

Synonyms: RplQ

Gene: rplQ Accession Numbers: EG10878 (EcoCyc), b3294, ECK3281

Locations: cytosol, ribosome

Sequence Length: 127 AAs

Molecular Weight: 14.365 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a, Gaudet10]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35801N , EcoliWiki:b3294 , Mint:MINT-1251899 , ModBase:P0AG44 , PR:PRO_000023823 , Pride:P0AG44 , Protein Model Portal:P0AG44 , RefSeq:NP_417753 , SMR:P0AG44 , String:511145.b3294 , Swiss-Model:P0AG44 , UniProt:P0AG44

Relationship Links: InterPro:IN-FAMILY:IPR000456 , Panther:IN-FAMILY:PTHR14413 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF01196 , Prosite:IN-FAMILY:PS01167

Summary:
The L17 protein is a component of the 50S subunit of the ribosome.

L17 interacts directly with tRNA [Metspalu81] and can be crosslinked to 23S rRNA [Osswald90]. L17 can also be crosslinked to the spiramycin derivative dihydrospiramycin and may thus be located near the peptidyl transferase center [Bischof95].

Essentiality data for rplQ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L18

Synonyms: RplR

Gene: rplR Accession Numbers: EG10879 (EcoCyc), b3304, ECK3291

Locations: cytosol, ribosome

Sequence Length: 117 AAs

Molecular Weight: 12.77 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-47908N , EcoliWiki:b3304 , Mint:MINT-1293631 , ModBase:P0C018 , PR:PRO_000023824 , Pride:P0C018 , Protein Model Portal:P0C018 , RefSeq:NP_417763 , SMR:P0C018 , String:511145.b3304 , UniProt:P0C018

Relationship Links: InterPro:IN-FAMILY:IPR004389 , InterPro:IN-FAMILY:IPR005484 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00861

Summary:
The L18 protein is a component of the 50S subunit of the ribosome and is required for incorporation of 5S rRNA into the ribosome [Rohl82].

L18 interacts with both 23S rRNA [Osswald90] and 5S rRNA [Huber84, Newberry78, Spierer78, Fanning81]. L18 together with L5 can associate into a quaternary complex with 5S and 23S rRNAs [Spierer79]. The binding determinants of the 5S rRNA-L5-L18-L25 complex have been mapped [Peattie81, Newberry80, Speek82, Brewer83, Christiansen85, Goringer86, Gewirth88, Egebjerg89, Zhang89c, Ciesiolka92, Shpanchenko96, Ostergaard98]. Iodination at a tyrosine residue abolishes binding of L18 to 5S rRNA [Fanning81a].

L18 has RNA chaperone-like activity in an in vitro trans splicing assay [Semrad04].

L18 is photoaffinity labeled by puromycin, an analog of the 3' end of aminoacylated tRNA [Bischof94]. L18 can also be crosslinked to the spiramycin derivative dihydrospiramycin and may thus be located near the peptidyl transferase center [Bischof95].

Essentiality data for rplR knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L19

Synonyms: RplS

Gene: rplS Accession Numbers: EG10880 (EcoCyc), b2606, ECK2603

Locations: cytosol, ribosome

Sequence Length: 115 AAs

Molecular Weight: 13.133 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35793N , EcoliWiki:b2606 , Mint:MINT-1245288 , PR:PRO_000023825 , Pride:P0A7K6 , Protein Model Portal:P0A7K6 , RefSeq:NP_417097 , SMR:P0A7K6 , String:511145.b2606 , UniProt:P0A7K6

Relationship Links: InterPro:IN-FAMILY:IPR001857 , InterPro:IN-FAMILY:IPR008991 , InterPro:IN-FAMILY:IPR018257 , Panther:IN-FAMILY:PTHR15680 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF01245 , Prints:IN-FAMILY:PR00061 , Prosite:IN-FAMILY:PS01015

Summary:
The L19 protein is a component of the 50S subunit of the ribosome. Depending on the method used, L19 does [Persson95] or does not [Stoffler84] appear to be essential for viability.

L19 can be crosslinked to 23S rRNA [Bernabeu78, Skold81, Giocanti80, Osswald90], mRNA [Gimautdinova81], and ribosomal proteins S9 and L18 [Scheibe86], L3 [Walleczek89a, Walleczek89], L14 [Walleczek89a, Walleczek89], L6 [Redl89], and L25 [Walleczek89a, Redl89, Walleczek89].

L19 has RNA chaperone-like activity in an in vitro trans splicing assay [Semrad04].

L19 is photoaffinity labeled by dyhydrorosaramyicin [Siegrist85].

The phenotypes of mutants lacking L19 vary; a slow growth phenotype [Stoffler84] and accumulation of ribosome precursor particles during exponential growth and unbalanced synthesis of RNA [Wild88] have been reported.

Expression of proteins encoded by the rpsP-rimM-trmD-rplS operon does not appear to be regulated at the transcriptional level [Wikstrom88]. The lower expression levels of rimM and trmD appear to be achieved by regulating their level of translation [Wikstrom92].

Essentiality data for rplS knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L20

Synonyms: PdzA, RplT

Gene: rplT Accession Numbers: EG10881 (EcoCyc), b1716, ECK1714

Locations: cytosol, ribosome

Sequence Length: 118 AAs

Molecular Weight: 13.497 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0000027 - ribosomal large subunit assembly Inferred from experiment Inferred by computational analysis [GOA06, Nowotny80]
GO:0006412 - translation Inferred from experiment Inferred by computational analysis [GOA01a]
GO:0017148 - negative regulation of translation Inferred from experiment [Lesage92]
Molecular Function: GO:0000900 - translation repressor activity, nucleic acid binding Inferred from experiment [Lesage92]
GO:0003735 - structural constituent of ribosome Inferred from experiment Inferred by computational analysis [GOA01a, Nowotny80]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a, Olsson96]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation
regulation type of regulation posttranscriptional

Unification Links: DIP:DIP-47941N , EcoliWiki:b1716 , Mint:MINT-1321645 , ModBase:P0A7L3 , PR:PRO_000023826 , Pride:P0A7L3 , Protein Model Portal:P0A7L3 , RefSeq:NP_416231 , SMR:P0A7L3 , String:511145.b1716 , UniProt:P0A7L3

Relationship Links: InterPro:IN-FAMILY:IPR005813 , Panther:IN-FAMILY:PTHR10986 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00453 , Prints:IN-FAMILY:PR00062 , Prosite:IN-FAMILY:PS00937

Summary:
The L20 protein is a component of the 50S subunit of the ribosome and autoregulates its own expression and that of L35 at the posttranscriptional level. The N-terminal domain of L20 is required for ribosome assembly, and the C-terminal domain is required for its regulatory function [Guillier05].

L20 binds to the 5' terminal third of 23S rRNA [Spierer75, Marquardt79, Tumminia94] and is required for early assembly of the 4.3c core particle, but is not required for function of the mature 50S ribosomal subunit [Nowotny80]. L20 can replace L24 for the initiation of assembly of the 50S subunit at permissive temperatures in an L24 mutant [Franceschi88]. L20 can be crosslinked to L13 and L21 [Walleczek89a, Redl89, Walleczek89].

L20 might be required for maintaining the 50S subunit in the correct conformation for binding of aminoacyl-tRNAs [Kazemie76]. Decreasing the amount of L20 in the cell leads to a decrease in growth rate and the appearance of an aberrant ribosome peak at 41-43S [Olsson96].

Expression of rplT is autoregulated at the posttranscriptional level. L20 acts in trans at two sites, one located within infC [Lesage90] and a second located close to the translation start site of rpmI [Chiaruttini96]. The two sites may form a long-range RNA pseudoknot structure [Chiaruttini96]. Of the two L20 binding sites within the regulatory region of the mRNA, only one shows direct similarity to the L20 binding site within 23S rRNA [Guillier02]. However, both sites share secondary structure similarity with the L20 binding site in rRNA [Guillier05a]. The two binding sites interact, and only one molecule of L20 binds to the L20 mRNA [Allemand07]. Structural analysis of RNA binding by the L20 C-terminal domain by NMR show that binding of L20 to rRNA and mRNA is similar [Raibaud03]. Decreased translation of infC leads to increased L20-mediated repression of L35 expression [Chiaruttini97].

L20 directly represses the expression of rpmI, but only indirectly that of rplT, via translational coupling with rpmI [Lesage92]. A secondary structure forms between the translation initiation site of rplT and a site internal to rpmI [Lesage92]; this structure forms in vivo and is required for translational coupling [Chiaruttini96a]. It is thought that the secondary structure can form when rpmI is not translated, and it can be shown that it blocks binding of the ribosome to the ribosome binding site of rplT [Chiaruttini96a].

Unlike the regulation of the ribosomal alpha operon and of rpsO, translational autoregulation by L20 appears to be based on competition with the ribosome for binding to its mRNA [HaentjensSitri08].

Essentiality data for rplT knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L21

Synonyms: RplU

Gene: rplU Accession Numbers: EG50001 (EcoCyc), b3186, ECK3175

Locations: cytosol, ribosome

Sequence Length: 103 AAs

Molecular Weight: 11.564 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Zhang07]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-47852N , EcoliWiki:b3186 , Mint:MINT-1280768 , ModBase:P0AG48 , PR:PRO_000023827 , Pride:P0AG48 , Protein Model Portal:P0AG48 , RefSeq:NP_417653 , SMR:P0AG48 , String:511145.b3186 , UniProt:P0AG48

Relationship Links: InterPro:IN-FAMILY:IPR001787 , InterPro:IN-FAMILY:IPR018258 , InterPro:IN-FAMILY:IPR028909 , Panther:IN-FAMILY:PTHR21349 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00829 , Prosite:IN-FAMILY:PS01169

Summary:
The L21 protein is a component of the 50S subunit of the ribosome.

L21 interacts with 23S rRNA [Thiede98, Yamada80a].

L4, L5, and L21 bind to erythromycin cooperatively [Pye90].

Essentiality data for rplU knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L22

Synonyms: EryB, RplV

Gene: rplV Accession Numbers: EG10882 (EcoCyc), b3315, ECK3302

Locations: cytosol, ribosome

Sequence Length: 110 AAs

Molecular Weight: 12.226 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
GO:0046677 - response to antibiotic Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Butland05]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0015934 - large ribosomal subunit Inferred by computational analysis [GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35983N , EcoliWiki:b3315 , Mint:MINT-1253134 , ModBase:P61175 , PR:PRO_000023828 , Pride:P61175 , Protein Model Portal:P61175 , RefSeq:NP_417774 , SMR:P61175 , String:511145.b3315 , UniProt:P61175

Relationship Links: InterPro:IN-FAMILY:IPR001063 , InterPro:IN-FAMILY:IPR005727 , InterPro:IN-FAMILY:IPR018260 , Panther:IN-FAMILY:PTHR13501 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00237 , Prosite:IN-FAMILY:PS00464

Summary:
The L22 protein is a component of the 50S subunit of the ribosome; it can interact with nascent translation products in the exit tunnel [Nakatogawa02] and provides one of the earliest contacts with a nascent peptide chain past the peptidyl transferase center [Houben05].

L22 is an early assembly protein and binds to the 5' end of 23S rRNA [Tumminia94, Marquardt79]; it can be crosslinked to 23S rRNA in both free ribosomes and the initiation complex [Chistyakov89]. L22 that lacks part of its extended loop that lines the peptide exit tunnel is functional in ribosome assembly [Zengel03]. L22 also crosslinks to L32 [Walleczek89a] and L18 [Redl89].

In addition to preventing elongation of the peptide chain, the antibiotic erythromycin inhibits the assembly of the 50S ribosomal subunit [Chittum95]. L22 is a component of the binding site for erythromycin on the ribosome [Arevalo88]. A 9 bp deletion in rplV, removing codons 82-84 of L22, leads to erythromycin resistance; the mutant phenotype is recessive [Chittum94]. Erythromycin-resistant L22 mutants show a perturbed conformation of 23S rRNA [Gregory99] and affect the topology of the nascent polypeptide exit tunnel [Gabashvili01].

Temperature-sensitive rplV mutants are defective in protein synthesis [BurnetteVick94, Champney80].

Essentiality data for rplV knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 4]
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L23

Synonyms: RplW

Gene: rplW Accession Numbers: EG10883 (EcoCyc), b3318, ECK3305

Locations: cytosol, ribosome

Sequence Length: 100 AAs

Molecular Weight: 11.199 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06]
GO:0000166 - nucleotide binding Inferred by computational analysis [GOA01a]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35972N , EcoliWiki:b3318 , Mint:MINT-1225825 , ModBase:P0ADZ0 , PR:PRO_000023829 , Pride:P0ADZ0 , Protein Model Portal:P0ADZ0 , RefSeq:NP_417777 , SMR:P0ADZ0 , String:511145.b3318 , Swiss-Model:P0ADZ0 , UniProt:P0ADZ0

Relationship Links: InterPro:IN-FAMILY:IPR001014 , InterPro:IN-FAMILY:IPR012677 , InterPro:IN-FAMILY:IPR012678 , InterPro:IN-FAMILY:IPR013025 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VRH , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IY9 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J45 , PDB:Structure:3J46 , PDB:Structure:3J4X , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00276 , Prosite:IN-FAMILY:PS00050

Summary:
The L23 protein is a component of the 50S subunit of the ribosome and provides a chaperone docking site that links protein biosynthesis with protein folding. L23 is essential for growth of E. coli [Kramer02].

L23 crosslinks to Trigger Factor (TF), a protein that interacts with nascent polypeptides on the ribosome, and is essential for the association of TF with the ribosome [Kramer02, Ullers03]. It also crosslinks to the Ffh component of the Signal Recognition Particle (SRP) [Gu03b, Ullers03]. Kd values for binding of TF and SRP to the ribosome under various conditions have been estimated, and TF and SRP are thought to have separate binding sites on L23 [Raine04]. L23 can also be crosslinked to a nascent peptide chain [Houben05].

L23 is an early assembly protein that interacts with 23S rRNA [Marquardt79, Osswald90, Egebjerg91, Chistyakov89, Tumminia94, Thiede98, Skold81, Vester84, Thiede98]. L23 crosslinks to tRNA in the A site [Graifer89]. L23 can also be crosslinked to L34 [Walleczek89a, Walleczek89] and L29 [Walleczek89].

L23 is photoaffinity labeled by puromycin, thus placing it within the A-site domain of the peptidyl transferase center [Cooperman75, Jaynes78, Weitzmann85]. Puromycin-crosslinked L23 interferes with tRNA binding, but 50S subunits containing it retain peptidyl transferase activity [Weitzmann90].

Reviews: [Albanese02, Ito05]

Essentiality data for rplW knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L24

Synonyms: RplX

Gene: rplX Accession Numbers: EG10884 (EcoCyc), b3309, ECK3296

Locations: cytosol, ribosome

Sequence Length: 104 AAs

Molecular Weight: 11.316 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-47846N , EcoliWiki:b3309 , Mint:MINT-1294921 , ModBase:P60624 , PR:PRO_000023830 , Pride:P60624 , Protein Model Portal:P60624 , RefSeq:NP_417768 , SMR:P60624 , String:511145.b3309 , UniProt:P60624

Relationship Links: InterPro:IN-FAMILY:IPR003256 , InterPro:IN-FAMILY:IPR005824 , InterPro:IN-FAMILY:IPR005825 , InterPro:IN-FAMILY:IPR008991 , InterPro:IN-FAMILY:IPR014722 , Panther:IN-FAMILY:PTHR12903 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2VRH , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J45 , PDB:Structure:3J46 , PDB:Structure:3J4X , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00467 , Prosite:IN-FAMILY:PS01108 , Smart:IN-FAMILY:SM00739

Summary:
The L24 protein is a component of the 50S subunit of the ribosome. L3 and L24 are the two proteins that initiate assembly of the 50S subunit; L24 is not thought to be involved in ribosomal function [Spillmann78, Nowotny82].

L24 binds directly to 23S rRNA [Tritton76, Branlant77a, Egebjerg87, Osswald90, Ostergaard98]; binding of L24 together with L4 to 23S rRNA leads to a change in tertiary structure of the RNA [Stelzl01].

A mutant lacking L24 is temperature sensitive and shows a very slow growth rate [Dabbs82, Nishi85, Nishi87]. The defect is in the assembly of 50S subunits [Herold86]. Suppressors of certain temperature sensitive rplX mutations map to 23S rRNA [Nishi86] or the Lon protease [Nishi88].

L20 can replace L24 for the initiation of assembly of the 50S subunit at permissive temperatures in an L24 mutant [Franceschi88].

Essentiality data for rplX knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L25

Synonyms: RplY

Gene: rplY Accession Numbers: EG10885 (EcoCyc), b2185, ECK2179

Locations: cytosol, ribosome

Sequence Length: 94 AAs

Molecular Weight: 10.693 kD (from nucleotide sequence)

Molecular Weight: 12.0 kD (experimental) [Giri79]

GO Terms:

Biological Process: GO:0006412 - translation Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Korepanov07]
GO:0017148 - negative regulation of translation Inferred from experiment [Aseev15]
Molecular Function: GO:0008097 - 5S rRNA binding Inferred from experiment Inferred by computational analysis [GOA01a, Spierer78]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35885N , EcoliWiki:b2185 , Mint:MINT-1261165 , ModBase:P68919 , PR:PRO_000023831 , Pride:P68919 , Protein Model Portal:P68919 , RefSeq:NP_416690 , SMR:P68919 , String:511145.b2185 , UniProt:P68919

Relationship Links: InterPro:IN-FAMILY:IPR011035 , InterPro:IN-FAMILY:IPR020055 , InterPro:IN-FAMILY:IPR020056 , InterPro:IN-FAMILY:IPR029751 , PDB:Structure:1B75 , PDB:Structure:1D6K , PDB:Structure:1DFU , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:487D , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF01386 , ProDom:IN-FAMILY:PD012503

Summary:
The L25 protein is a component of the 50S subunit of the ribosome and binds to 5S rRNA. L25 is not an essential protein [Korepanov07].

Binding of L25 to 5S rRNA has been studied in detail [Spierer78, Spierer78a, Douthwaite79, Osterberg79, Garrett79, Speek82, Huber84, Kime83, Kime84, Kime84a, Szymkowiak85, Goringer86, Leontis86, Leontis86a, Shpanchenko96]. Solution structures of L25 alone and in complex with a segment of 5S rRNA has been determined [Stoldt98, Wohnert99, Stoldt99], and a crystal structure of L25 bound to a loop E-containing fragment of 5S rRNA has been solved at 1.8 Å resolution [Lu00]. The interaction of L25 with 5S rRNA is not required for incorporation of L25 into the ribosome, although it is important for its retention [Anikaev14].

L25 can be crosslinked to 23 S rRNA in the initiation complex [Chistyakov89] and to ribosomal protein L19 [Walleczek89a, Redl89, Walleczek89].

A truncated form of L25 can be detected in 2-D gels [Wasinger98]. L25 is not posttranslationally modified [Arnold99].

Although rplY has a non-canonical ribosome binding site, the gene is translated with high efficiency. Conserved elements in the 5' UTR play a role in autogenous translation control [Aseev15].

An rplY deletion mutant is viable, but has a slower growth rate than wild type. Mutant ribosomes lack only L25 and are impaired in protein biosynthesis [Korepanov07].

Citations: [Fuenteun75, GauntKlopfer75, Sander75, Dovgas75, Ulbrich75, Bitar75, Gast76, Chu76a, Osterberg76, Branlant76, ChenSchmeisser77, Morrison77, Bear77, Gray73, Hernandez77, Branlant77, Fox78, Zimmermann78, Krassnigg78, Schnier79, Newberry80, Maimets81, Kime81, Guerin81, Metspalu82, Douthwaite82, Gimautdinova, Pieler82, Parker83, Silberklang83, Tumanova83, Tewari83, vandeVen83, Moore83, Tate83, AbdelMeguid83, Tumanova, Bausk85, Gimautdinova85, Gewirth87, Fox88, Lotti89, Dontsova90, Herfurth95, Willumeit01a, Reblova04, Chigradze08]

Essentiality data for rplY knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L27

Synonyms: Rpz, RpmA

Gene: rpmA Accession Numbers: EG50002 (EcoCyc), b3185, ECK3174

Locations: cytosol, ribosome

Sequence Length: 85 AAs

Molecular Weight: 9.124 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14]
GO:0000049 - tRNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-47933N , DisProt:DP00140 , EcoliWiki:b3185 , Mint:MINT-1317488 , PR:PRO_000023832 , Pride:P0A7L8 , Protein Model Portal:P0A7L8 , RefSeq:NP_417652 , SMR:P0A7L8 , String:511145.b3185 , UniProt:P0A7L8

Relationship Links: InterPro:IN-FAMILY:IPR001684 , InterPro:IN-FAMILY:IPR018261 , Panther:IN-FAMILY:PTHR15893 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF01016 , Prints:IN-FAMILY:PR00063 , ProDom:IN-FAMILY:PD003114 , Prosite:IN-FAMILY:PS00831

Summary:
The L27 protein is a component of the 50S subunit of the ribosome and may be an integral and functional component of the peptidyl transferase center [Hindennach71a, Chen75a]. Single-molecule fluorescence resonance energy transfer studies have indicated that L27 stabilizes the peptidyl-tRNA [Wang12l].

L27 participates both in the assembly of the 50S subunit and in the peptidyl transferase reaction [Wower98, Maguire05]. L27 crosslinks to aminoacylated tRNA in the A and P site [Wower89, Parker83, Rosen93, Osswald95, Maguire05]. Involvement of L27 with the peptidyl transferase center was also suggested by its interactions with various antibiotics: N-bromoacetyl chloramphenicol, an antibiotic that interacts with the peptidyl transferase center, affinity labels L27 [Sonenberg73]. L27 is labeled by the macrolides carbomycin A, niddamycin and tylosin, which inhibit ribosomal activity [Tejedor85a]. L27 can also be crosslinked to the spiramycin derivative dihydrospiramycin [Bischof95].

L27 interacts with domain V of 23S rRNA [Osswald90, Urlaub95, Thiede98] and can be crosslinked to L33 [Redl89]. L27 is exposed on the surface of the 70S ribosome [Agafonov97].

An rpmA deletion mutant has a severe growth defect and is cold- and temperature-sensitive [Wower98]. Deleting as few as three amino acids from the amino terminus of L27 leads to a defect in peptidyl transferase activity of the resulting ribosomes [Maguire05].

Citations: [Wower95, WittmannLiebold95, Amarantos01, Maguire01, Kirillov02, Shoji11]

Essentiality data for rpmA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L28

Synonyms: RpmB

Gene: rpmB Accession Numbers: EG10886 (EcoCyc), b3637, ECK3627

Locations: cytosol, ribosome

Sequence Length: 78 AAs

Molecular Weight: 9.006 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Zheng11, Rajagopala14, Arifuzzaman06]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35745N , EcoliWiki:b3637 , Mint:MINT-1306660 , PR:PRO_000023833 , Pride:P0A7M2 , Protein Model Portal:P0A7M2 , RefSeq:NP_418094 , SMR:P0A7M2 , String:511145.b3637 , UniProt:P0A7M2

Relationship Links: InterPro:IN-FAMILY:IPR001383 , InterPro:IN-FAMILY:IPR026569 , Panther:IN-FAMILY:PTHR13528 , PDB:Structure:1VT2 , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00830

Summary:
The L28 protein is a component of the 50S subunit of the ribosome and is required for ribosome assembly [Maguire97, Maguire97a, Maguire97b].

L28 interacts with 23S rRNA [Skold81, Osswald90, Urlaub95, Chistyakov89] and crosslinks to L9 [Walleczek89a, Redl89, Walleczek89].

L28 is labeled by the macrolides carbomycin A, niddamycin and tylosin, which inhibit ribosomal activity [Tejedor85a].

Essentiality data for rpmB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L29

Synonyms: RpmC

Gene: rpmC Accession Numbers: EG10887 (EcoCyc), b3312, ECK3299

Locations: cytosol, ribosome

Sequence Length: 63 AAs

Molecular Weight: 7.273 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-47911N , EcoliWiki:b3312 , Mint:MINT-1240640 , ModBase:P0A7M6 , PR:PRO_000023834 , Pride:P0A7M6 , Protein Model Portal:P0A7M6 , RefSeq:NP_417771 , SMR:P0A7M6 , String:511145.b3312 , UniProt:P0A7M6

Relationship Links: InterPro:IN-FAMILY:IPR001854 , InterPro:IN-FAMILY:IPR018254 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2VRH , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J45 , PDB:Structure:3J46 , PDB:Structure:3J4X , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00831 , Prosite:IN-FAMILY:PS00579

Summary:
The L29 protein is a component of the 50S subunit of the ribosome .

L29 interacts with 23S rRNA [WittmannLiebold95, Urlaub95] and is photoaffinity labeled by puromycin, an analog of the 3' end of aminoacylated tRNA [Bischof94]. L29 crosslinks to Trigger Factor (TF) [Kramer02] and contacts the Signal Recognition Particle [Ullers03], but is not required for the association of TF with the ribosome [Kramer02].

L29 together with ACP stimulates the binding of Tn7-encoded TnsD to attTn7, the insertion site for Tn7 in the E. coli chromosome. L23 also stimulates Tn7 transposition in vitro. A mutation in L29 decreases Tn7 transposition in vivo [Sharpe98].

Essentiality data for rpmC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L30

Synonyms: RpmD

Gene: rpmD Accession Numbers: EG10888 (EcoCyc), b3302, ECK3289

Locations: cytosol, ribosome

Sequence Length: 59 AAs

Molecular Weight: 6.542 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
Cellular Component: GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a]
GO:0015934 - large ribosomal subunit Inferred by computational analysis [GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35970N , EcoliWiki:b3302 , PR:PRO_000023835 , Pride:P0AG51 , Protein Model Portal:P0AG51 , RefSeq:NP_417761 , SMR:P0AG51 , String:511145.b3302 , Swiss-Model:P0AG51 , UniProt:P0AG51

Relationship Links: InterPro:IN-FAMILY:IPR005996 , InterPro:IN-FAMILY:IPR016082 , InterPro:IN-FAMILY:IPR018038 , PDB:Structure:1ML5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00327 , Prosite:IN-FAMILY:PS00634

Summary:
The L30 protein is a component of the 50S subunit of the ribosome.

L30 crosslinks to 23S rRNA [Osswald90]. An rpmD mutant has a growth and ribosomal assembly defect at 20°C [Geyl77].

Essentiality data for rpmD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L31

Synonyms: RpmE

Gene: rpmE Accession Numbers: EG10889 (EcoCyc), b3936, ECK3928

Locations: cytosol, ribosome

Sequence Length: 70 AAs

Molecular Weight: 7.871 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0008270 - zinc ion binding Inferred from experiment [Hensley12]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a, Eistetter99]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: EcoliWiki:b3936 , ModBase:P0A7M9 , PR:PRO_000023836 , Pride:P0A7M9 , Protein Model Portal:P0A7M9 , RefSeq:NP_418371 , SMR:P0A7M9 , String:511145.b3936 , UniProt:P0A7M9

Relationship Links: InterPro:IN-FAMILY:IPR002150 , InterPro:IN-FAMILY:IPR027491 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2J28 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:3BBX , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J37 , Pfam:IN-FAMILY:PF01197 , Prints:IN-FAMILY:PR01249 , Prosite:IN-FAMILY:PS01143

Summary:
The L31 protein is a component of the 50S subunit of the ribosome.

L31 can be isolated in a complex with 5S rRNA and L5, L18, and L25 [Fanning81] and can be crosslinked to tRNA in the P site [Graifer89]. Modeling shows that L31 may participate in the formation, dynamics and stabilization of the S13-L5 bridge [Shasmal10]. L31 may only be loosely associated with the ribosome [Eistetter99].

L31 was found to be phosphorylated [Soung09], and the purified protein binds Zn2+ [Hensley12].

YkgM is a paralog of RpmE that has lost the predicted metal-binding "zinc ribbon" motif [Makarova01a] and was shown to lack bound Zn2+, in contrast to L31 [Hensley12]. The authors propose a model where YkgM can provide the function of L31 in the ribosome under zinc limiting conditions.

Citations: [Dabbs81a]

Essentiality data for rpmE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L32

Synonyms: RpmF

Gene: rpmF Accession Numbers: EG10890 (EcoCyc), b1089, ECK1075

Locations: cytosol, ribosome

Sequence Length: 57 AAs

Molecular Weight: 6.446 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a]
GO:0015934 - large ribosomal subunit Inferred by computational analysis [GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35782N , EcoliWiki:b1089 , ModBase:P0A7N4 , PR:PRO_000023838 , Pride:P0A7N4 , Protein Model Portal:P0A7N4 , RefSeq:NP_415607 , SMR:P0A7N4 , String:511145.b1089 , UniProt:P0A7N4

Relationship Links: InterPro:IN-FAMILY:IPR002677 , InterPro:IN-FAMILY:IPR011332 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF01783

Summary:
The L32 protein is a component of the 50S subunit of the ribosome.

L32 is located within 21 Å of nucleotide C2475 of 23S rRNA, near the peptidyltransferase center [Muralikrishna95].

Essentiality data for rpmF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L33

Synonyms: RpmG

Gene: rpmG Accession Numbers: EG10891 (EcoCyc), b3636, ECK3626

Locations: cytosol, ribosome

Sequence Length: 55 AAs

Molecular Weight: 6.372 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0000049 - tRNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a, Gaudet10]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: DIP:DIP-35968N , DisProt:DP00143 , EcoliWiki:b3636 , Mint:MINT-1234559 , ModBase:P0A7N9 , PR:PRO_000023839 , Pride:P0A7N9 , Protein Model Portal:P0A7N9 , RefSeq:NP_418093 , SMR:P0A7N9 , String:511145.b3636 , UniProt:P0A7N9

Relationship Links: InterPro:IN-FAMILY:IPR001705 , InterPro:IN-FAMILY:IPR011332 , InterPro:IN-FAMILY:IPR018264 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5S , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00471 , Prosite:IN-FAMILY:PS00582

Summary:
The L33 protein is a component of the 50S subunit of the ribosome.

L33 is located within 21 Å of nucleotide C2475 of 23S rRNA, near the peptidyltransferase center [Muralikrishna95]. L33 had previously been shown to crosslink to 23S rRNA [Osswald90] and to tRNA in the P site [Bausk85, Graifer89, Podkowinski89, Sumpter90, Podkowinski91, Mitchell93b, Osswald95] and E site [Osswald95]. L33 also crosslinks to L1 and L27 [Walleczek89a, Redl89, Walleczek89].

The initiating methionine of L33 is lost [Arnold99] or may be methylated [Chang77a]; L33 is methylated at the first alanine residue [Cammack65, Chang77a, Arnold99].

A strain containing an IS element insertion in rpmG shows no major defect in ribosome assembly [Coleman93]; L33 appears to have no significant role in ribosome synthesis or function [Maguire97, Maguire97a, Maguire97b].

Essentiality data for rpmG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L34

Synonyms: SsaF, RimA, RpmH

Gene: rpmH Accession Numbers: EG10892 (EcoCyc), b3703, ECK3695

Locations: cytosol, ribosome

Sequence Length: 46 AAs

Molecular Weight: 5.38 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation
regulation type of regulation posttranscriptional inhibition / activation of enzymes

Unification Links: DIP:DIP-581N , EcoliWiki:b3703 , PR:PRO_000023840 , Pride:P0A7P5 , Protein Model Portal:P0A7P5 , RefSeq:NP_418158 , SMR:P0A7P5 , String:511145.b3703 , UniProt:P0A7P5

Relationship Links: InterPro:IN-FAMILY:IPR000271 , InterPro:IN-FAMILY:IPR020939 , Panther:IN-FAMILY:PTHR14503 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4UY8 , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00468 , ProDom:IN-FAMILY:PD003101 , Prosite:IN-FAMILY:PS00784

Summary:
The L34 protein is a component of the 50S subunit of the ribosome. L34 was also identified as antizyme 2, an inhibitor of the biosynthetic ornithine and arginine decarboxylases; these enzymes are involved in the biosynthesis of polyamine [Panagiotidis84].

L34 physically interacts with ornithine and arginine decarboxylase, and overexpression of L34 decreases the production of polyamine in vivo [Panagiotidis95]. Levels of L34 increase in response to polyamines; the effect is thought to be due to an increase in the level of transcription of rpmH [Huang90a].

The rimA mutant, likely an allele of rpmH [Hansen82], has a cold-sensitive growth and ribosome assembly defect [Bryant74].

Reviews: [Canellakis85, Panagiotidis88].

Essentiality data for rpmH knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 3]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L35

Synonyms: RpmI, 50S ribosomal subunit protein A, X1 protein

Gene: rpmI Accession Numbers: EG11231 (EcoCyc), b1717, ECK1715

Locations: cytosol, ribosome

Sequence Length: 65 AAs

Molecular Weight: 7.289 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
Molecular Function: GO:0003735 - structural constituent of ribosome Inferred from experiment Inferred by computational analysis [GOA01a, Wada87a]
Cellular Component: GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Wada87a]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: EcoliWiki:b1717 , PR:PRO_000023841 , Pride:P0A7Q1 , Protein Model Portal:P0A7Q1 , RefSeq:NP_416232 , SMR:P0A7Q1 , String:511145.b1717 , UniProt:P0A7Q1

Relationship Links: InterPro:IN-FAMILY:IPR001706 , InterPro:IN-FAMILY:IPR018265 , InterPro:IN-FAMILY:IPR021137 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF01632 , Prints:IN-FAMILY:PR00064 , Prosite:IN-FAMILY:PS00936

Summary:
The L35 protein is a component of the 50S subunit of the ribosome [Wada87a].

L35 can be crosslinked to the spiramycin derivative dihydrospiramycin and may thus be located near the peptidyl transferase center [Bischof95].

Essentiality data for rpmI knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Subunit of 50S ribosomal subunit: 50S ribosomal subunit protein L36

Synonyms: SecX, RpmJ, 50S ribosomal subunit protein B

Gene: rpmJ Accession Numbers: EG11232 (EcoCyc), b3299, ECK3286

Locations: cytosol, ribosome

Sequence Length: 38 AAs

Molecular Weight: 4.364 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01a]
GO:0042254 - ribosome biogenesis Inferred by computational analysis [Gaudet10]
Molecular Function: GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0022625 - cytosolic large ribosomal subunit
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Unification Links: EcoliWiki:b3299 , PR:PRO_000023842 , Protein Model Portal:P0A7Q6 , RefSeq:NP_417758 , SMR:P0A7Q6 , String:511145.b3299 , UniProt:P0A7Q6

Relationship Links: InterPro:IN-FAMILY:IPR000473 , Panther:IN-FAMILY:PTHR18804 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J4X , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3J50 , PDB:Structure:3J51 , PDB:Structure:3J52 , PDB:Structure:3J54 , PDB:Structure:3J56 , PDB:Structure:3J58 , PDB:Structure:3J5A , PDB:Structure:3J5C , PDB:Structure:3J5E , PDB:Structure:3J5G , PDB:Structure:3J5I , PDB:Structure:3J5K , PDB:Structure:3J5L , PDB:Structure:3J5O , PDB:Structure:3J5U , PDB:Structure:3J5W , PDB:Structure:3J7Z , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:4CSU , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , PDB:Structure:4PEB , PDB:Structure:4PEC , PDB:Structure:4TOM , PDB:Structure:4TOO , PDB:Structure:4TOV , PDB:Structure:4TOX , PDB:Structure:4TP1 , PDB:Structure:4TP3 , PDB:Structure:4TP5 , PDB:Structure:4TP7 , PDB:Structure:4TP9 , PDB:Structure:4TPB , PDB:Structure:4TPD , PDB:Structure:4TPF , PDB:Structure:4WAP , PDB:Structure:4WAR , Pfam:IN-FAMILY:PF00444 , Prosite:IN-FAMILY:PS00828

Summary:
The L36 protein is a component of the 50S subunit of the ribosome [Wada87a]. L36 is highly conserved in bacteria, mitochondria and chloroplasts, but not present in archaea and eucarya [Maeder05].

Ribosomes lacking L36 are correctly assembled. However, chemical protection experiments suggest that rRNA tertiary interactions are disrupted in ribosomes lacking L36, thus arguing that L36 plays a significant role in organizing 23S rRNA structure [Maeder05]. L36 has ben shown to crosslink to 23S rRNA [Urlaub95].

Deletion of rpmJ causes a temperature-sensitive growth defect [Ikegami05, Maeder05]; the rpmJ deletion led to decreased expression of secY, located immediately upstream of rpmJ. rpmJ does not appear to be essential for protein synthesis [Ikegami05].

Essentiality data for rpmJ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

References

AbdelMeguid83: Abdel-Meguid SS, Moore PB, Steitz TA (1983). "Crystallization of a ribonuclease-resistant fragment of Escherichia coli 5 S ribosomal RNA and its complex with protein L25." J Mol Biol 171(2);207-15. PMID: 6197527

Abdurashidova79: Abdurashidova GG, Turchinsky MF, Aslanov KA, Budowsky EI (1979). "Polynucleotide-protein interactions in the translation system. Identification of proteins interacting with tRNA in the A- and P-sites of E. coli ribosomes." Nucleic Acids Res 6(12);3891-909. PMID: 386278

Abdurashidova85: Abdurashidova GG, Tsvetkova EA, Chernyi AA, Kaminir LB, Budowsky EI (1985). "Intersubunit RNA-protein contacts in pre- and post-translocated E. coli ribosome." FEBS Lett 185(2);291-4. PMID: 2581817

Abdurashidova90: Abdurashidova GG, Tsvetkova EA, Budowsky EI (1990). "Determination of tRNA nucleotide residues directly interacting with proteins in the post- and pretranslocated ribosomal complexes." FEBS Lett 269(2);398-401. PMID: 2205514

Abdurashidova91: Abdurashidova GG, Tsvetkova EA, Budowsky EI (1991). "Direct tRNA-protein interactions in ribosomal complexes." Nucleic Acids Res 19(8);1909-15. PMID: 1709494

Adachi79: Adachi K, Sells BH (1979). "The effect of magnesium starvation on the dissociation of ribosomal proteins from Escherichia coli K-12 ribosomes." Biochim Biophys Acta 563(1);163-70. PMID: 387084

Adamski96: Adamski FM, Atkins JF, Gesteland RF (1996). "Ribosomal protein L9 interactions with 23 S rRNA: the use of a translational bypass assay to study the effect of amino acid substitutions." J Mol Biol 261(3);357-71. PMID: 8780779

Agafonov97: Agafonov DE, Kolb VA, Spirin AS (1997). "Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique." Proc Natl Acad Sci U S A 94(24);12892-7. PMID: 9371771

Agrawal04: Agrawal RK, Sharma MR, Kiel MC, Hirokawa G, Booth TM, Spahn CM, Grassucci RA, Kaji A, Frank J (2004). "Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implications." Proc Natl Acad Sci U S A 101(24);8900-5. PMID: 15178758

Akiyama81: Akiyama T, Tanaka N (1981). "Ribosomal proteins S9 and L6 participate in the binding of [3H]dibekacin to E. coli ribosomes." J Antibiot (Tokyo) 34(6);763-9. PMID: 6268595

Albanese02: Albanese V, Frydman J (2002). "Where chaperones and nascent polypeptides meet." Nat Struct Biol 9(10);716-8. PMID: 12352951

Allemand07: Allemand F, Haentjens J, Chiaruttini C, Royer C, Springer M (2007). "Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites." Nucleic Acids Res 35(9):3016-31. PMID: 17439971

AlMajdoub13: Al-Majdoub ZM, Owoseni A, Gaskell SJ, Barber J (2013). "Effects of gentamicin on the proteomes of aerobic and oxygen-limited Escherichia coli." J Med Chem 56(7);2904-10. PMID: 23517076

Amarantos01: Amarantos I, Xaplanteri MA, Choli-Papadopoulou T, Kalpaxis DL (2001). "Effects of two photoreactive spermine analogues on peptide bond formation and their application for labeling proteins in Escherichia coli functional ribosomal complexes." Biochemistry 40(25);7641-50. PMID: 11412118

Andrieux84: Andrieux E, Cozzone AJ (1984). "Conformational changes in bacterial polysomes induced by amino acid starvation." Int J Biochem 16(1);113-6. PMID: 6365649

Anikaev14: Anikaev AY, Korepanov AP, Korobeinikova AV, Kljashtorny VG, Piendl W, Nikonov SV, Garber MB, Gongadze GM (2014). "Mutant Forms of Escherichia coli Protein L25 Unable to Bind to 5S rRNA Are Incorporated Efficiently into the Ribosome in vivo." Biochemistry (Mosc) 79(8);826-35. PMID: 25365493

Apirion67: Apirion D (1967). "Three genes that affect Escherichia coli ribosomes." J Mol Biol 30(2);255-75. PMID: 4870510

Arevalo88: Arevalo MA, Tejedor F, Polo F, Ballesta JP (1988). "Protein components of the erythromycin binding site in bacterial ribosomes." J Biol Chem 263(1);58-63. PMID: 3275651

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Arnold99: Arnold RJ, Reilly JP (1999). "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry." Anal Biochem 269(1);105-12. PMID: 10094780

Arthur87a: Arthur M, Brisson-Noel A, Courvalin P (1987). "Origin and evolution of genes specifying resistance to macrolide, lincosamide and streptogramin antibiotics: data and hypotheses." J Antimicrob Chemother 20(6);783-802. PMID: 3326871

Aseev15: Aseev LV, Bylinkina NS, Boni IV (2015). "Regulation of the rplY gene encoding 5S rRNA binding protein L25 in Escherichia coli and related bacteria." RNA 21(5);851-61. PMID: 25749694

Atkins09: Atkins JF, Bjork GR (2009). "A gripping tale of ribosomal frameshifting: extragenic suppressors of frameshift mutations spotlight P-site realignment." Microbiol Mol Biol Rev 73(1);178-210. PMID: 19258537

Azad79: Azad AA (1979). "Intermolecular base-paired interaction between complementary sequences present near the 3' ends of 5S rRNA and 18S (16S) rRNA might be involved in the reversible association of ribosomal subunits." Nucleic Acids Res 7(7);1913-29. PMID: 94160

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Barciszewska96: Barciszewska MZ, Erdmann VA, Barciszewski J (1996). "Ribosomal 5S RNA: tertiary structure and interactions with proteins." Biol Rev Camb Philos Soc 71(1);1-25. PMID: 8603119

Barciszewska97: Barciszewska MZ (1997). "[RNA tectonics]." Postepy Biochem 43(4);267-74. PMID: 9572078

Barritault75: Barritault D, Expert-Bezancon A, Milet M (1975). "[Nearest-neighbor relationships among 50S ribosomal proteins of E. coli]." C R Acad Sci Hebd Seances Acad Sci D 281(14);1043-6. PMID: 813873

Barry80: Barry G, Squires C, Squires CL (1980). "Attenuation and processing of RNA from the rplJL--rpoBC transcription unit of Escherichia coli." Proc Natl Acad Sci U S A 77(6);3331-5. PMID: 6158044

Baughman83: Baughman G, Nomura M (1983). "Localization of the target site for translational regulation of the L11 operon and direct evidence for translational coupling in Escherichia coli." Cell 34(3);979-88. PMID: 6354472

Baughman84: Baughman G, Nomura M (1984). "Translational regulation of the L11 ribosomal protein operon of Escherichia coli: analysis of the mRNA target site using oligonucleotide-directed mutagenesis." Proc Natl Acad Sci U S A 81(17);5389-93. PMID: 6382263

Bausk85: Bausk EV, Graifer DM, Karpova GG (1985). "[Study of the photoaffinity modification of Escherichia coli ribosomes near the donor tRNA-binding center]." Mol Biol (Mosk) 19(2);545-52. PMID: 3889589

Baxter78: Baxter RM, Zahid ND (1978). "The modification of the peptidyl transferase activity of 50-S ribosomal subunits, LiC1-split proteins and L16 ribosomal protein by ethoxyformic anhydride." Eur J Biochem 91(1);49-56. PMID: 363428

Baxter80: Baxter RM, White VT, Zahid ND (1980). "The modification of the peptidyltransferase activity of 50-S ribosomal subunits, LiCl-split proteins and L16 ribosomal protein by pyridoxal phosphate." Eur J Biochem 110(1);161-6. PMID: 6254759

Baxter87: Baxter RM, Ganoza MC, Zahid N, Chung DG (1987). "Reconstruction of peptidyltransferase activity on 50S and 70S ribosomal particles by peptide fragments of protein L16." Eur J Biochem 163(3);473-9. PMID: 3549294

Bear77: Bear DG, Schleich T, Noller HF, Garrett RA (1977). "Alteration of 5S RNA conformation by ribosomal proteins L18 and L25." Nucleic Acids Res 4(7);2511-26. PMID: 333392

Beauclerk84: Beauclerk AA, Cundliffe E, Dijk J (1984). "The binding site for ribosomal protein complex L8 within 23 s ribosomal RNA of Escherichia coli." J Biol Chem 259(10);6559-63. PMID: 6373761

Beauclerk88: Beauclerk AA, Cundliffe E (1988). "The binding site for ribosomal protein L2 within 23S ribosomal RNA of Escherichia coli." EMBO J 7(11);3589-94. PMID: 3061801

Bernabeu76: Bernabeu C, Vazquez D, Ballesta JP (1976). "Activities of protein-deficient particles derived from 50-S ribosomal subunits by NH4Cl/ethanol treatment." Eur J Biochem 69(1);233-41. PMID: 791646

Bernabeu77: Bernabeu C, Vazquez D, Ballesta JP (1977). "The involvement of protein L16 on ribosomal peptidyl transferase activity." Eur J Biochem 79(2);469-72. PMID: 336360

Bernabeu78: Bernabeu C, Vazquez D, Ballesta JP (1978). "Proteins associated with rRNA in the Escherichia coli ribosome." Biochim Biophys Acta 518(2);290-7. PMID: 350280

Bischof94: Bischof O, Kruft V, Wittmann-Liebold B (1994). "Analysis of the puromycin binding site in the 70 S ribosome of Escherichia coli at the peptide level." J Biol Chem 269(28);18315-9. PMID: 8034577

Bischof95: Bischof O, Urlaub H, Kruft V, Wittmann-Liebold B (1995). "Peptide environment of the peptidyl transferase center from Escherichia coli 70 S ribosomes as determined by thermoaffinity labeling with dihydrospiramycin." J Biol Chem 270(39);23060-4. PMID: 7559446

Bitar75: Bitar KG, Wittmann-Liebold B (1975). "The primary structure of the 5s rRNA binding protein L25 of Escherichia coli ribosomes." Hoppe Seylers Z Physiol Chem 356(9);1343-52. PMID: 1100506

Blyn00: Blyn LB, Risen LM, Griffey RH, Draper DE (2000). "The RNA-binding domain of ribosomal protein L11 recognizes an rRNA tertiary structure stabilized by both thiostrepton and magnesium ion." Nucleic Acids Res 28(8);1778-84. PMID: 10734197

Bocharov98: Bocharov EV, Gudkov AT, Budovskaya EV, Arseniev AS (1998). "Conformational independence of N- and C-domains in ribosomal protein L7/L12 and in the complex with protein L10." FEBS Lett 423(3);347-50. PMID: 9515737

Bock13: Bock LV, Blau C, Schroder GF, Davydov II, Fischer N, Stark H, Rodnina MV, Vaiana AC, Grubmuller H (2013). "Energy barriers and driving forces in tRNA translocation through the ribosome." Nat Struct Mol Biol 20(12);1390-6. PMID: 24186064

Bosl81: Bosl A, Bock A (1981). "Ribosomal mutation in Escherichia coli affecting membrane stability." Mol Gen Genet 182(2);358-60. PMID: 7026977

Bosling03: Bosling J, Poulsen SM, Vester B, Long KS (2003). "Resistance to the peptidyl transferase inhibitor tiamulin caused by mutation of ribosomal protein l3." Antimicrob Agents Chemother 47(9);2892-6. PMID: 12936991

Bouakaz06: Bouakaz L, Bouakaz E, Murgola EJ, Ehrenberg M, Sanyal S (2006). "The role of ribosomal protein L11 in class I release factor-mediated translation termination and translational accuracy." J Biol Chem 281(7);4548-56. PMID: 16371360

Bowen05: Bowen WS, Van Dyke N, Murgola EJ, Lodmell JS, Hill WE (2005). "Interaction of thiostrepton and elongation factor-G with the ribosomal protein L11-binding domain." J Biol Chem 280(4);2934-43. PMID: 15492007

Branlant76: Branlant C, Krol A, Sriwidada J, Brimacombe R (1976). "RNA sequences associated with proteins L1, L9, and L5, L18, L25, in ribonucleoprotein fragments isolated from the 50-S subunit of Escherichia coli ribosomes." Eur J Biochem 70(2);483-92. PMID: 827440

Branlant76a: Branlant C, Krol A, Sriwdada J, Ebel JP, Sloof P, Garrett RA (1976). "The binding site of protein L1 ON 23-S ribosomal RNA of Escherichia coli. 2. Identification of the rna region contained in the L1 ribonucleoproteins and determination of the order of the RNA subfragments within this region." Eur J Biochem 70(2);457-69. PMID: 827439

Branlant77: Branlant C, Widada JS, Krol A, Ebel JP (1977). "Studies on the primary structure of the ribosomal 23S RNA of Escherichia coli: II. A characterisation and an alignment of 24 sections spanning the entire molecule and its application to the localisation of specific fragments." Nucleic Acids Res 4(12);4323-45. PMID: 414209

Branlant77a: Branlant C, Sri Widada J, Krol A, Ebel JP (1977). "RNA sequences in ribonucleoprotein fragments of the complex formed from ribosomal 23-S RNA and ribosomal protein L24 of Escherichia coli." Eur J Biochem 74(1);155-70. PMID: 404143

Branlant80: Branlant C, Krol A, Ebel JP (1980). "Characterization of the Escherichia coli 23S Ribosomal RNA region associated with ribosomal protein L1. Evidence for homologies with the 5'-end region of the L11 operon." Nucleic Acids Res 8(23);5567-77. PMID: 6162152

Brewer83: Brewer LA, Goelz S, Noller HF (1983). "Ribonucleic acid-protein cross-linking within the intact Escherichia coli ribosome, utilizing ethylene glycol bis[3-(2-ketobutyraldehyde) ether], a reversible, bifunctional reagent: synthesis and cross-linking within 30S and 50S subunits." Biochemistry 22(18);4303-9. PMID: 6354252

Brimacombe91: Brimacombe R (1991). "RNA-protein interactions in the Escherichia coli ribosome." Biochimie 73(7-8);927-36. PMID: 1720671

Brimacombe92: Brimacombe R (1992). "Structure-function correlations (and discrepancies) in the 16S ribosomal RNA from Escherichia coli." Biochimie 74(4);319-26. PMID: 1379076

BrissonNoel88: Brisson-Noel A, Trieu-Cuot P, Courvalin P (1988). "Mechanism of action of spiramycin and other macrolides." J Antimicrob Chemother 22 Suppl B;13-23. PMID: 3053566

Brosius76: Brosius J, Chen R (1976). "The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes." FEBS Lett 68(1);105-9. PMID: 786730

Brot81: Brot N, Caldwell P, Weissbach H (1981). "Regulation of synthesis of Escherichia coli ribosomal proteins L1 and L11." Arch Biochem Biophys 206(1);51-3. PMID: 7011209

Bryant74: Bryant RE, Sypherd PS (1974). "Genetic analysis of cold-sensitive ribosome maturation mutants of Escherichia coli." J Bacteriol 117(3);1082-92. PMID: 4591943

Buckel77: Buckel P, Buchberger A, Bock A, Wittmann HG (1977). "Alteration of ribosomal protein L6 in mutants of Escherichia coli resistant to gentamicin." Mol Gen Genet 158(1);47-54. PMID: 342908

BurnetteVick94: Burnette-Vick B, Champney WS, Musich PR (1994). "A temperature-sensitive mutant of Escherichia coli with an alteration in ribosomal protein L22." Genetica 94(1);17-25. PMID: 7729693

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Cabezon80: Cabezon T, Delcuve G, Faelen M, Desmet L, Bollen A (1980). "Polarity of amber mutations in ribosomal protein genes of Escherichia coli." J Bacteriol 141(1);41-51. PMID: 6986365

Cammack65: Cammack KA, Wade HE (1965). "The sedimentation behaviour of ribonuclease-active and -inactive ribosomes from bacteria." Biochem J 96(3);671-80. PMID: 5324303

Campbell08: Campbell TL, Brown ED (2008). "Genetic interaction screens with ordered overexpression and deletion clonesets implicate the Escherichia coli GTPase YjeQ in late ribosome biogenesis." J Bacteriol 190(7);2537-45. PMID: 18223068

Canellakis85: Canellakis ES, Kyriakidis DA, Rinehart CA, Huang SC, Panagiotidis C, Fong WF (1985). "Regulation of polyamine biosynthesis by antizyme and some recent developments relating the induction of polyamine biosynthesis to cell growth. Review." Biosci Rep 5(3);189-204. PMID: 3893559

Caulfield12: Caulfield T, Devkota B (2012). "Motion of transfer RNA from the A/T state into the A-site using docking and simulations." Proteins 80(11);2489-500. PMID: 22730134

Cerretti83: Cerretti DP, Dean D, Davis GR, Bedwell DM, Nomura M (1983). "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene." Nucleic Acids Res 1983;11(9);2599-616. PMID: 6222285

Cerretti88: Cerretti DP, Mattheakis LC, Kearney KR, Vu L, Nomura M (1988). "Translational regulation of the spc operon in Escherichia coli. Identification and structural analysis of the target site for S8 repressor protein." J Mol Biol 204(2);309-29. PMID: 2464692

Chaires82: Chaires JB, Hawley DA, Wahba AJ (1982). "Chain initiation factor 3 crosslinks to E. coli 30S and 50S ribosomal subunits and alters the UV absorbance spectrum of 70S ribosomes." Nucleic Acids Res 10(18);5681-93. PMID: 6755396

Champney80: Champney WS (1980). "Protein synthesis defects in temperature-sensitive mutants of Escherichia coli with altered ribosomal proteins." Biochim Biophys Acta 609(3);464-74. PMID: 6159923

Chang74: Chang FN, Chang CN, Paik WK (1974). "Methylation of ribosomal proteins in Escherichia coli." J Bacteriol 120(2);651-6. PMID: 4616944

Chang75a: Chang CN, Chang N (1975). "Methylation of the ribosomal proteins in Escherichia coli. Nature and stoichiometry of the methylated amino acids in 50S ribosomal proteins." Biochemistry 14(3);468-77. PMID: 1089427

Chang77a: Chang FN, Budzilowicz C (1977). "Characterization of methylated neutral amino acids from Escherichia coli ribosomes." J Bacteriol 131(1);105-10. PMID: 326752

Charette00: Charette M, Gray MW (2000). "Pseudouridine in RNA: what, where, how, and why." IUBMB Life 49(5);341-51. PMID: 10902565

Charollais03: Charollais J, Pflieger D, Vinh J, Dreyfus M, Iost I (2003). "The DEAD-box RNA helicase SrmB is involved in the assembly of 50S ribosomal subunits in Escherichia coli." Mol Microbiol 48(5);1253-65. PMID: 12787353

Chen75a: Chen R, Mende L, Arfsten U (1975). "The primary structure of protein L27 from the peptidyl-tRNA binding site of Escherichia coli ribosomes." FEBS Lett 59(1);96-9. PMID: 1225626

Chen76: Chen R, Ehrke G (1976). "The primary structure of the 5 S RNA binding protein L5 of Escherichia coli ribosomes." FEBS Lett 69(1);240-5. PMID: 791672

Chen77: Chen R, Brosius J, Wittmann-Liebold B (1977). "Occurrence of methylated amino acids as N-termini of proteins from Escherichia coli ribosomes." J Mol Biol 111(2);173-81. PMID: 323502

ChenSchmeisser77: Chen-Schmeisser U, Garrett RA (1977). "A new method for the isolation of a 5 S RNA complex with proteins L5, L18 and L25 from Escherichia coli ribosomes." FEBS Lett 74(2);287-91. PMID: 321249

Chiaruttini96: Chiaruttini C, Milet M, Springer M (1996). "A long-range RNA-RNA interaction forms a pseudoknot required for translational control of the IF3-L35-L20 ribosomal protein operon in Escherichia coli." EMBO J 15(16);4402-13. PMID: 8861967

Chiaruttini96a: Chiaruttini C, Milet M, de Smit M, Springer M (1996). "Translational coupling in the Escherichia coli operon encoding translation initiation factor IF3 and ribosomal proteins L20 and L35." Biochimie 78(7);555-67. PMID: 8955899

Chiaruttini97: Chiaruttini C, Milet M, Springer M (1997). "Translational coupling by modulation of feedback repression in the IF3 operon of Escherichia coli." Proc Natl Acad Sci U S A 94(17);9208-13. PMID: 9256461

Chigradze08: Chigradze IuN (2008). "[Structural behavior of RNA-binding proteins in free and complex states: ribosomal protein L25 and 5S RNA from Escherichia coli]." Mol Biol (Mosk) 42(4);685-92. PMID: 18856069

Chistyakov89: Chistyakov PG, Venjaminova AG, Vladimirov SN, Graifer DM, Kazakov SA, Karpova GG (1989). "Differences in 23 S rRNA-protein neighbourhood in Escherichia coli 70 S ribosomes and 70 S initiation complex. Probing by bifunctional Pt(II)-containing reagent." FEBS Lett 246(1-2);197-201. PMID: 2495985

Chittum94: Chittum HS, Champney WS (1994). "Ribosomal protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli." J Bacteriol 176(20);6192-8. PMID: 7928988

Chittum95: Chittum HS, Champney WS (1995). "Erythromycin inhibits the assembly of the large ribosomal subunit in growing Escherichia coli cells." Curr Microbiol 30(5);273-9. PMID: 7766155

Chodavarapu11: Chodavarapu S, Felczak MM, Kaguni JM (2011). "Two forms of ribosomal protein L2 of Escherichia coli that inhibit DnaA in DNA replication." Nucleic Acids Res 39(10);4180-91. PMID: 21288885

Christensen84: Christensen T, Johnsen M, Fiil NP, Friesen JD (1984). "RNA secondary structure and translation inhibition: analysis of mutants in the rplJ leader." EMBO J 3(7);1609-12. PMID: 6378628

Christiansen85: Christiansen J, Douthwaite SR, Christensen A, Garrett RA (1985). "Does unpaired adenosine-66 from helix II of Escherichia coli 5S RNA bind to protein L18?." EMBO J 4(4);1019-24. PMID: 2990903

Chu76: Chu F, Caldwell P, Samuels M, Weissbach H, Brot N (1976). "DNA-dependent in vitro synthesis of Escherichia coli ribosomal protein L10 and the formation of an L10L12 complex." Biochem Biophys Res Commun 76(2);593-601. PMID: 800342

Chu76a: Chu FK, Maeba PY (1976). "Protein binding and subunit association activity in particles reconstituted from Escherichia coli MRE600 50S ribosomal components." Can J Biochem 54(5);470-6. PMID: 776368

Ciesiolka92: Ciesiolka J, Lorenz S, Erdmann VA (1992). "Structural analysis of three prokaryotic 5S rRNA species and selected 5S rRNA--ribosomal-protein complexes by means of Pb(II)-induced hydrolysis." Eur J Biochem 204(2);575-81. PMID: 1541273

Climie87: Climie SC, Friesen JD (1987). "Feedback regulation of the rplJL-rpoBC ribosomal protein operon of Escherichia coli requires a region of mRNA secondary structure." J Mol Biol 198(3);371-81. PMID: 2448482

Climie88: Climie SC, Friesen JD (1988). "In vivo and in vitro structural analysis of the rplJ mRNA leader of Escherichia coli. Protection by bound L10-L7/L12." J Biol Chem 263(29);15166-75. PMID: 3049601

Cole86: Cole JR, Nomura M (1986). "Translational regulation is responsible for growth-rate-dependent and stringent control of the synthesis of ribosomal proteins L11 and L1 in Escherichia coli." Proc Natl Acad Sci U S A 83(12);4129-33. PMID: 3520566

Coleman93: Coleman SH, Maguire BA, Wild DG (1993). "Ribosome assembly in three strains of Escherichia coli with mutations in the rpmB,G operon." J Gen Microbiol 139(4);707-16. PMID: 7685806

Cooperman75: Cooperman BS, Jaynes EN, Brunswick DJ, Luddy MA (1975). "Photoincorporation of puromycin and N-(ethyl-2-diazomalonyl)puromycin into Escherichia coli ribosomes." Proc Natl Acad Sci U S A 72(8);2974-8. PMID: 1103130

Czernilofsky74: Czernilofsky AP, Collatz EE, Stoffler G, Kuechler E (1974). "Proteins at the tRNA binding sites of Escherichia coli ribosomes." Proc Natl Acad Sci U S A 71(1);230-4. PMID: 4589893

Dabbs77: Dabbs ER (1977). "A spectinomycin dependent mutant of Escherichia coli." Mol Gen Genet 151(3);261-7. PMID: 141001

Dabbs81: Dabbs ER, Ehrlich R, Hasenbank R, Schroeter BH, Stoffler-Meilicke M, Stoffler G (1981). "Mutants of Escherichia coli lacking ribosomal protein L1." J Mol Biol 149(4);553-78. PMID: 6171646

Dabbs81a: Dabbs ER (1981). "The gene for ribosomal protein L31, rpmE, is located at 88.5 minutes on the Escherichia coli chromosomal linkage map." J Bacteriol 148(1);379-82. PMID: 7026537

Dabbs82: Dabbs ER (1982). "A spontaneous mutant of Escherichia coli with protein L24 lacking from the ribosome." Mol Gen Genet 187(3);453-8. PMID: 6757660

Dahlberg89: Dahlberg AE (1989). "The functional role of ribosomal RNA in protein synthesis." Cell 57(4);525-9. PMID: 2655923

Datta05: Datta PP, Sharma MR, Qi L, Frank J, Agrawal RK (2005). "Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM." Mol Cell 20(5);723-31. PMID: 16337596

deBethune78: de Bethune MP, Nierhaus KH (1978). "Characterisation of the binding of virginiamycin S to Escherichia coli ribosomes." Eur J Biochem 86(1);187-91. PMID: 95947

deNarvaez79: de Narvaez CC, Schaup HW (1979). "In vivo transcriptionally coupled assembly of Escherichia coli ribosomal subunits." J Mol Biol 134(1);1-22. PMID: 94102

Dey98: Dey D, Bochkariov DE, Jokhadze GG, Traut RR (1998). "Cross-linking of selected residues in the N- and C-terminal domains of Escherichia coli protein L7/L12 to other ribosomal proteins and the effect of elongation factor Tu." J Biol Chem 273(3);1670-6. PMID: 9430711

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Diedrich00: Diedrich G, Spahn CM, Stelzl U, Schafer MA, Wooten T, Bochkariov DE, Cooperman BS, Traut RR, Nierhaus KH (2000). "Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer." EMBO J 19(19);5241-50. PMID: 11013226

Diner09: Diner EJ, Hayes CS (2009). "Recombineering reveals a diverse collection of ribosomal proteins L4 and L22 that confer resistance to macrolide antibiotics." J Mol Biol 386(2);300-15. PMID: 19150357

Dognin80: Dognin MJ, Wittmann-Liebold B (1980). "Identification of methylated amino acids during sequence analysis. Application to the Escherichia coli ribosomal protein L11." Hoppe Seylers Z Physiol Chem 361(11);1697-705. PMID: 6778808

Dognin80a: Dognin MJ, Wittmann-Liebold B (1980). "Purification and primary structure determination of the N-terminal blocked protein, L11, from Escherichia coli ribosomes." Eur J Biochem 112(1);131-51. PMID: 7004866

Dontsova90: Dontsova OA, Efimov AV, Kopylov AM (1990). "[The 5S rRNA-protein complex of Escherichia coli studied by carbodiimide modification]." Nauchnye Doki Vyss Shkoly Biol Nauki (2);22-30. PMID: 1693861

Douthwaite79: Douthwaite S, Garrett RA, Wagner R, Feunteun J (1979). "A ribonuclease-resistant region of 5S RNA and its relation to the RNA binding sites of proteins L18 and L25." Nucleic Acids Res 6(7);2453-70. PMID: 379819

Douthwaite82: Douthwaite S, Christensen A, Garrett RA (1982). "Binding site of ribosomal proteins on prokaryotic 5S ribonucleic acids: a study with ribonucleases." Biochemistry 21(10);2313-20. PMID: 6178424

Douthwalte95: Douthwalte S, Voldborg B, Hansen LH, Rosendahl G, Vester B (1995). "Recognition determinants for proteins and antibiotics within 23S rRNA." Biochem Cell Biol 73(11-12);1179-85. PMID: 8722035

Dovgas75: Dovgas NV, Markova LF, Mednikova TA, Vinokurov LM, Alakhov YB, Ovhinnikov YA (1975). "The primary structure of the 5 S RNA binding protein L25 from Escherichia coli ribosomes." FEBS Lett 53(3);351-4. PMID: 1093874

Drygin00: Drygin D, Zimmermann RA (2000). "Magnesium ions mediate contacts between phosphoryl oxygens at positions 2122 and 2176 of the 23S rRNA and ribosomal protein L1." RNA 6(12);1714-26. PMID: 11142372

Dunkle10: Dunkle JA, Xiong L, Mankin AS, Cate JH (2010). "Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action." Proc Natl Acad Sci U S A 107(40);17152-7. PMID: 20876128

Dunkle11: Dunkle JA, Wang L, Feldman MB, Pulk A, Chen VB, Kapral GJ, Noeske J, Richardson JS, Blanchard SC, Cate JH (2011). "Structures of the bacterial ribosome in classical and hybrid states of tRNA binding." Science 332(6032);981-4. PMID: 21596992

Dzionara77: Dzionara M, Robinson SM, Wittmann-Liebold B (1977). "Prediction for secondary structures of ten proteins from the 50S subunit of the Escherichia coli ribosome." J Supramol Struct 7(2);191-204. PMID: 340794

Egebjerg87: Egebjerg J, Leffers H, Christensen A, Andersen H, Garrett RA (1987). "Structure and accessibility of domain I of Escherichia coli 23 S RNA in free RNA, in the L24-RNA complex and in 50 S subunits. Implications for ribosomal assembly." J Mol Biol 196(1);125-36. PMID: 2443713

Egebjerg89: Egebjerg J, Christiansen J, Brown RS, Larsen N, Garrett RA (1989). "Protein L18 binds primarily at the junctions of helix II and internal loops A and B in Escherichia coli 5 S RNA. Implications for 5 S RNA structure." J Mol Biol 206(4);651-68. PMID: 2472486

Egebjerg90: Egebjerg J, Douthwaite SR, Liljas A, Garrett RA (1990). "Characterization of the binding sites of protein L11 and the L10.(L12)4 pentameric complex in the GTPase domain of 23 S ribosomal RNA from Escherichia coli." J Mol Biol 213(2);275-88. PMID: 1692883

Egebjerg91: Egebjerg J, Christiansen J, Garrett RA (1991). "Attachment sites of primary binding proteins L1, L2 and L23 on 23 S ribosomal RNA of Escherichia coli." J Mol Biol 222(2);251-64. PMID: 1960726

Eistetter99: Eistetter AJ, Butler PD, Traut RR, Fanning TG (1999). "Characterization of Escherichia coli 50S ribosomal protein L31." FEMS Microbiol Lett 180(2);345-9. PMID: 10556732

Fanning81: Fanning TG, Traut RR (1981). "Topography of the E. coli 5S RNA-protein complex as determined by crosslinking with dimethyl suberimidate and dimethyl-3,3'-dithiobispropionimidate." Nucleic Acids Res 9(4);993-1004. PMID: 7015289

Fanning81a: Fanning TG, Traut RR (1981). "Iodination of Escherichia coli ribosomal protein L18 abolishes its 5 S RNA binding activity." Biochim Biophys Acta 652(2);256-60. PMID: 7011398

Fiil80: Fiil NP, Friesen JD, Downing WL, Dennis PP (1980). "Post-transcriptional regulatory mutants in a ribosomal protein-RNA polymerase operon of E. coli." Cell 19(4);837-44. PMID: 6991124

Fischer15: Fischer N, Neumann P, Konevega AL, Bock LV, Ficner R, Rodnina MV, Stark H (2015). "Structure of the E. coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM." Nature 520(7548);567-70. PMID: 25707802

Fox78: Fox JW, Wong KP (1978). "Changes in the conformation and stability of 5 S RNA upon the binding of ribosomal proteins." J Biol Chem 253(1);18-20. PMID: 338605

Fox88: Fox JW, Owens DP, Wong KP (1988). "Purification and conformation of ribosomal protein L25 from E. coli ribosome." Int J Pept Protein Res 31(3);255-64. PMID: 3286550

Franceschi88: Franceschi FJ, Nierhaus KH (1988). "Ribosomal protein L20 can replace the assembly-initiator protein L24 at low temperatures." Biochemistry 27(18);7056-9. PMID: 2461735

Franceschi90: Franceschi FJ, Nierhaus KH (1990). "Ribosomal proteins L15 and L16 are mere late assembly proteins of the large ribosomal subunit. Analysis of an Escherichia coli mutant lacking L15." J Biol Chem 265(27);16676-82. PMID: 2204629

Freedman87: Freedman LP, Zengel JM, Archer RH, Lindahl L (1987). "Autogenous control of the S10 ribosomal protein operon of Escherichia coli: genetic dissection of transcriptional and posttranscriptional regulation." Proc Natl Acad Sci U S A 84(18);6516-20. PMID: 2442760

Friesen74: Friesen JD, Fiil NP, Parker JM, Haseltine WA (1974). "A new relaxed mutant of Escherichia coli with an altered 50S ribosomal subunit." Proc Natl Acad Sci U S A 71(9);3465-9. PMID: 4610577

Friesen83: Friesen JD, Tropak M, An G (1983). "Mutations in the rpIJ leader of Escherichia coli that abolish feedback regulation." Cell 32(2);361-9. PMID: 6186394

Fu13: Fu Y, Deiorio-Haggar K, Anthony J, Meyer MM (2013). "Most RNAs regulating ribosomal protein biosynthesis in Escherichia coli are narrowly distributed to Gammaproteobacteria." Nucleic Acids Res 41(6);3491-503. PMID: 23396277

Fuenteun75: Fuenteun J, Monier R, Garrett R, Le Bret M, Le Pecq JB (1975). "Effect of 50 S subunit proteins L5, L18 and L25 on the fluorescence of 5 S RNA-bound ethidium bromide." J Mol Biol 93(4);535-41. PMID: 1095766

Gabashvili01: Gabashvili IS, Gregory ST, Valle M, Grassucci R, Worbs M, Wahl MC, Dahlberg AE, Frank J (2001). "The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22." Mol Cell 8(1);181-8. PMID: 11511371

Gagnon10: Gagnon MG, Boutorine YI, Steinberg SV (2010). "Recurrent RNA motifs as probes for studying RNA-protein interactions in the ribosome." Nucleic Acids Res 38(10);3441-53. PMID: 20139416

Ganoza85: Ganoza MC, Zahid N, Baxter RM (1985). "Stimulation of peptidyltransferase reactions by a soluble protein." Eur J Biochem 146(2);287-94. PMID: 3881259

Gao03a: Gao H, Sengupta J, Valle M, Korostelev A, Eswar N, Stagg SM, Van Roey P, Agrawal RK, Harvey SC, Sali A, Chapman MS, Frank J (2003). "Study of the structural dynamics of the E coli 70S ribosome using real-space refinement." Cell 113(6);789-801. PMID: 12809609

Garrett79: Garrett RA, Noller HF (1979). "Structures of complexes of 5S RNA with ribosomal proteins L5, L18 and L25 from Escherichia coli: identification of kethoxal-reactive sites on the 5S RNA." J Mol Biol 132(4);637-48. PMID: 393829

Gast76: Gast WH, Leberman R (1976). "Release of certain ribosomal proteins from 70-S Escherichia coli ribosomes by mild ribonuclease digestion." Biochim Biophys Acta 432(1);98-103. PMID: 769834

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

GauntKlopfer75: Gaunt-Klopfer M, Erdmann VA (1975). "ATPase and GTPase activities associated with the 5-S RNA-protein complex of Escherichia coli ribosomes." Biochim Biophys Acta 390(2);226-30. PMID: 239743

Ge12: Ge W, Wolf A, Feng T, Ho CH, Sekirnik R, Zayer A, Granatino N, Cockman ME, Loenarz C, Loik ND, Hardy AP, Claridge TD, Hamed RB, Chowdhury R, Gong L, Robinson CV, Trudgian DC, Jiang M, Mackeen MM, McCullagh JS, Gordiyenko Y, Thalhammer A, Yamamoto A, Yang M, Liu-Yi P, Zhang Z, Schmidt-Zachmann M, Kessler BM, Ratcliffe PJ, Preston GM, Coleman ML, Schofield CJ (2012). "Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans." Nat Chem Biol 8(12);960-2. PMID: 23103944

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Gewirth87: Gewirth DT, Abo SR, Leontis NB, Moore PB (1987). "Secondary structure of 5S RNA: NMR experiments on RNA molecules partially labeled with nitrogen-15." Biochemistry 26(16);5213-20. PMID: 2444255

Gewirth88: Gewirth DT, Moore PB (1988). "Exploration of the L18 binding site on 5S RNA by deletion mutagenesis." Nucleic Acids Res 16(22);10717-32. PMID: 3060848

Geyl77: Geyl D, Bock A, Wittmann HG (1977). "Cold-sensitive growth of a mutant of Escherichia coli with an altered ribosomal protein S8: analysis of revertants." Mol Gen Genet 152(3);331-6. PMID: 327286

Gimautdinova: Gimautdinova OI, Karpova GG, Kozyreva NA "[Affinity labeling of ribosomes from Escherichia coli with 4-(N-2-chloroethyl-N-methylamino) benzyl-5'-phosphamides of oligouridylates of different length]." Mol Biol (Mosk) 16(4);752-62. PMID: 6750359

Gimautdinova81: Gimautdinova OI, Karpova GG, Knorre DG, Kobetz ND (1981). "The proteins of the messenger RNA binding site of Escherichia coli ribosomes." Nucleic Acids Res 9(14);3465-81. PMID: 7024914

Gimautdinova85: Gimautdinova OI, Karpova GG, Knorre DG, Frolova SB (1985). "Direct cross-linking of heptauridilate to E. coli ribosomes by water-soluble carbodiimide in the complex stabilized by codon-anticodon interaction at both A- and P-sites." FEBS Lett 185(2);221-5. PMID: 3888673

Giocanti80: Giocanti N, Ekert B (1980). "Radiochemical cross-linking of proteins to RNA within ribosomal subunits from E. colil MRE 600." Int J Radiat Biol Relat Stud Phys Chem Med 38(1);63-82. PMID: 6998892

Giri79: Giri L, Franz A, Dijk J (1979). "Shapes of proteins L1, L9, L25, and L30 from the 50S subunit of the Escherichia coli ribosome, determined by hydrodynamic studies." Biochemistry 18(12);2520-5. PMID: 375974

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Gordiyenko08: Gordiyenko Y, Deroo S, Zhou M, Videler H, Robinson CV (2008). "Acetylation of L12 increases interactions in the Escherichia coli ribosomal stalk complex." J Mol Biol 380(2);404-14. PMID: 18514735

Goringer86: Goringer HU, Wagner R (1986). "Construction and functional analysis of ribosomal 5S RNA from Escherichia coli with single base changes in the ribosomal protein binding sites." Biol Chem Hoppe Seyler 367(8);769-80. PMID: 2429677

Goringer88: Goringer HU, Wagner R (1988). "5S RNA structure and function." Methods Enzymol 164;721-47. PMID: 3071691

Gotz89: Gotz F, Fleischer C, Pon CL, Gualerzi CO (1989). "Subunit association defects in Escherichia coli ribosome mutants lacking proteins S20 and L11." Eur J Biochem 183(1);19-24. PMID: 2666133

Gourse81: Gourse RL, Thurlow DL, Gerbi SA, Zimmermann RA (1981). "Specific binding of a prokaryotic ribosomal protein to a eukaryotic ribosomal RNA: implications for evolution and autoregulation." Proc Natl Acad Sci U S A 78(5);2722-6. PMID: 6265904

Graifer89: Graifer DM, Babkina GT, Matasova NB, Vladimirov SN, Karpova GG, Vlassov VV (1989). "Structural arrangement of tRNA binding sites on Escherichia coli ribosomes, as revealed from data on affinity labelling with photoactivatable tRNA derivatives." Biochim Biophys Acta 1008(2);146-56. PMID: 2660905

Gray73: Gray PN, Bellemare G, Monier R, Garrett RA, Stoffler G (1973). "Identification of the nucleotide sequences involved in the interaction between Escherichia coli 5 RNA and specific 50 S subunit proteins." J Mol Biol 77(1);133-52. PMID: 4588880

Gregory99: Gregory ST, Dahlberg AE (1999). "Erythromycin resistance mutations in ribosomal proteins L22 and L4 perturb the higher order structure of 23 S ribosomal RNA." J Mol Biol 289(4);827-34. PMID: 10369764

Griaznova00: Griaznova O, Traut RR (2000). "Deletion of C-terminal residues of Escherichia coli ribosomal protein L10 causes the loss of binding of one L7/L12 dimer: ribosomes with one L7/L12 dimer are active." Biochemistry 39(14);4075-81. PMID: 10747797

Gu03b: Gu SQ, Peske F, Wieden HJ, Rodnina MV, Wintermeyer W (2003). "The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome." RNA 9(5);566-73. PMID: 12702815

Gudkov78: Gudkov AT, Tumanova LG, Venyaminov SY, Khechinashvilli NN (1978). "Stoichiometry and properties of the complex between ribosomal proteins L7 and L10 in solution." FEBS Lett 93(2);215-8. PMID: 361431

Guerin81: Guerin MF, Hayes DH, Nierhaus KH (1981). "Effects of partial deproteinization on the functional properties of 50S ribosomal subunits of E. coli." Biochimie 63(8-9);699-707. PMID: 7030408

Guillier02: Guillier M, Allemand F, Raibaud S, Dardel F, Springer M, Chiaruttini C (2002). "Translational feedback regulation of the gene for L35 in Escherichia coli requires binding of ribosomal protein L20 to two sites in its leader mRNA: a possible case of ribosomal RNA-messenger RNA molecular mimicry." RNA 8(7);878-89. PMID: 12166643

Guillier05: Guillier M, Allemand F, Graffe M, Raibaud S, Dardel F, Springer M, Chiaruttini C (2005). "The N-terminal extension of Escherichia coli ribosomal protein L20 is important for ribosome assembly, but dispensable for translational feedback control." RNA 11(5);728-38. PMID: 15840820

Guillier05a: Guillier M, Allemand F, Dardel F, Royer CA, Springer M, Chiaruttini C (2005). "Double molecular mimicry in Escherichia coli: binding of ribosomal protein L20 to its two sites in mRNA is similar to its binding to 23S rRNA." Mol Microbiol 56(6);1441-56. PMID: 15916597

Gulle88: Gulle H, Hoppe E, Osswald M, Greuer B, Brimacombe R, Stoffler G (1988). "RNA-protein cross-linking in Escherichia coli 50S ribosomal subunits; determination of sites on 23S RNA that are cross-linked to proteins L2, L4, L24 and L27 by treatment with 2-iminothiolane." Nucleic Acids Res 16(3);815-32. PMID: 3278299

HaentjensSitri08: Haentjens-Sitri J, Allemand F, Springer M, Chiaruttini C (2008). "A competition mechanism regulates the translation of the Escherichia coli operon encoding ribosomal proteins L35 and L20." J Mol Biol 375(3);612-25. PMID: 18037435

Hamman96: Hamman BD, Oleinikov AV, Jokhadze GG, Bochkariov DE, Traut RR, Jameson DM (1996). "Tetramethylrhodamine dimer formation as a spectroscopic probe of the conformation of Escherichia coli ribosomal protein L7/L12 dimers." J Biol Chem 271(13);7568-73. PMID: 8631789

Hansen82: Hansen FG, Hansen EB, Atlung T (1982). "The nucleotide sequence of the dnaA gene promoter and of the adjacent rpmH gene, coding for the ribosomal protein L34, of Escherichia coli." EMBO J 1982;1(9);1043-8. PMID: 6329723

Hanson03: Hanson CL, Fucini P, Ilag LL, Nierhaus KH, Robinson CV (2003). "Dissociation of intact Escherichia coli ribosomes in a mass spectrometer. Evidence for conformational change in a ribosome elongation factor G complex." J Biol Chem 278(2);1259-67. PMID: 12409297

Hauser12: Hauser R, Pech M, Kijek J, Yamamoto H, Titz B, Naeve F, Tovchigrechko A, Yamamoto K, Szaflarski W, Takeuchi N, Stellberger T, Diefenbacher ME, Nierhaus KH, Uetz P (2012). "RsfA (YbeB) Proteins Are Conserved Ribosomal Silencing Factors." PLoS Genet 8(7);e1002815. PMID: 22829778

Hensley11: Hensley MP, Tierney DL, Crowder MW (2011). "Zn(II) binding to Escherichia coli 70S ribosomes." Biochemistry 50(46);9937-9. PMID: 22026583

Hensley12: Hensley MP, Gunasekera TS, Easton JA, Sigdel TK, Sugarbaker SA, Klingbeil L, Breece RM, Tierney DL, Crowder MW (2012). "Characterization of Zn(II)-responsive ribosomal proteins YkgM and L31 in E. coli." J Inorg Biochem 111;164-72. PMID: 22196016

Herbst94: Herbst KL, Nichols LM, Gesteland RF, Weiss RB (1994). "A mutation in ribosomal protein L9 affects ribosomal hopping during translation of gene 60 from bacteriophage T4." Proc Natl Acad Sci U S A 91(26);12525-9. PMID: 7809071

Herfurth95: Herfurth E, Wittmann-Liebold B (1995). "Determination of peptide regions exposed at the surface of the bacterial ribosome with antibodies against synthetic peptides." Biol Chem Hoppe Seyler 376(2);81-90. PMID: 7794529

Hernandez77: Hernandez F, Vazquez D, Ballesta JP (1977). "Functional roles of 50-S ribosomal proteins." Eur J Biochem 78(1);267-72. PMID: 334534

Herold86: Herold M, Nowotny V, Dabbs ER, Nierhaus KH (1986). "Assembly analysis of ribosomes from a mutant lacking the assembly-initiator protein L24: lack of L24 induces temperature sensitivity." Mol Gen Genet 203(2);281-7. PMID: 3526091

Herold87: Herold M, Nierhaus KH (1987). "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes." J Biol Chem 262(18);8826-33. PMID: 3298242

Herr00: Herr AJ, Gesteland RF, Atkins JF (2000). "One protein from two open reading frames: mechanism of a 50 nt translational bypass." EMBO J 19(11);2671-80. PMID: 10835364

Herr01: Herr AJ, Nelson CC, Wills NM, Gesteland RF, Atkins JF (2001). "Analysis of the roles of tRNA structure, ribosomal protein L9, and the bacteriophage T4 gene 60 bypassing signals during ribosome slippage on mRNA." J Mol Biol 309(5);1029-48. PMID: 11399077

Highland75a: Highland JH, Howard GA, Ochsner E, Hasenbank R, Gordon J, Stoffler G (1975). "Identification of a ribosomal protein necessary for thiostrepton binding to Escherichia coli ribosomes." J Biol Chem 250(3);1141-5. PMID: 1089652

Hindennach71a: Hindennach I, Kaltschmidt E, Wittmann HG (1971). "Ribosomal proteins. Isolation of proteins from 50S ribosomal subunits of Escherichia coli." Eur J Biochem 23(1);12-6. PMID: 4942547

Houben05: Houben EN, Zarivach R, Oudega B, Luirink J (2005). "Early encounters of a nascent membrane protein: specificity and timing of contacts inside and outside the ribosome." J Cell Biol 170(1);27-35. PMID: 15983062

Huang90a: Huang SC, Panagiotidis CA, Canellakis ES (1990). "Transcriptional effects of polyamines on ribosomal proteins and on polyamine-synthesizing enzymes in Escherichia coli." Proc Natl Acad Sci U S A 87(9);3464-8. PMID: 2185470

Huber84: Huber PW, Wool IG (1984). "Nuclease protection analysis of ribonucleoprotein complexes: use of the cytotoxic ribonuclease alpha-sarcin to determine the binding sites for Escherichia coli ribosomal proteins L5, L18, and L25 on 5S rRNA." Proc Natl Acad Sci U S A 81(2);322-6. PMID: 6364140

Hui82: Hui I, Maltman K, Little R, Hastrup S, Johnsen M, Fiil N, Dennis P (1982). "Insertions of transposon Tn5 into ribosomal protein PNA polymerase operons." J Bacteriol 152(3);1022-32. PMID: 6292159

Hwang06: Hwang J, Inouye M (2006). "The tandem GTPase, Der, is essential for the biogenesis of 50S ribosomal subunits in Escherichia coli." Mol Microbiol 61;1660-1672. PMID: 16930151

Ikegami05: Ikegami A, Nishiyama K, Matsuyama S, Tokuda H (2005). "Disruption of rpmJ encoding ribosomal protein L36 decreases the expression of secY upstream of the spc operon and inhibits protein translocation in Escherichia coli." Biosci Biotechnol Biochem 69(8);1595-602. PMID: 16116291

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Isono77: Isono K, Cumberlidge AG, Isono S (1977). "Further temperature-sensitive mutants of Escherichia coli with altered ribosomal proteins." Mol Gen Genet 152(3);239-43. PMID: 327280

Isono78: Isono S, Isono K, Hirota Y (1978). "Mutations affecting the structural genes and the genes coding for modifying enzymes for ribosomal proteins in Escherichia coli." MGG Molecular & General Genetics 165(1);15-20.

Isono78a: Isono K, Kitakawa M (1978). "Cluster of ribosomal protein genes in Escherichia coli containing genes for proteins S6, S18, and L9." Proc Natl Acad Sci U S A 75(12);6163-7. PMID: 366612

Ito05: Ito K (2005). "Ribosome-based protein folding systems are structurally divergent but functionally universal across biological kingdoms." Mol Microbiol 57(2);313-7. PMID: 15978066

Ito84: Ito K, Cerretti DP, Nashimoto H, Nomura M (1984). "Characterization of an amber mutation in the structural gene for ribosomal protein L15, which impairs the expression of the protein export gene, secY, in Escherichia coli." EMBO J 3(10);2319-24. PMID: 6389119

Jaskunas77: Jaskunas SR, Fallon AM, Nomura M (1977). "Identification and organization of ribosomal protein genes of Escherichia coli carried by lambdafus2 transducing phage." J Biol Chem 252(20);7323-36. PMID: 332690

Jaskunas77a: Jaskunas SR, Nomura M (1977). "Organization of ribosomal protein genes of Escherichia coli as analyzed by polar insertion mutations." J Biol Chem 252(20);7337-43. PMID: 332691

Jaynes78: Jaynes EN, Grant PG, Giangrande G, Wieder R, Cooperman BS (1978). "Photoinduced affinity labeling of the Escherichia coli ribosome puromycin site." Biochemistry 17(4);561-9. PMID: 341968

Jenvert07: Jenvert RM, Schiavone LH (2007). "The flexible N-terminal domain of ribosomal protein L11 from Escherichia coli is necessary for the activation of stringent factor." J Mol Biol 365(3);764-72. PMID: 17095013

Jerez80: Jerez C, Weissbach H (1980). "Methylation of newly synthesized ribosomal protein L11 in a DNA-directed in vitro system." J Biol Chem 255(18);8706-10. PMID: 6447699

Johnsen82: Johnsen M, Christensen T, Dennis PP, Fiil NP (1982). "Autogenous control: ribosomal protein L10-L12 complex binds to the leader sequence of its mRNA." EMBO J 1(8);999-1004. PMID: 6765237

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kaczanowska07: Kaczanowska M, Ryden-Aulin M (2007). "Ribosome biogenesis and the translation process in Escherichia coli." Microbiol Mol Biol Rev 71(3);477-94. PMID: 17804668

Kakegawa86: Kakegawa T, Sato E, Hirose S, Igarashi K (1986). "Polyamine binding sites on Escherichia coli ribosomes." Arch Biochem Biophys 251(2);413-20. PMID: 3541786

Kaltschmidt70: Kaltschmidt E, Wittmann HG (1970). "Ribosomal proteins. XII. Number of proteins in small and large ribosomal subunits of Escherichia coli as determined by two-dimensional gel electrophoresis." Proc Natl Acad Sci U S A 67(3);1276-82. PMID: 4922286

Kamp83: Kamp RM, Yao ZJ, Wittmann-Liebold B (1983). "Direct micro-sequence analysis of peptides from Escherichia coli ribosomal proteins S11, L9 and L29 after separation by reversed phase chromatography." Hoppe Seylers Z Physiol Chem 364(2);141-55. PMID: 6341200

Kargel87: Kargel HJ, Stahl J, Gross B, Knespel S, Bielka H, Saarma M (1987). "Studies on interaction of 5 S RNA with ribosomal proteins." FEBS Lett 220(1);126-8. PMID: 3301408

Kashiwagi87: Kashiwagi K, Igarashi K (1987). "Nonspecific inhibition of Escherichia coli ornithine decarboxylase by various ribosomal proteins: detection of a new ribosomal protein possessing strong antizyme activity." Biochim Biophys Acta 1987;911(2);180-90. PMID: 3542048

Katayama02: Katayama A, Tsujii A, Wada A, Nishino T, Ishihama A (2002). "Systematic search for zinc-binding proteins in Escherichia coli." Eur J Biochem 269(9);2403-13. PMID: 11985624

Kazemie75: Kazemie M (1975). "The importance of Escherichia coli ribosomal proteins L1, L11 and L16 for the association of ribosomal subunits and the formation of the 70-S initiation complex." Eur J Biochem 58(2);501-10. PMID: 1102306

Kazemie76: Kazemie M (1976). "Binding of aminoacyl-tRNA to reconstituted subparticles of Escherichia coli large ribosomal subunits." Eur J Biochem 67(2);373-8. PMID: 786630

Kearney87: Kearney KR, Nomura M (1987). "Secondary structure of the autoregulatory mRNA binding site of ribosomal protein L1." Mol Gen Genet 210(1);60-8. PMID: 2448590

Kenny75: Kenny JW, Sommer A, Traut RR (1975). "Cross-linking studies on the 50 S ribosomal subunit of Escherichia coli with methyl 4-mercaptobutyrimidate." J Biol Chem 250(24);9434-6. PMID: 1104622

Kim01g: Kim DF, Semrad K, Green R (2001). "Analysis of the active site of the ribosome by site-directed mutagenesis." Cold Spring Harb Symp Quant Biol 66;119-26. PMID: 12762014

Kime81: Kime MJ, Ratcliffe RG, Moore PB, Williams RJ (1981). "A proton NMR study of ribosomal protein L25 from Escherichia coli." Eur J Biochem 116(2);269-76. PMID: 7018905

Kime83: Kime MJ, Moore PB (1983). "Nuclear Overhauser experiments at 500 MHz on the downfield proton spectra of 5S ribonucleic acid and its complex with ribosomal protein L25." Biochemistry 22(11);2622-9. PMID: 6347250

Kime84: Kime MJ, Moore PB (1984). "Escherichia coli ribosomal 5S RNA-protein L25 nucleoprotein complex: effects of RNA binding on the protein structure and the nature of the interaction." Biochemistry 23(8);1688-95. PMID: 6372859

Kime84a: Kime MJ (1984). "Assignment of resonances of exchangeable protons in the NMR spectrum of the complex formed by Escherichia coli ribosomal protein L25 and uniformly nitrogen-15 enriched 5 S RNA fragment." FEBS Lett 175(2);259-62. PMID: 6383867

Kirillov02: Kirillov SV, Wower J, Hixson SS, Zimmermann RA (2002). "Transit of tRNA through the Escherichia coli ribosome: cross-linking of the 3' end of tRNA to ribosomal proteins at the P and E sites." FEBS Lett 514(1);60-6. PMID: 11904182

Kitakawa80: Kitakawa M, Blumenthal L, Isono K (1980). "Isolation and characterization of specialized transducing lambda phages carrying ribosomal protein genes of Escherichia coli." Mol Gen Genet 180(2);343-9. PMID: 6450872

Korepanov07: Korepanov AP, Gongadze GM, Garber MB, Court DL, Bubunenko MG (2007). "Importance of the 5 S rRNA-binding ribosomal proteins for cell viability and translation in Escherichia coli." J Mol Biol 366(4);1199-208. PMID: 17198710

Korepanov12: Korepanov AP, Korobeinikova AV, Shestakov SA, Garber MB, Gongadze GM (2012). "Protein L5 is crucial for in vivo assembly of the bacterial 50S ribosomal subunit central protuberance." Nucleic Acids Res 40(18);9153-9. PMID: 22821559

Kostopoulou12: Kostopoulou ON, Petropoulos AD, Dinos GP, Choli-Papadopoulou T, Kalpaxis DL (2012). "Investigating the entire course of telithromycin binding to Escherichia coli ribosomes." Nucleic Acids Res 40(11);5078-87. PMID: 22362747

Kovacs09: Kovacs D, Rakacs M, Agoston B, Lenkey K, Semrad K, Schroeder R, Tompa P (2009). "Janus chaperones: assistance of both RNA- and protein-folding by ribosomal proteins." FEBS Lett 583(1);88-92. PMID: 19071121

Kramer02: Kramer G, Rauch T, Rist W, Vorderwulbecke S, Patzelt H, Schulze-Specking A, Ban N, Deuerling E, Bukau B (2002). "L23 protein functions as a chaperone docking site on the ribosome." Nature 419(6903);171-4. PMID: 12226666

Krassnigg78: Krassnigg F, Erdmann VA, Fasold H (1978). "The synthesis of a photoreactive puromycin analogue and its application for labeling proteins in the 50-S subunit of Escherichia coli ribosomes." Eur J Biochem 87(3);439-43. PMID: 354931

Kuhberger79: Kuhberger R, Piepersberg W, Petzet A, Buckel P, Bock A (1979). "Alteration of ribosomal protein L6 in gentamicin-resistant strains of Escherichia coli. Effects on fidelity of protein synthesis." Biochemistry 18(1);187-93. PMID: 369594

Kuhlenkoetter11: Kuhlenkoetter S, Wintermeyer W, Rodnina MV (2011). "Different substrate-dependent transition states in the active site of the ribosome." Nature 476(7360);351-4. PMID: 21804565

Kuroda01: Kuroda A, Nomura K, Ohtomo R, Kato J, Ikeda T, Takiguchi N, Ohtake H, Kornberg A (2001). "Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli." Science 293(5530);705-8. PMID: 11474114

Lambert81: Lambert JM, Traut RR (1981). "The subunit interface of the Escherichia coli ribosome. Identification of proteins at the interface between the 30 S and 50 S subunits by crosslinking with 2-iminothiolane." J Mol Biol 149(3);451-76. PMID: 7031269

Lancaster08: Lancaster L, Lambert NJ, Maklan EJ, Horan LH, Noller HF (2008). "The sarcin-ricin loop of 23S rRNA is essential for assembly of the functional core of the 50S ribosomal subunit." RNA 14(10);1999-2012. PMID: 18755834

Lane92: Lane BG, Ofengand J, Gray MW (1992). "Pseudouridine in the large-subunit (23 S-like) ribosomal RNA. The site of peptidyl transfer in the ribosome?." FEBS Lett 302(1);1-4. PMID: 1587345

Larrinua79: Larrinua I, Delihas N (1979). "Accessibility of guanine at position 44 in the invariant sequence 5'CCG44AAC3' of Escherichia coli 5S RNA to reaction with kethoxal." Proc Natl Acad Sci U S A 76(9);4400-4. PMID: 388442

Lawrence08a: Lawrence MG, Lindahl L, Zengel JM (2008). "Effects on translation pausing of alterations in protein and RNA components of the ribosome exit tunnel." J Bacteriol 190(17);5862-9. PMID: 18586934

Lederer77: Lederer F, Alix JH, Hayes D (1977). "N-Trimethylalanine, a novel blocking group, found in E. coli ribosomal protein L11." Biochem Biophys Res Commun 77(2);470-80. PMID: 332162

Leffers88: Leffers H, Egebjerg J, Andersen A, Christensen T, Garrett RA (1988). "Domain VI of Escherichia coli 23 S ribosomal RNA. Structure, assembly and function." J Mol Biol 204(3);507-22. PMID: 2465415

Leontis86: Leontis NB, Moore PB (1986). "Imino proton exchange in the 5S RNA of Escherichia coli and its complex with protein L25 at 490 MHz." Biochemistry 25(19);5736-44. PMID: 3535886

Leontis86a: Leontis NB, Ghosh P, Moore PB (1986). "Effect of magnesium ion on the structure of the 5S RNA from Escherichia coli. An imino proton magnetic resonance study of the helix I, IV, and V regions of the molecule." Biochemistry 25(23);7386-92. PMID: 3542026

Lesage90: Lesage P, Truong HN, Graffe M, Dondon J, Springer M (1990). "Translated translational operator in Escherichia coli. Auto-regulation in the infC-rpmI-rplT operon." J Mol Biol 213(3);465-75. PMID: 2191140

Lesage92: Lesage P, Chiaruttini C, Graffe M, Dondon J, Milet M, Springer M (1992). "Messenger RNA secondary structure and translational coupling in the Escherichia coli operon encoding translation initiation factor IF3 and the ribosomal proteins, L35 and L20." J Mol Biol 228(2);366-86. PMID: 1453449

Lhoest77: Lhoest J, Colson C (1977). "Genetics of ribosomal protein methylation in Escherichia coli. II. A mutant lacking a new type of methylated amino acid, N5-methylglutamine, in protein L3." Mol Gen Genet 154(2);175-80. PMID: 331083

Lhoest81: Lhoest J, Colson C (1981). "Cold-sensitive ribosome assembly in an Escherichia coli mutant lacking a single methyl group in ribosomal protein L3." Eur J Biochem 121(1);33-7. PMID: 6173216

Li96e: Li X, Lindahl L, Zengel JM (1996). "Ribosomal protein L4 from Escherichia coli utilizes nonidentical determinants for its structural and regulatory functions." RNA 2(1);24-37. PMID: 8846294

Liang99: Liang ST, Ehrenberg M, Dennis P, Bremer H (1999). "Decay of rplN and lacZ mRNA in Escherichia coli." J Mol Biol 288(4);521-38. PMID: 10329160

Lieberman00: Lieberman KR, Firpo MA, Herr AJ, Nguyenle T, Atkins JF, Gesteland RF, Noller HF (2000). "The 23 S rRNA environment of ribosomal protein L9 in the 50 S ribosomal subunit." J Mol Biol 297(5);1129-43. PMID: 10764578

Lieberman98: Lieberman KR, Noller HF (1998). "Ribosomal protein L15 as a probe of 50 S ribosomal subunit structure." J Mol Biol 284(5);1367-78. PMID: 9878356

Liebman95: Liebman SW, Chernoff YO, Liu R (1995). "The accuracy center of a eukaryotic ribosome." Biochem Cell Biol 73(11-12);1141-9. PMID: 8722031

Lind78: Lind AIa, Villems RL, Uuskiula LS (1978). "[5S RNA: structure and function]." Usp Sovrem Biol 86(1);3-18. PMID: 152015

Lindahl83: Lindahl L, Archer R, Zengel JM (1983). "Transcription of the S10 ribosomal protein operon is regulated by an attenuator in the leader." Cell 33(1);241-8. PMID: 6380754

Lindahl90: Lindahl L, Zengel JM (1990). "Autogenous control is not sufficient to ensure steady-state growth rate-dependent regulation of the S10 ribosomal protein operon of Escherichia coli." J Bacteriol 172(1);305-9. PMID: 2152906

Liou75: Liou YF, Yoshikawa M, Tanaka N (1975). "Alteration of ribosomal protein L5 in a thiopeptin-resistant mutant of Escherichia coli." Biochem Biophys Res Commun 65(3);1096-101. PMID: 1098662

Little81a: Little R, Fiil NP, Dennis PP (1981). "Transcriptional and post-transcriptional control of ribosomal protein and ribonucleic acid polymerase genes." J Bacteriol 147(1);25-35. PMID: 7016843

Littlechild77: Littlechild J, Dijk J, Garrett RA (1977). "The identification of new RNA-binding proteins in the Escherichia coli ribosome." FEBS Lett 74(2);292-4. PMID: 321250

Long06: Long KS, Hansen LH, Jakobsen L, Vester B (2006). "Interaction of pleuromutilin derivatives with the ribosomal peptidyl transferase center." Antimicrob Agents Chemother 50(4);1458-62. PMID: 16569865

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Lotti89: Lotti M, Noah M, Stoffler-Meilicke M, Stoffler G (1989). "Localization of proteins L4, L5, L20 and L25 on the ribosomal surface by immuno-electron microscopy." Mol Gen Genet 216(2-3);245-53. PMID: 2664451

Lovmar09: Lovmar M, Nilsson K, Lukk E, Vimberg V, Tenson T, Ehrenberg M (2009). "Erythromycin resistance by L4/L22 mutations and resistance masking by drug efflux pump deficiency." EMBO J 28(6);736-44. PMID: 19197244

Lu00: Lu M, Steitz TA (2000). "Structure of Escherichia coli ribosomal protein L25 complexed with a 5S rRNA fragment at 1.8-A resolution." Proc Natl Acad Sci U S A 97(5);2023-8. PMID: 10696113

Maassen74: Maassen JA, Moller W (1974). "Identification by photo-affinity labeling of the proteins in Escherichia coli ribosomes involved in elongation factor G-dependent GDP binding." Proc Natl Acad Sci U S A 71(4);1277-80. PMID: 4598298

Macek08: Macek B, Gnad F, Soufi B, Kumar C, Olsen JV, Mijakovic I, Mann M (2008). "Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation." Mol Cell Proteomics 7(2);299-307. PMID: 17938405

Maeder05: Maeder C, Draper DE (2005). "A small protein unique to bacteria organizes rRNA tertiary structure over an extensive region of the 50 S ribosomal subunit." J Mol Biol 354(2);436-46. PMID: 16246363

Maeder06: Maeder C, Conn GL, Draper DE (2006). "Optimization of a ribosomal structural domain by natural selection." Biochemistry 45(21);6635-43. PMID: 16716074

Maguire01: Maguire BA, Manuilov AV, Zimmermann RA (2001). "Differential effects of replacing Escherichia coli ribosomal protein L27 with its homologue from Aquifex aeolicus." J Bacteriol 183(22);6565-72. PMID: 11673426

Maguire05: Maguire BA, Beniaminov AD, Ramu H, Mankin AS, Zimmermann RA (2005). "A protein component at the heart of an RNA machine: the importance of protein l27 for the function of the bacterial ribosome." Mol Cell 20(3);427-35. PMID: 16285924

Maguire97: Maguire BA, Wild DG (1997). "The roles of proteins L28 and L33 in the assembly and function of Escherichia coli ribosomes in vivo." Mol Microbiol 23(2);237-45. PMID: 9044258

Maguire97a: Maguire BA, Wild DG (1997). "Mutations in the rpmBG operon of Escherichia coli that affect ribosome assembly." J Bacteriol 1997;179(8);2486-93. PMID: 9098043

Maguire97b: Maguire BA, Wild DG (1997). "The effects of mutations in the rpmB,G operon of Escherichia coli on ribosome assembly and ribosomal protein synthesis." Biochim Biophys Acta 1353(2);137-47. PMID: 9294008

Maimets: Maimets TO, Ustav MB, Remme IaL, Villems RL "[Protein L16 of the Escherichia coli ribosome: possible role in protein biosynthesis]." Mol Biol (Mosk) 18(6);1597-605. PMID: 6084168

Maimets81: Maimets TO, Ustav MB, Villems RL, Saarma MIu, Lind AIa (1981). "[Binding of Escherichia coli 50S ribosomal subunit proteins with two large 5S RNA fragments]." Mol Biol (Mosk) 15(3);569-74. PMID: 7019670

Maimets84: Maimets T, Remme J, Villems R (1984). "Ribosomal protein L16 binds to the 3'-end of transfer RNA." FEBS Lett 166(1);53-6. PMID: 6363130

Makarov93: Makarov EM, Oleinikov AV, Zecherle GN, Traut RR (1993). "Zero-length cross-linking of the C-terminal domain of Escherichia coli ribosomal protein L7/L12 to L10 in the ribosome and in the (L7/L12)4-L10 pentameric complex." Biochimie 75(11);963-9. PMID: 8123703

Makarova01a: Makarova KS, Ponomarev VA, Koonin EV (2001). "Two C or not two C: recurrent disruption of Zn-ribbons, gene duplication, lineage-specific gene loss, and horizontal gene transfer in evolution of bacterial ribosomal proteins." Genome Biol 2(9);RESEARCH 0033. PMID: 11574053

Malhotra98: Malhotra A, Penczek P, Agrawal RK, Gabashvili IS, Grassucci RA, Junemann R, Burkhardt N, Nierhaus KH, Frank J (1998). "Escherichia coli 70 S ribosome at 15 A resolution by cryo-electron microscopy: localization of fMet-tRNAfMet and fitting of L1 protein." J Mol Biol 280(1);103-16. PMID: 9653034

Maly80: Maly P, Rinke J, Ulmer E, Zwieb C, Brimacombe R (1980). "Precise localization of the site of cross-linking between protein L4 and 23S ribonucleic acid induced by mild ultraviolet irradiation of Escherichia coli 50S ribosomal subunits." Biochemistry 19(18);4179-88. PMID: 6998491

Maly83: Maly P, Wower J, Zobawa M, Brimacombe R (1983). "Identification of tyrosine residues that are susceptible to lactoperoxidase-catalyzed iodination on the surface of Escherichia coli 50s ribosomal subunits or 70s ribosomes." Biochemistry 22(13);3157-62. PMID: 6349680

Marquardt79: Marquardt O, Roth HE, Wystup G, Nierhaus KH (1979). "Binding of Escherichia coli ribosomal proteins to 23S RNA under reconstitution conditions for the 50S subunit." Nucleic Acids Res 6(11);3641-50. PMID: 386275

Matadeen99: Matadeen R, Patwardhan A, Gowen B, Orlova EV, Pape T, Cuff M, Mueller F, Brimacombe R, van Heel M (1999). "The Escherichia coli large ribosomal subunit at 7.5 A resolution." Structure 7(12);1575-83. PMID: 10647188

Mattheakis88: Mattheakis LC, Nomura M (1988). "Feedback regulation of the spc operon in Escherichia coli: translational coupling and mRNA processing." J Bacteriol 170(10);4484-92. PMID: 3049533

McCaughan84: McCaughan KK, Ward CD, Trotman CN, Tate WP (1984). "The ribosomal binding domain for the bacterial release factors RF-1, RF-2 and RF-3." FEBS Lett 175(1);90-4. PMID: 6383864

Meng12: Meng J, Kanzaki G, Meas D, Lam CK, Crummer H, Tain J, Xu HH (2012). "A genome-wide inducible phenotypic screen identifies antisense RNA constructs silencing Escherichia coli essential genes." FEMS Microbiol Lett 329(1);45-53. PMID: 22268863

Merianos04: Merianos HJ, Wang J, Moore PB (2004). "The structure of a ribosomal protein S8/spc operon mRNA complex." RNA 10(6);954-64. PMID: 15146079

Metspalu81: Metspalu E, Maimets T, Ustav M, Villems R (1981). "A quaternary complex consisting of two molecules of tRNA and ribosomal proteins L2 and L17." FEBS Lett 132(1);105-8. PMID: 6170527

Metspalu82: Metspalu E, Ustav M, Maimets T, Villems R (1982). "The composition and properties of the Escherichia coli 5-S RNA-protein complex." Eur J Biochem 121(2);383-9. PMID: 6174328

Mitchell93b: Mitchell P, Stade K, Osswald M, Brimacombe R (1993). "Site-directed cross-linking studies on the E. coli tRNA-ribosome complex: determination of sites labelled with an aromatic azide attached to the variable loop or aminoacyl group of tRNA." Nucleic Acids Res 21(4);887-96. PMID: 7680805

Moore83: Moore PB, Kime MJ, Leontis NB, Abdel-Meguid SS (1983). "Physical studies on a nucleoprotein from the ribosome of E. coli." J Biomol Struct Dyn 1(2);383-94. PMID: 6401116

Moore88a: Moore PB, Abo S, Freeborn B, Gewirth DT, Leontis NB, Sun G (1988). "Preparation of 5S RNA-related materials for nuclear magnetic resonance and crystallography studies." Methods Enzymol 164;158-74. PMID: 3071660

Morrison77: Morrison CA, Tischendorf G, Stoffler G, Garrett RA (1977). "Accessibility of proteins in 50S ribosomal subunits of Escherichia coli to antibodies: an ultracentrifugation study." Mol Gen Genet 151(3);245-52. PMID: 68433

Moureau83: Moureau P, Di Giambattista M, Cocito C (1983). "The lasting ribosome alteration produced by virginiamycin M disappears upon removal of certain ribosomal proteins." Biochim Biophys Acta 739(2);164-72. PMID: 6402016

Mueller95: Mueller F, Doring T, Erdemir T, Greuer B, Junke N, Osswald M, Rinke-Appel J, Stade K, Thamm S, Brimacombe R (1995). "Getting closer to an understanding of the three-dimensional structure of ribosomal RNA." Biochem Cell Biol 73(11-12);767-73. PMID: 8721993

Muralikrishna95: Muralikrishna P, Cooperman BS (1995). "Ribosomal components neighboring the 2475 loop in Escherichia coli 50S subunits." Biochemistry 34(1);115-21. PMID: 7529559

Naaktgeboren76: Naaktgeboren N, Schrier P, Moller W, Voorma HO (1976). "The involvement of protein L11 in the joining of the 30-S initiation complex to the 50-S subunit." Eur J Biochem 62(1);117-23. PMID: 765132

Nag87: Nag B, Tewari DS, Sommer A, Olson HM, Glitz DG, Traut RR (1987). "Probing ribosome function and the location of Escherichia coli ribosomal protein L5 with a monoclonal antibody." J Biol Chem 262(20);9681-7. PMID: 3298260

Nag91: Nag B, Akella SS, Cann PA, Tewari DS, Glitz DG, Traut RR (1991). "Monoclonal antibodies to Escherichia coli ribosomal proteins L9 and L10. Effects on ribosome function and localization of L9 on the surface of the 50 S ribosomal subunit." J Biol Chem 266(33);22129-35. PMID: 1939233

Nag91a: Nag B, Glitz DG, Tewari DS, Traut RR (1991). "Probing the functional role and localization of Escherichia coli ribosomal protein L16 with a monoclonal antibody." J Biol Chem 266(17);11116-21. PMID: 2040621

Naganathan13: Naganathan A, Moore SD (2013). "Crippling the essential GTPase Der causes dependence on ribosomal protein L9." J Bacteriol 195(16);3682-91. PMID: 23772068

Naganathan15: Naganathan A, Wood MP, Moore SD (2015). "The Large Ribosomal Subunit Protein L9 Enables the Growth of EF-P Deficient Cells and Enhances Small Subunit Maturation." PLoS One 10(4);e0120060. PMID: 25879934

Nakajima99: Nakajima Y (1999). "Mechanisms of bacterial resistance to macrolide antibiotics." J Infect Chemother 5(2);61-74. PMID: 11810493

Nakatogawa02: Nakatogawa H, Ito K (2002). "The ribosomal exit tunnel functions as a discriminating gate." Cell 108(5);629-36. PMID: 11893334

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

Nesterchuk11: Nesterchuk MV, Sergiev PV, Dontsova OA (2011). "Posttranslational Modifications of Ribosomal Proteins in Escherichia coli." Acta Naturae 3(2);22-33. PMID: 22649682

Newberry78: Newberry V, Brosius J, Garrett R (1978). "Fragment of protein L18 from the Escherichia coli ribosome that contains the 5S RNA binding site." Nucleic Acids Res 5(6);1753-66. PMID: 353728

Newberry80: Newberry V, Garrett RA (1980). "The role of the basic N-terminal region of protein L18 in 5S RNA-23S RNA complex formation." Nucleic Acids Res 8(18);4131-42. PMID: 6159586

Nierhaus73: Nierhaus D, Nierhaus KH (1973). "Identification of the chloramphenicol-binding protein in Escherichia coli ribosomes by partial reconstitution." Proc Natl Acad Sci U S A 70(8);2224-8. PMID: 4365366

Nishi85: Nishi K, Dabbs ER, Schnier J (1985). "DNA sequence and complementation analysis of a mutation in the rplX gene from Escherichia coli leading to loss of ribosomal protein L24." J Bacteriol 163(3);890-4. PMID: 2993250

Nishi86: Nishi K, Schnier J (1986). "A temperature-sensitive mutant in the gene rplX for ribosomal protein L24 and its suppression by spontaneous mutations in a 23S rRNA gene of Escherichia coli." EMBO J 5(6);1373-6. PMID: 3525151

Nishi87: Nishi K, Muller M, Schnier J (1987). "Spontaneous missense mutations in the rplX gene for ribosomal protein L24 from Escherichia coli." J Bacteriol 169(10);4854-6. PMID: 3308860

Nishi88: Nishi K, Schnier J (1988). "The phenotypic suppression of a mutation in the gene rplX for ribosomal protein L24 by mutations affecting the lon gene product for protease LA in Escherichia coli K12." Mol Gen Genet 212(1);177-81. PMID: 3287098

Nowotny80: Nowotny V, Nierhaus KH (1980). "Protein L20 from the large subunit of Escherichia coli ribosomes is an assembly protein." J Mol Biol 137(4);391-9. PMID: 7021848

Nowotny82: Nowotny V, Nierhaus KH (1982). "Initiator proteins for the assembly of the 50S subunit from Escherichia coli ribosomes." Proc Natl Acad Sci U S A 79(23);7238-42. PMID: 6760192

Nowotny88: Nowotny P, Nowotny V, Voss H, Nierhaus KH (1988). "Preparation and activity measurements of deuterated 50S subunits for neutron-scattering analysis." Methods Enzymol 164;131-47. PMID: 3071658

OConnor04: O'Connor M, Gregory ST, Dahlberg AE (2004). "Multiple defects in translation associated with altered ribosomal protein L4." Nucleic Acids Res 32(19);5750-6. PMID: 15509870

Ogle05: Ogle JM, Ramakrishnan V (2005). "Structural insights into translational fidelity." Annu Rev Biochem 74;129-77. PMID: 15952884

Okada00b: Okada S, Okada T, Aimi T, Morinaga T, Itoh T (2000). "HSP70 and ribosomal protein L2: novel 5S rRNA binding proteins in Escherichia coli." FEBS Lett 485(2-3);153-6. PMID: 11094158

Olins81a: Olins PO, Nomura M (1981). "Translational regulation by ribosomal protein S8 in Escherichia coli: structural homology between rRNA binding site and feedback target on mRNA." Nucleic Acids Res 9(7);1757-64. PMID: 6262737

Olsson96: Olsson CL, Graffe M, Springer M, Hershey JW (1996). "Physiological effects of translation initiation factor IF3 and ribosomal protein L20 limitation in Escherichia coli." Mol Gen Genet 250(6);705-14. PMID: 8628231

Osswald90: Osswald M, Greuer B, Brimacombe R (1990). "Localization of a series of RNA-protein cross-link sites in the 23S and 5S ribosomal RNA from Escherichia coli, induced by treatment of 50S subunits with three different bifunctional reagents." Nucleic Acids Res 18(23);6755-60. PMID: 1702198

Osswald95: Osswald M, Doring T, Brimacombe R (1995). "The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site." Nucleic Acids Res 23(22);4635-41. PMID: 8524654

Osterberg76: Osterberg R, Sjoberg B (1976). "Small-angle x-ray scattering study of the 5S RNA binding proteins L18 and L25 from Escherichia coli ribosomes." FEBS Lett 65(1);73-6. PMID: 776688

Osterberg77: Osterberg R, Sjoberg B, Pettersson I, Liljas A, Kurland CG (1977). "Small-angle x-ray scattering study of the protein complex of L7/L12 and L10 from Escherichia coli ribosomes." FEBS Lett 73(1);22-4. PMID: 320036

Osterberg79: Osterberg R (1979). "The ternary 5-S RNA complex of proteins L 18 and L 25. A small-angle X-ray scattering titration study." Eur J Biochem 97(2);463-9. PMID: 380994

Ostergaard98: Ostergaard P, Phan H, Johansen LB, Egebjerg J, Ostergaard L, Porse BT, Garrett RA (1998). "Assembly of proteins and 5 S rRNA to transcripts of the major structural domains of 23 S rRNA." J Mol Biol 284(2);227-40. PMID: 9813114

Panagiotidis84: Panagiotidis CA, Canellakis ES (1984). "Comparison of the basic Escherichia coli antizyme 1 and antizyme 2 with the ribosomal proteins S20/L26 and L34." J Biol Chem 259(24);15025-7. PMID: 6392292

Panagiotidis88: Panagiotidis CA, Huang SC, Tsirka SA, Kyriakidis DA, Canellakis ES (1988). "Regulation of polyamine biosynthesis in Escherichia coli by the acidic antizyme and the ribosomal proteins S20 and L34." Adv Exp Med Biol 250;13-24. PMID: 3076320

Panagiotidis95: Panagiotidis CA, Huang SC, Canellakis ES (1995). "Relationship of the expression of the S20 and L34 ribosomal proteins to polyamine biosynthesis in Escherichia coli." Int J Biochem Cell Biol 27(2);157-68. PMID: 7539334

Parker76: Parker J, Watson RJ, Friesen JD (1976). "A relaxed mutant with an altered ribosomal protein L11." Mol Gen Genet 144(1);111-4. PMID: 772409

Parker83: Parker KK, Wickstrom E (1983). "Crosslinking of Escherichia coli 50S ribosomal subunits with chlorambucilyl oligoprolyl phenylalanyl-tRNA molecular rulers." Nucleic Acids Res 11(2);515-24. PMID: 6338479

Peattie81: Peattie DA, Douthwaite S, Garrett RA, Noller HF (1981). "A "bulged" double helix in a RNA-protein contact site." Proc Natl Acad Sci U S A 78(12);7331-5. PMID: 7038676

Perederina02: Perederina A, Nevskaya N, Nikonov O, Nikulin A, Dumas P, Yao M, Tanaka I, Garber M, Gongadze G, Nikonov S (2002). "Detailed analysis of RNA-protein interactions within the bacterial ribosomal protein L5/5S rRNA complex." RNA 8(12);1548-57. PMID: 12515387

Persson95: Persson BC, Bylund GO, Berg DE, Wikstrom PM (1995). "Functional analysis of the ffh-trmD region of the Escherichia coli chromosome by using reverse genetics." J Bacteriol 177(19);5554-60. PMID: 7559342

Petersen90a: Petersen C (1990). "Escherichia coli ribosomal protein L10 is rapidly degraded when synthesized in excess of ribosomal protein L7/L12." J Bacteriol 172(1);431-6. PMID: 2403546

Pettersson76: Pettersson I, Hardy SJ, Liljas A (1976). "The ribosomal protein L8 is a complex L7/L12 and L10." FEBS Lett 64(1);135-8. PMID: 773698

Pettersson79: Pettersson I (1979). "Studies on the RNA and protein binding sites of the E. coli ribosomal protein L10." Nucleic Acids Res 6(7);2637-46. PMID: 379826

Pichon77: Pichon JL, Coeroli C, Marchis-Mouren G (1977). "Studies on ribosomal protein biosynthesis in an RNA polymerase temperature sensitive E. coli mutant." Mol Gen Genet 150(3);257-64. PMID: 321934

Pieler82: Pieler T, Erdmann VA (1982). "Three-dimensional structural model of eubacterial 5S RNA that has functional implications." Proc Natl Acad Sci U S A 79(15);4599-603. PMID: 6181508

Podkowinski89: Podkowinski J, Gornicki P (1989). "Ribosomal proteins S7 and L1 are located close to the decoding site of E. coli ribosome--affinity labeling studies with modified tRNAs carrying photoreactive probes attached adjacent to the 3'-end of the anticodon." Nucleic Acids Res 17(21);8767-82. PMID: 2685749

Podkowinski91: Podkowinski J, Gornicki P (1991). "Neighbourhood of the central fold of the tRNA molecule bound to the E. coli ribosome--affinity labeling studies with modified tRNAs carrying photoreactive probes attached to the dihydrouridine loop." Nucleic Acids Res 19(4);801-8. PMID: 1708125

Pongs73: Pongs O, Bald R, Erdmann VA (1973). "Identification of chloramphenicol-binding protein in Escherichia coli ribosomes by affinity labeling." Proc Natl Acad Sci U S A 70(8);2229-33. PMID: 4599619

Pye90: Pye DA, Barber J (1990). "Co-operative binding of ribosomal proteins to an erythromycin affinity column." Biochem Int 21(5);909-14. PMID: 2256953

Raibaud03: Raibaud S, Vachette P, Guillier M, Allemand F, Chiaruttini C, Dardel F (2003). "How bacterial ribosomal protein L20 assembles with 23 S ribosomal RNA and its own messenger RNA." J Biol Chem 278(38);36522-30. PMID: 12840018

Raine04: Raine A, Ivanova N, Wikberg JE, Ehrenberg M (2004). "Simultaneous binding of trigger factor and signal recognition particle to the E. coli ribosome." Biochimie 86(7);495-500. PMID: 15308339

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Ralling84: Ralling G, Linn T (1984). "Relative activities of the transcriptional regulatory sites in the rplKAJLrpoBC gene cluster of Escherichia coli." J Bacteriol 158(1);279-85. PMID: 6325390

Ramagopal84: Ramagopal S (1984). "Metabolic changes in ribosomes of Escherichia coli during prolonged culture in different media." Eur J Biochem 140(2);353-61. PMID: 6201363

Ramakrishnan02: Ramakrishnan V (2002). "Ribosome structure and the mechanism of translation." Cell 108(4);557-72. PMID: 11909526

RandolphAnderso89: Randolph-Anderson BL, Gillham NW, Boynton JE (1989). "Electrophoretic and immunological comparisons of chloroplast and prokaryotic ribosomal proteins reveal that certain families of large subunit proteins are evolutionarily conserved." J Mol Evol 29(1);68-88. PMID: 2504932

Reblova04: Reblova K, Spackova N, Koca J, Leontis NB, Sponer J (2004). "Long-residency hydration, cation binding, and dynamics of loop E/helix IV rRNA-L25 protein complex." Biophys J 87(5);3397-412. PMID: 15339800

Redl89: Redl B, Walleczek J, Stoffler-Meilicke M, Stoffler G (1989). "Immunoblotting analysis of protein-protein crosslinks within the 50S ribosomal subunit of Escherichia coli. A study using dimethylsuberimidate as crosslinking reagent." Eur J Biochem 181(2);351-6. PMID: 2653827

Remme83: Remme J, Maimets T, Ustav M, Villems R (1983). "The interaction of ribosomal protein L16 and its fragments with tRNA." FEBS Lett 153(2);267-9. PMID: 6352325

Remme85: Remme J, Metspalu E, Maimets T, Villems R (1985). "The properties of the complex between ribosomal protein L2 and tRNA." FEBS Lett 190(2);275-8. PMID: 2412896

Rippa10a: Rippa V, Cirulli C, Di Palo B, Doti N, Amoresano A, Duilio A (2010). "The ribosomal protein L2 interacts with the RNA polymerase alpha subunit and acts as a transcription modulator in Escherichia coli." J Bacteriol 192(7);1882-9. PMID: 20097853

Robakis81: Robakis N, Meza-Basso L, Brot N, Weissbach H (1981). "Translational control of ribosomal protein L10 synthesis occurs prior to formation of first peptide bond." Proc Natl Acad Sci U S A 78(7);4261-4. PMID: 7027258

Robertson77: Robertson WR, Dowsett SJ, Hardy SJ (1977). "Exchange of ribosomal proteins among the ribosomes of Escherichia coli." Mol Gen Genet 157(2);205-14. PMID: 340925

Rohl82: Rohl R, Nierhaus KH (1982). "Assembly map of the large subunit (50S) of Escherichia coli ribosomes." Proc Natl Acad Sci U S A 79(3);729-33. PMID: 7038683

Romero90: Romero DP, Arredondo JA, Traut RR (1990). "Identification of a region of Escherichia coli ribosomal protein L2 required for the assembly of L16 into the 50 S ribosomal subunit." J Biol Chem 265(30);18185-91. PMID: 2211695

Rosen93: Rosen KV, Alexander RW, Wower J, Zimmermann RA (1993). "Mapping the central fold of tRNA2(fMet) in the P site of the Escherichia coli ribosome." Biochemistry 32(47);12802-11. PMID: 8251501

Rosendahl93: Rosendahl G, Douthwaite S (1993). "Ribosomal proteins L11 and L10.(L12)4 and the antibiotic thiostrepton interact with overlapping regions of the 23 S rRNA backbone in the ribosomal GTPase centre." J Mol Biol 234(4);1013-20. PMID: 8263910

Rosendahl95: Rosendahl G, Douthwaite S (1995). "Cooperative assembly of proteins in the ribosomal GTPase centre demonstrated by their interactions with mutant 23S rRNAs." Nucleic Acids Res 23(13);2396-403. PMID: 7630717

Ryan91: Ryan PC, Lu M, Draper DE (1991). "Recognition of the highly conserved GTPase center of 23 S ribosomal RNA by ribosomal protein L11 and the antibiotic thiostrepton." J Mol Biol 221(4);1257-68. PMID: 1942050

Said88: Said B, Cole JR, Nomura M (1988). "Mutational analysis of the L1 binding site of 23S rRNA in Escherichia coli." Nucleic Acids Res 16(22);10529-45. PMID: 3060846

Sander75: Sander G, Marsh RC, Voigt J, Parmeggiani A (1975). "A comparative study of the 50S ribosomal subunit and several 50S subparticles in EF-T-and EF-G-dependent activities." Biochemistry 14(9);1805-14. PMID: 1092342

Sander83: Sander G (1983). "Ribosomal protein L1 from Escherichia coli. Its role in the binding of tRNA to the ribosome and in elongation factor g-dependent gtp hydrolysis." J Biol Chem 258(16);10098-103. PMID: 6350280

Sato01: Sato S, Xiang S, Raleigh DP (2001). "On the relationship between protein stability and folding kinetics: a comparative study of the N-terminal domains of RNase HI, E. coli and Bacillus stearothermophilus L9." J Mol Biol 312(3);569-77. PMID: 11563917

Sato06: Sato H, Ito K, Nakamura Y (2006). "Ribosomal protein L11 mutations in two functional domains equally affect release factors 1 and 2 activity." Mol Microbiol 60(1);108-20. PMID: 16556224

Scheibe86: Scheibe U, Wagner R (1986). "Identification of neighbouring proteins by cross-linking of intact 70 S ribosomes from Escherichia coli." Biochim Biophys Acta 869(1);1-7. PMID: 3510664

Schmid84: Schmid G, Strobel O, Stoffler-Meilicke M, Stoffler G, Bock A (1984). "A ribosomal protein that is immunologically conserved in archaebacteria, eubacteria and eukaryotes." FEBS Lett 177(2);189-94. PMID: 6209167

Schmidt81a: Schmidt FJ, Thompson J, Lee K, Dijk J, Cundliffe E (1981). "The binding site for ribosomal protein L11 within 23 S ribosomal RNA of Escherichia coli." J Biol Chem 256(23);12301-5. PMID: 6271782

Schneider03: Schneider DA, Ross W, Gourse RL (2003). "Control of rRNA expression in Escherichia coli." Curr Opin Microbiol 6(2);151-6. PMID: 12732305

Schnier79: Schnier J, Isono K (1979). "The gene for ribosomal protein L25 (rplY) maps at 47.3 min near nalA in Escherichia coli K-12." Mol Gen Genet 176(3);313-8. PMID: 392236

Schnier86: Schnier J, Kitakawa M, Isono K (1986). "The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame." Mol Gen Genet 204(1);126-32. PMID: 3528756

Schonfeld87: Schonfeld HJ, Foulaki K (1987). "Preoperative isolation of a reversible protein-protein crosslink generated in 50 S subunits of Escherichia coli ribosomes and identification of its components." Anal Biochem 164(1);23-30. PMID: 3314578

Schrier75: Schrier PI, Moller W (1975). "The involvement of 50S ribosomal protein l11 in the EF-G dependent GTP hydrolysis of E. coli ribosomes." FEBS Lett 54(2);130-4. PMID: 165973

Schulze82: Schulze H, Nierhaus KH (1982). "Minimal set of ribosomal components for reconstitution of the peptidyltransferase activity." EMBO J 1(5);609-13. PMID: 6765232

Schuwirth05: Schuwirth BS, Borovinskaya MA, Hau CW, Zhang W, Vila-Sanjurjo A, Holton JM, Cate JH (2005). "Structures of the bacterial ribosome at 3.5 A resolution." Science 310(5749);827-34. PMID: 16272117

Seidman11: Seidman JS, Janssen BD, Hayes CS (2011). "Alternative fates of paused ribosomes during translation termination." J Biol Chem 286(36);31105-12. PMID: 21757758

Semrad04: Semrad K, Green R, Schroeder R (2004). "RNA chaperone activity of large ribosomal subunit proteins from Escherichia coli." RNA 10(12);1855-60. PMID: 15525706

Sergiev07: Sergiev PV, Bogdanov AA, Dontsova OA (2007). "Ribosomal RNA guanine-(N2)-methyltransferases and their targets." Nucleic Acids Res 35(7):2295-301. PMID: 17389639

Sha95: Sha Y, Lindahl L, Zengel JM (1995). "Role of NusA in L4-mediated attenuation control of the S10 r-protein operon of Escherichia coli." J Mol Biol 245(5);474-85. PMID: 7844821

Sharpe98: Sharpe PL, Craig NL (1998). "Host proteins can stimulate Tn7 transposition: a novel role for the ribosomal protein L29 and the acyl carrier protein." EMBO J 17(19);5822-31. PMID: 9755182

Shasmal10: Shasmal M, Chakraborty B, Sengupta J (2010). "Intrinsic molecular properties of the protein-protein bridge facilitate ratchet-like motion of the ribosome." Biochem Biophys Res Commun 399(2);192-7. PMID: 20643101

Shen80: Shen V, King TC, Kumar V, Daugherty B (1980). "Monoclonal antibodies to Escherichia coli 50S ribosomes." Nucleic Acids Res 8(20);4639-49. PMID: 6160475

Shoji11: Shoji S, Dambacher CM, Shajani Z, Williamson JR, Schultz PG (2011). "Systematic chromosomal deletion of bacterial ribosomal protein genes." J Mol Biol 413(4);751-61. PMID: 21945294

Shpanchenko96: Shpanchenko OV, Zvereva MI, Dontsova OA, Nierhaus KH, Bogdanov AA (1996). "5S rRNA sugar-phosphate backbone protection in complexes with specific ribosomal proteins." FEBS Lett 394(1);71-5. PMID: 8925931

Siegrist84: Siegrist S, Moreau N, Le Goffic F (1984). "[Photochemical affinity labeling of the macrolide binding site on the 70S E. coli ribosome]." C R Acad Sci III 299(3);49-51. PMID: 6437621

Siegrist85: Siegrist S, Moreau N, Le Goffic F (1985). "About the specificity of photoinduced affinity labeling of Escherichia coli ribosomes by dihydrorosaramicin, a macrolide related to erythromycin." Eur J Biochem 153(1);131-5. PMID: 3905404

Silberklang83: Silberklang M, RajBhandary UL, Luck A, Erdmann VA (1983). "Chemical reactivity of E. coli 5S RNA in situ in the 50S ribosomal subunit." Nucleic Acids Res 11(3);605-17. PMID: 6340064

Singh09a: Singh D, Chang SJ, Lin PH, Averina OV, Kaberdin VR, Lin-Chao S (2009). "Regulation of ribonuclease E activity by the L4 ribosomal protein of Escherichia coli." Proc Natl Acad Sci U S A 106(3);864-9. PMID: 19144914

Skold81: Skold SE (1981). "RNA-protein complexes identified by crosslinking of polysomes." Biochimie 63(1);53-60. PMID: 6163479

Smith89b: Smith KR, Yancey JE, Matson SW (1989). "Identification and purification of a protein that stimulates the helicase activity of the Escherichia coli Rep protein." J Biol Chem 264(11);6119-26. PMID: 2522929

Sonenberg73: Sonenberg N, Wilchek M, Zamir A (1973). "Mapping of Escherichia coli ribosomal components involved in peptidyl transferase activity." Proc Natl Acad Sci U S A 70(5);1423-6. PMID: 4576018

Soung09: Soung GY, Miller JL, Koc H, Koc EC (2009). "Comprehensive analysis of phosphorylated proteins of Escherichia coli ribosomes." J Proteome Res 8(7);3390-402. PMID: 19469554

Speek82: Speek M, Lind A (1982). "Structural analyses of E. coli 5S RNA fragments, their associates and complexes with proteins L18 and L25." Nucleic Acids Res 10(3);947-63. PMID: 6278442

Spierer75: Spierer P, Zimmerman RA, Mackie GA (1975). "RNA-protein interactions in the ribosome. Binding of 50-S-subunit proteins to 5' and 3' terminal segments of the 23-S RNA." Eur J Biochem 52(3);459-68. PMID: 800986

Spierer76: Spierer P, Zimmermann RA (1976). "RNA-protein interactions in the ribosome. Binding of proteins L1, L3, L6, L13 and L23 to specific fragments of the 23S RNA." FEBS Lett 68(1);71-5. PMID: 823048

Spierer78: Spierer P, Zimmermann RA (1978). "Stoichiometry, cooperativity, and stability of interactions between 5S RNA and proteins L5, L18, and L25 from the 50S ribosomal subunit of Escherichia coli." Biochemistry 17(13);2474-9. PMID: 354687

Spierer78a: Spierer P, Bogdanov AA, Zimmermann RA (1978). "Parameters for the interaction of ribosomal proteins L5, L18, and L25 with 5S RNA from Escherichia coli." Biochemistry 17(25);5394-8. PMID: 365228

Spierer79: Spierer P, Wang CC, Marsh TL, Zimmermann RA (1979). "Cooperative interactions among protein and RNA components of the 50S ribosomal subunit of Escherichia coli." Nucleic Acids Res 6(4);1669-82. PMID: 109811

Spillmann78: Spillmann S, Nierhaus KH (1978). "The ribosomal protein L24 of Escherichia coli is an assembly protein." J Biol Chem 253(19);7047-50. PMID: 357435

Srivastava91: Srivastava AK, Schlessinger D (1991). "Structure and organization of ribosomal DNA." Biochimie 73(6);631-8. PMID: 1764510

Stark02: Stark H (2002). "Three-dimensional electron cryomicroscopy of ribosomes." Curr Protein Pept Sci 3(1);79-91. PMID: 12370013

Stelzl00: Stelzl U, Spahn CM, Nierhaus KH (2000). "Selecting rRNA binding sites for the ribosomal proteins L4 and L6 from randomly fragmented rRNA: application of a method called SERF." Proc Natl Acad Sci U S A 97(9);4597-602. PMID: 10781065

Stelzl01: Stelzl U, Nierhaus KH (2001). "A short fragment of 23S rRNA containing the binding sites for two ribosomal proteins, L24 and L4, is a key element for rRNA folding during early assembly." RNA 7(4);598-609. PMID: 11345438

Stelzl03: Stelzl U, Zengel JM, Tovbina M, Walker M, Nierhaus KH, Lindahl L, Patel DJ (2003). "RNA-structural mimicry in Escherichia coli ribosomal protein L4-dependent regulation of the S10 operon." J Biol Chem 278(30);28237-45. PMID: 12738792

Steward91: Steward KL, Linn T (1991). "In vivo analysis of overlapping transcription units in the rplKAJLrpoBC ribosomal protein-RNA polymerase gene cluster of Escherichia coli." J Mol Biol 218(1);23-31. PMID: 1825852

Stoffler71: Stoffler G, Daya L, Rak KH, Garrett RA (1971). "Ribosomal proteins. XXVI. The number of specific protein binding sites on 16 s and 23 s RNA of Escherichia coli." J Mol Biol 62(2);411-4. PMID: 4944932

Stoffler81: Stoffler G, Hasenbank R, Dabbs ER (1981). "Expression of the L11-L1 operon in mutants of Escherichia coli lacking the ribosomal proteins L1 or L11." Mol Gen Genet 181(2);164-8. PMID: 7024735

Stoffler84: Stoffler G, Noah M, Stoffler-Meilicke M, Dabbs ER (1984). "The localization of protein L19 on the surface of 50 S subunits of Escherichia coli aided by the use of mutants lacking protein L19." J Biol Chem 259(7);4521-6. PMID: 6423642

StofflerMeilick83: Stoffler-Meilicke M, Noah M, Stoffler G (1983). "Location of eight ribosomal proteins on the surface of the 50S subunit from Escherichia coli." Proc Natl Acad Sci U S A 80(22);6780-4. PMID: 6359156

Stoldt98: Stoldt M, Wohnert J, Gorlach M, Brown LR (1998). "The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases." EMBO J 17(21);6377-84. PMID: 9799245

Stoldt99: Stoldt M, Wohnert J, Ohlenschlager O, Gorlach M, Brown LR (1999). "The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition." EMBO J 18(22);6508-21. PMID: 10562563

Subramanian77: Subramanian AR, van Duin J (1977). "Exchange of individual ribosomal proteins between ribosomes as studied by heavy isotope-transfer experiments." Mol Gen Genet 158(1);1-9. PMID: 342903

Subramanian80: Subramanian AR, Dabbs ER (1980). "Functional studies on ribosomes lacking protein L1 from mutant Escherichia coli." Eur J Biochem 112(2);425-30. PMID: 7007045

Sumpter90: Sumpter VG, Tate WP, Nierhaus KH (1990). "The complex between ribosomal proteins and aminoacyl-tRNA: the interactions and hydrolytic activities are not confined to the proteins L2 and L16 of Escherichia coli ribosomes." Biochim Biophys Acta 1048(2-3);265-9. PMID: 2182127

Sumpter91: Sumpter VG, Tate WP, Nowotny P, Nierhaus KH (1991). "Modification of histidine residues on proteins from the 50S subunit of the Escherichia coli ribosome. Effects on subunit assembly and peptidyl transferase centre activity." Eur J Biochem 196(2);255-60. PMID: 1706660

Suryanarayana83: Suryanarayana T (1983). "Identification by affinity chromatography of Escherichia coli ribosomal proteins that bind erythromycin and chloramphenicol." Biochem Int 7(6);719-25. PMID: 6385986

Szymkowiak85: Szymkowiak C, Wagner R (1985). "Analysis of a sequence region of 5S RNA from E. coli cross-linked in situ to the ribosomal protein L25." Nucleic Acids Res 13(11);3953-68. PMID: 3892485

Tanaka85: Tanaka T, Ogata K (1985). "[The structure and the evolution of the 5S RNA protein complex]." Seikagaku 57(11);1531-4. PMID: 3913708

Tangy83: Tangy F, Capmau ML, Le Goffic F (1983). "Photo-induced labelling of Escherichia coli ribosomes by a tobramycin analog." Eur J Biochem 131(3);581-7. PMID: 6341055

Tate83: Tate WP, Schulze H, Nierhaus KH (1983). "The importance of the Escherichia coli ribosomal protein L16 for the reconstitution of the peptidyl-tRNA hydrolysis activity of peptide chain termination." J Biol Chem 258(21);12810-5. PMID: 6355096

Tate83a: Tate WP, Schulze H, Nierhaus KH (1983). "The Escherichia coli ribosomal protein L11 suppresses release factor 2 but promotes the release factor 1 activities in peptide chain termination." J Biol Chem 258(21);12816-20. PMID: 6355097

Tate84: Tate WP, Dognin MJ, Noah M, Stoffler-Meilicke M, Stoffler G (1984). "The NH2-terminal domain of Escherichia coli ribosomal protein L11. Its three-dimensional location and its role in the binding of release factors 1 and 2." J Biol Chem 259(11);7317-24. PMID: 6373771

Tate86: Tate WP, McCaughan KK, Ward CD, Sumpter VG, Trotman CN, Stoffler-Meilicke M, Maly P, Brimacombe R (1986). "The ribosomal binding domain of the Escherichia coli release factors. Modification of tyrosine in the N-terminal domain of ribosomal protein L11 affects release factors 1 and 2 differentially." J Biol Chem 261(5);2289-93. PMID: 3511060

Tate87: Tate WP, Sumpter VG, Trotman CN, Herold M, Nierhaus KH (1987). "The peptidyltransferase centre of the Escherichia coli ribosome. The histidine of protein L16 affects the reconstitution and control of the active centre but is not essential for release-factor-mediated peptidyl-tRNA hydrolysis and peptide bond formation." Eur J Biochem 165(2);403-8. PMID: 3297687

Tejedor85: Tejedor F, Amils R, Ballesta JP (1985). "Photoaffinity labeling of the pactamycin binding site on eubacterial ribosomes." Biochemistry 24(14);3667-72. PMID: 3899171

Tejedor85a: Tejedor F, Ballesta JP (1985). "Components of the macrolide binding site on the ribosome." J Antimicrob Chemother 16 Suppl A;53-62. PMID: 4055551

Tenson95: Tenson T, Mankin A (1995). "Comparison of functional peptide encoded in the Escherichia coli 23S rRNA with other peptides involved in cis-regulation of translation." Biochem Cell Biol 73(11-12);1061-70. PMID: 8722022

Teraoka78: Teraoka H, Nierhaus KH (1978). "Protein L16 induces a conformational change when incorporated into a L16-deficient core derived from Escherichia coli ribosomes." FEBS Lett 88(2);223-6. PMID: 348495

Terhorst73: Terhorst C, Moller W, Laursen R, Wittmann-Liebold B (1973). "The primary structure of an acidic protein from 50-S ribosomes of Escherichia coli which is involved in GTP hydrolysis dependent on elongation factors G and T." Eur J Biochem 34(1);138-52. PMID: 4573678

Tewari83: Tewari DS, Burma DP (1983). "Incorporation of 5S RNA into 16S-23S RNA complex." Biochem Biophys Res Commun 114(1);348-54. PMID: 6349628

Thiede98: Thiede B, Urlaub H, Neubauer H, Grelle G, Wittmann-Liebold B (1998). "Precise determination of RNA-protein contact sites in the 50 S ribosomal subunit of Escherichia coli." Biochem J 334 ( Pt 1);39-42. PMID: 9693099

Thomas87: Thomas MS, Bedwell DM, Nomura M (1987). "Regulation of alpha operon gene expression in Escherichia coli. A novel form of translational coupling." J Mol Biol 196(2);333-45. PMID: 3309351

Thomas87a: Thomas MS, Nomura M (1987). "Translational regulation of the L11 ribosomal protein operon of Escherichia coli: mutations that define the target site for repression by L1." Nucleic Acids Res 15(7);3085-96. PMID: 3104883

Traut83: Traut RR, Lambert JM, Kenny JW (1983). "Ribosomal protein L7/L12 cross-links to proteins in separate regions of the 50 S ribosomal subunit of Escherichia coli." J Biol Chem 258(23);14592-8. PMID: 6358224

Traut95: Traut RR, Dey D, Bochkariov DE, Oleinikov AV, Jokhadze GG, Hamman B, Jameson D (1995). "Location and domain structure of Escherichia coli ribosomal protein L7/L12: site specific cysteine crosslinking and attachment of fluorescent probes." Biochem Cell Biol 73(11-12);949-58. PMID: 8722010

Triman96a: Triman KL (1996). "The 23S Ribosomal RNA Mutation Database (23SMDB)." Nucleic Acids Res 24(1);169-71. PMID: 8594571

Triman97: Triman KL, Adams BJ (1997). "Expansion of the 16S and 23S ribosomal RNA mutation databases (16SMDB and 23SMDB)." Nucleic Acids Res 25(1);188-91. PMID: 9016533

Triman98: Triman KL, Peister A, Goel RA (1998). "Expanded versions of the 16S and 23S ribosomal RNA mutation databases (16SMDBexp and 23SMDBexp)." Nucleic Acids Res 26(1);280-4. PMID: 9399853

Triman99: Triman KL (1999). "Mutational analysis of 23S ribosomal RNA structure and function in Escherichia coli." Adv Genet 41;157-95. PMID: 10494619

Tritton76: Tritton TR, Crothers DM (1976). "Physical characterization of a ribosomal nucleoprotein complex." Biochemistry 15(20);4377-85. PMID: 788777

Tumanova: Tumanova LG, Gongadze GM, Ven'iaminov SIu, Gudkov AT, Bushuev VN "[Comparison of the physical properties of ribosomal proteins from Escherichia coli 50S subparticles isolated by different methods]." Mol Biol (Mosk) 18(3);751-8. PMID: 6381990

Tumanova83: Tumanova LG, Gongadze GM, Venyaminov SYu , Gudkov AT, Bushuev VN (1983). "Physical properties of ribosomal proteins isolated under different conditions from the Escherichia coli 50 S subunit." FEBS Lett 157(1);85-90. PMID: 6345195

Tumminia94: Tumminia SJ, Hellmann W, Wall JS, Boublik M (1994). "Visualization of protein-nucleic acid interactions involved in the in vitro assembly of the Escherichia coli 50 S ribosomal subunit." J Mol Biol 235(4);1239-50. PMID: 8308887

Uchiumi99: Uchiumi T, Sato N, Wada A, Hachimori A (1999). "Interaction of the sarcin/ricin domain of 23 S ribosomal RNA with proteins L3 and L6." J Biol Chem 274(2);681-6. PMID: 9873002

Uhlein98: Uhlein M, Weglohner W, Urlaub H, Wittmann-Liebold B (1998). "Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies." Biochem J 331 ( Pt 2);423-30. PMID: 9531480

Ulbrich75: Ulbrich B, Nierhaus KH (1975). "Pools of ribosomal proteins in Escherichia coli. Studies on the exchange of proteins between pools and ribosomes." Eur J Biochem 57(1);49-54. PMID: 1100403

Ullers03: Ullers RS, Houben EN, Raine A, ten Hagen-Jongman CM, Ehrenberg M, Brunner J, Oudega B, Harms N, Luirink J (2003). "Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome." J Cell Biol 161(4);679-84. PMID: 12756233

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Urlaub95: Urlaub H, Kruft V, Bischof O, Muller EC, Wittmann-Liebold B (1995). "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies." EMBO J 14(18);4578-88. PMID: 7556101

Van02a: Van Dyke N, Xu W, Murgola EJ (2002). "Limitation of ribosomal protein L11 availability in vivo affects translation termination." J Mol Biol 319(2);329-39. PMID: 12051910

Van03b: Van Dyke N, Murgola EJ (2003). "Site of functional interaction of release factor 1 with the ribosome." J Mol Biol 330(1);9-13. PMID: 12818198

vandeVen83: van de Ven FJ, de Bruin SH, Hilbers CW (1983). "500-MHz 1H-NMR studies of ribosomal proteins isolated from 70-S ribosomes of Escherichia coli." Eur J Biochem 134(3);429-38. PMID: 6349991

Vanet94: Vanet A, Plumbridge JA, Guerin MF, Alix JH (1994). "Ribosomal protein methylation in Escherichia coli: the gene prmA, encoding the ribosomal protein L11 methyltransferase, is dispensable." Mol Microbiol 14(5);947-58. PMID: 7715456

Vester84: Vester B, Garrett RA (1984). "Structure of a protein L23-RNA complex located at the A-site domain of the ribosomal peptidyl transferase centre." J Mol Biol 179(3);431-52. PMID: 6392564

Vester88: Vester B, Egebjerg J, Garrett R, Christiansen J (1988). "Primer-directed deletions in 5S ribosomal RNA." Methods Enzymol 164;710-21. PMID: 3071690

Vladimirov00: Vladimirov SN, Druzina Z, Wang R, Cooperman BS (2000). "Identification of 50S components neighboring 23S rRNA nucleotides A2448 and U2604 within the peptidyl transferase center of Escherichia coli ribosomes." Biochemistry 39(1);183-93. PMID: 10625493

Vladimirov85: Vladimirov SN, Graifer DM, Karpova GG, Semenkov YuP , Makhno VI, Kirillov SV (1985). "The effect of GTP hydrolysis and transpeptidation on the arrangement of aminoacyl-tRNA at the A-site of Escherichia coli 70 S ribosomes." FEBS Lett 181(2);367-72. PMID: 2578985

Vladimirov90: Vladimirov SN, Babkina GT, Venijaminova AG, Gimautdinova OI, Zenkova MA, Karpova GG (1990). "Structural arrangement of the decoding site of Escherichia coli ribosomes as revealed from the data on affinity labelling of ribosomes by analogs of mRNA--derivatives of oligoribonucleotides." Biochim Biophys Acta 1048(2-3);245-56. PMID: 2182126

Wada87a: Wada A, Sako T (1987). "Primary structures of and genes for new ribosomal proteins A and B in Escherichia coli." J Biochem 101(3);817-20. PMID: 3298224

Walleczek89: Walleczek J, Martin T, Redl B, Stoffler-Meilicke M, Stoffler G (1989). "Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli." Biochemistry 28(9);4099-105. PMID: 2665813

Walleczek89a: Walleczek J, Redl B, Stoffler-Meilicke M, Stoffler G (1989). "Protein-protein cross-linking of the 50 S ribosomal subunit of Escherichia coli using 2-iminothiolane. Identification of cross-links by immunoblotting techniques." J Biol Chem 264(7);4231-7. PMID: 2645289

Wang12l: Wang Y, Xiao M (2012). "Role of the ribosomal protein L27 revealed by single-molecule FRET study." Protein Sci 21(11);1696-704. PMID: 22930421

Wasinger98: Wasinger VC, Humphery-Smith I (1998). "Small genes/gene-products in Escherichia coli K-12." FEMS Microbiol Lett 169(2);375-82. PMID: 9868784

Weitzmann85: Weitzmann C, Cooperman BS (1985). "On the structural specificity of puromycin binding to Escherichia coli ribosomes." Biochemistry 24(9);2268-74. PMID: 3888269

Weitzmann90: Weitzmann CJ, Cooperman BS (1990). "Reconstitution of Escherichia coli 50S ribosomal subunits containing puromycin-modified L23: functional consequences." Biochemistry 29(14);3458-65. PMID: 2191716

Wendrich02: Wendrich TM, Blaha G, Wilson DN, Marahiel MA, Nierhaus KH (2002). "Dissection of the mechanism for the stringent factor RelA." Mol Cell 10(4);779-88. PMID: 12419222

Wikstrom88: Wikstrom PM, Bystrom AS, Bjork GR (1988). "Non-autogenous control of ribosomal protein synthesis from the trmD operon in Escherichia coli." J Mol Biol 203(1);141-52. PMID: 2460631

Wikstrom92: Wikstrom PM, Lind LK, Berg DE, Bjork GR (1992). "Importance of mRNA folding and start codon accessibility in the expression of genes in a ribosomal protein operon of Escherichia coli." J Mol Biol 224(4);949-66. PMID: 1569581

Wild88: Wild DG (1988). "Reversion from erythromycin dependence in Escherichia coli: strains altered in ribosomal sub-unit association and ribosome assembly." J Gen Microbiol 134(5);1251-63. PMID: 2462010

Willumeit01: Willumeit R, Forthmann S, Beckmann J, Diedrich G, Ratering R, Stuhrmann HB, Nierhaus KH (2001). "Localization of the protein L2 in the 50 S subunit and the 70 S E. coli ribosome." J Mol Biol 305(1);167-77. PMID: 11114255

Willumeit01a: Willumeit R, Diedrich G, Forthmann S, Beckmann J, May RP, Stuhrmann HB, Nierhaus KH (2001). "Mapping proteins of the 50S subunit from Escherichia coli ribosomes." Biochim Biophys Acta 1520(1);7-20. PMID: 11470155

Wimberly99: Wimberly BT, Guymon R, McCutcheon JP, White SW, Ramakrishnan V (1999). "A detailed view of a ribosomal active site: the structure of the L11-RNA complex." Cell 97(4);491-502. PMID: 10338213

Wittmann73: Wittmann HG, Stoffler G, Apirion D, Rosen L, Tanaka K, Tamaki M, Takata R, Dekio S, Otaka E (1973). "Biochemical and genetic studies on two different types of erythromycin resistant mutants of Escherichia coli with altered ribosomal proteins." Mol Gen Genet 127(2);175-89. PMID: 4589347

WittmannLiebold73: Wittmann-Liebold B (1973). "Studies on the primary structure of 20 proteins from Escherichia coli ribosomes by means of an improved protein sequenator." FEBS Lett 36(3);247-9. PMID: 4587209

WittmannLiebold95: Wittmann-Liebold B, Uhlein M, Urlaub H, Muller EC, Otto A, Bischof O (1995). "Structural and functional implications in the eubacterial ribosome as revealed by protein-rRNA and antibiotic contact sites." Biochem Cell Biol 73(11-12);1187-97. PMID: 8722036

Wohnert99: Wohnert J, Dingley AJ, Stoldt M, Gorlach M, Grzesiek S, Brown LR (1999). "Direct identification of NH...N hydrogen bonds in non-canonical base pairs of RNA by NMR spectroscopy." Nucleic Acids Res 27(15);3104-10. PMID: 10454606

Wower81: Wower I, Wower J, Meinke M, Brimacombe R (1981). "The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29." Nucleic Acids Res 9(17);4285-302. PMID: 6170935

Wower89: Wower J, Hixson SS, Zimmermann RA (1989). "Labeling the peptidyltransferase center of the Escherichia coli ribosome with photoreactive tRNA(Phe) derivatives containing azidoadenosine at the 3' end of the acceptor arm: a model of the tRNA-ribosome complex." Proc Natl Acad Sci U S A 86(14);5232-6. PMID: 2664777

Wower95: Wower J, Wower IK, Kirillov SV, Rosen KV, Hixson SS, Zimmermann RA (1995). "Peptidyl transferase and beyond." Biochem Cell Biol 73(11-12);1041-7. PMID: 8722019

Wower98: Wower IK, Wower J, Zimmermann RA (1998). "Ribosomal protein L27 participates in both 50 S subunit assembly and the peptidyl transferase reaction." J Biol Chem 273(31);19847-52. PMID: 9677420

Yamada80a: Yamada R, Nakatsuka H, Nakamura K, Sato M, Itami M, Kobayashi N, Minakuchi K, Onoyama T, Kanno T, Monna T, Yamamoto S (1980). "Hepatic artery embolization in 32 patients with unresectable hepatoma." Osaka City Med J 26(2);81-96. PMID: 6170035

Yamamoto09: Yamamoto N, Nakahigashi K, Nakamichi T, Yoshino M, Takai Y, Touda Y, Furubayashi A, Kinjyo S, Dose H, Hasegawa M, Datsenko KA, Nakayashiki T, Tomita M, Wanner BL, Mori H (2009). "Update on the Keio collection of Escherichia coli single-gene deletion mutants." Mol Syst Biol 5;335. PMID: 20029369

Yancey91: Yancey JE, Matson SW (1991). "The DNA unwinding reaction catalyzed by Rep protein is facilitated by an RHSP-DNA interaction." Nucleic Acids Res 19(14);3943-51. PMID: 1650456

Yang01c: Yang X, Ishiguro EE (2001). "Involvement of the N terminus of ribosomal protein L11 in regulation of the RelA protein of Escherichia coli." J Bacteriol 183(22);6532-7. PMID: 11673421

Yates80: Yates JL, Arfsten AE, Nomura M (1980). "In vitro expression of Escherichia coli ribosomal protein genes: autogenous inhibition of translation." Proc Natl Acad Sci U S A 77(4);1837-41. PMID: 6445562

Yates80a: Yates JL, Nomura M (1980). "E. coli ribosomal protein L4 is a feedback regulatory protein." Cell 21(2);517-22. PMID: 6996835

Yates81: Yates JL, Nomura M (1981). "Feedback regulation of ribosomal protein synthesis in E. coli: localization of the mRNA target sites for repressor action of ribosomal protein L1." Cell 24(1);243-9. PMID: 7016337

Yates81a: Yates JL, Dean D, Strycharz WA, Nomura M (1981). "E. coli ribosomal protein L10 inhibits translation of L10 and L7/L12 mRNAs by acting at a single site." Nature 294(5837);190-2. PMID: 6272122

Yonath05: Yonath A (2005). "Antibiotics targeting ribosomes: resistance, selectivity, synergism and cellular regulation." Annu Rev Biochem 74;649-79. PMID: 16180279

Yoshida02b: Yoshida H, Maki Y, Kato H, Fujisawa H, Izutsu K, Wada C, Wada A (2002). "The ribosome modulation factor (RMF) binding site on the 100S ribosome of Escherichia coli." J Biochem (Tokyo) 132(6);983-9. PMID: 12473202

Yusupov86: Yusupov MM, Spirin AS (1986). "Are there proteins between the ribosomal subunits? Hot tritium bombardment experiments." FEBS Lett 197(1-2);229-33. PMID: 3512304

Zaman07: Zaman S, Fitzpatrick M, Lindahl L, Zengel J (2007). "Novel mutations in ribosomal proteins L4 and L22 that confer erythromycin resistance in Escherichia coli." Mol Microbiol 66(4);1039-50. PMID: 17956547

Zengel02: Zengel JM, Sha Y, Lindahl L (2002). "Surprising flexibility of leader RNA determinants for r-protein L4-mediated transcription termination in the Escherichia coil S10 operon." RNA 8(5);572-8. PMID: 12022224

Zengel03: Zengel JM, Jerauld A, Walker A, Wahl MC, Lindahl L (2003). "The extended loops of ribosomal proteins L4 and L22 are not required for ribosome assembly or L4-mediated autogenous control." RNA 9(10);1188-97. PMID: 13130133

Zengel80: Zengel JM, Mueckl D, Lindahl L (1980). "Protein L4 of the E. coli ribosome regulates an eleven gene r protein operon." Cell 21(2);523-35. PMID: 6157482

Zengel90: Zengel JM, Lindahl L (1990). "Ribosomal protein L4 stimulates in vitro termination of transcription at a NusA-dependent terminator in the S10 operon leader." Proc Natl Acad Sci U S A 87(7);2675-9. PMID: 2157208

Zengel90a: Zengel JM, Lindahl L (1990). "Escherichia coli ribosomal protein L4 stimulates transcription termination at a specific site in the leader of the S10 operon independent of L4-mediated inhibition of translation." J Mol Biol 213(1);67-78. PMID: 1692593

Zengel91: Zengel JM, Lindahl L (1991). "Ribosomal protein L4 of Escherichia coli: in vitro analysis of L4-mediated attenuation control." Biochimie 73(6);719-27. PMID: 1764518

Zengel92: Zengel JM, Lindahl L (1992). "Ribosomal protein L4 and transcription factor NusA have separable roles in mediating terminating of transcription within the leader of the S10 operon of Escherichia coli." Genes Dev 6(12B);2655-62. PMID: 1285127

Zengel93: Zengel JM, Lindahl L (1993). "Domain I of 23S rRNA competes with a paused transcription complex for ribosomal protein L4 of Escherichia coli." Nucleic Acids Res 21(10);2429-35. PMID: 7685080

Zengel96: Zengel JM, Lindahl L (1996). "A hairpin structure upstream of the terminator hairpin required for ribosomal protein L4-mediated attenuation control of the S10 operon of Escherichia coli." J Bacteriol 178(8);2383-7. PMID: 8636042

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

Zhang09: Zhang W, Dunkle JA, Cate JH (2009). "Structures of the ribosome in intermediate states of ratcheting." Science 325(5943);1014-7. PMID: 19696352

Zhang89c: Zhang P, Popieniek P, Moore PB (1989). "Physical studies of 5S RNA variants at position 66." Nucleic Acids Res 17(21);8645-56. PMID: 2479908

Zheng11: Zheng C, Yang L, Hoopmann MR, Eng JK, Tang X, Weisbrod CR, Bruce JE (2011). "Cross-linking measurements of in vivo protein complex topologies." Mol Cell Proteomics 10(10);M110.006841. PMID: 21697552

Zimmermann78: Zimmermann J, Erdmann VA (1978). "Identification of Escherichia coli and Bacillus stearothermophilus ribosomal protein binding sites on Escherichia coli 5S RNA." Mol Gen Genet 160(3);247-57. PMID: 353489


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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