Escherichia coli K-12 substr. MG1655 Protein: HslU hexamer

Gene: hslU Accession Numbers: EG11881 (EcoCyc), b3931, ECK3923

Synonyms: clpY, htpI, D48.5

Regulation Summary Diagram: ?

Regulation summary diagram for hslU

Component of: HslVU protease (summary available)

Subunit composition of HslU hexamer = [HslU]6
         ATPase component of the HslVU protease = HslU

HslU is the ATPase component of the HslVU protease, which is composed of HslU and HslV [Rohrwild96, Yoo96]. This ATP-stimulated protease exhibits activity similar to that of the chymotrypsin-like activity of the eukaryotic proteasome [Rohrwild96]. HslU also exhibits protein chaperone activity [Seong00].

HslU is required for growth under conditions of elevated temperature [Peruski94, Katayama96a]. HslU is involved in wild-type cell size control under some conditions [Katayama96a]. The relationship between HslU and the cell division inhibitor SulA is complicated; HslVU degrades the Lon substrate SulA [Seong99], whereas HslU also exhibits chaperone activity toward SulA [Seong00]. A similar relationship may exist between HslU and DnaA [Slominska03]. The HslVU protease plays a role in clearing the defective peptides produced in the presence of puromycin [Missiakas96]. HslVU is capable of filling the role of the Lon protease under some conditions [Wu99].

Crystal structures of HslU [Bochtler00] and of the HslVU complex are presented [Bochtler00, Sousa00, Song00, Wang01a, Wang01b, Bochtler01, Wang03a, Kwon03]. HslU and HslV form ring shaped complexes [Rohrwild96] of protein hexamers [Kessel96] that stack into a four-ring cylinder with HslU rings on each end and HslV rings in the center [Rohrwild97]. HslU appears to be homodimeric in the absence of ATP and to form a higher-order complex in the presence of ATP [Yoo96]. HslU and HslV coimmunoprecipitate, whereas the association is labile under chromatographic conditions [Rohrwild96]. Interactions among HslU and HslV are discussed in detail [Yoo97, Huang97, Yoo96, Rohrwild97, Song00, Seong02, Lee03, Kwon03]. The role of ATP binding and hydrolysis in complex formation and activity is discussed [Yoo96, Yoo97a, Shin96, Huang97, Rohrwild96, Yoo96, Seong99, Song00, Wang01c]. Stimulation of HslU-mediated ATP hydrolysis by poly-L-lysine stimulates the peptidase activity of HslV within the HslVU complex [Yoo96a]. The presence of a protein substrate also stimulates HslVU protease activity [Seol97]. The activity of the HslVU complex is discussed in detail [Bogyo97, Huang97, Wang01a].

An hslU mutant exhibits a defect in growth at high temperature and shows abnormally small cell size under some conditions [Katayama96a]. A K63T mutation in the ATP binding site causes defects in ATPase activity and in HslU multimerization [Shin96]. A C287V mutation causes an ATPase defect but does not eliminate ATP-stimulated HslVU complex formation or protease activity [Yoo98]. A C261V mutation inhibits N-ethylmaleimide-mediated dissociation of HslU complexes [Yoo98]. Overproduction of HslU and HslV causes resistance to nitrofurantoin and to UV irradiation in a lon mutant background [Khattar97]. An hslU mutation causes synthetic lethality with a dnaA204 mutation [Slominska03]. An hslU mutation suppresses the heat sensitivity of a dnaA46 mutant [Katayama96a]. Genetic interactions between hslVU and lon are discussed; Lon functions can be carried out by HslVU [Wu99].

HslU has similarity to ClpX [Gottesman93]. HslU has structural similarity to FtsH [Karata01]. HslU has 52% identity to Bacillus subtilis CodX [Kang01]. HslU has similarity, including an ATP/GTP-binding motif, to a protein from Pasteurella haemolytica [Chuang93]. HslU has similarity to Leptospira borgpetersenii serovar hardjobovis HslU [Lin01], to Leishmania infantum HslU [Couvreur02], and to a Lactobacillus leichmannii protein [Becker96]. Structural similarity between Lon and Clp proteases is discussed [Smith99b]. E. coli HslU exhibits stimulatory activity toward Thermotoga maritima HslV [Song03].

Regulation has been described [Chuang93, Peruski94, Rohrwild96]. Transcription is induced by heat shock [Chuang93, Peruski94].

Review: [Goldberg97].

Locations: cytosol, membrane

Map Position: [4,118,439 <- 4,119,770] (88.77 centisomes, 320°)
Length: 1332 bp / 443 aa

Molecular Weight of Polypeptide: 49.594 kD (from nucleotide sequence), 50 kD (experimental)

Molecular Weight of Multimer: 350 kD (experimental) [Kessel96], 450 kD (experimental) [Yoo96]

Unification Links: ASAP:ABE-0012843 , CGSC:34157 , DIP:DIP-31855N , DisProt:DP00100 , EchoBASE:EB1827 , EcoGene:EG11881 , EcoliWiki:b3931 , ModBase:P0A6H5 , OU-Microarray:b3931 , PortEco:hslU , PR:PRO_000022934 , Pride:P0A6H5 , Protein Model Portal:P0A6H5 , RefSeq:NP_418366 , RegulonDB:EG11881 , SMR:P0A6H5 , String:511145.b3931 , UniProt:P0A6H5

Relationship Links: InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR003959 , InterPro:IN-FAMILY:IPR004491 , InterPro:IN-FAMILY:IPR019489 , InterPro:IN-FAMILY:IPR027417 , Panther:IN-FAMILY:PTHR11262:SF3 , PDB:Structure:1DO0 , PDB:Structure:1DO2 , PDB:Structure:1E94 , PDB:Structure:1G4A , PDB:Structure:1G4B , PDB:Structure:1HQY , PDB:Structure:1HT1 , PDB:Structure:1HT2 , PDB:Structure:1YYF , Pfam:IN-FAMILY:PF00004 , Pfam:IN-FAMILY:PF07724 , Pfam:IN-FAMILY:PF10431 , Smart:IN-FAMILY:SM00382 , Smart:IN-FAMILY:SM01086

In Paralogous Gene Group: 221 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0009408 - response to heat Inferred from experiment [Chuang93a]
GO:0006508 - proteolysis Inferred by computational analysis [GOA01a]
GO:0043335 - protein unfolding Inferred by computational analysis [GOA06]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Hsieh11, Lien09, Butland05, Lee03, Wang01c, Wang01a]
GO:0042802 - identical protein binding Inferred from experiment [Lasserre06, Lee03]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0016887 - ATPase activity Inferred by computational analysis [GOA06, GOA01a]
GO:0070011 - peptidase activity, acting on L-amino acid peptides Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009376 - HslUV protease complex Inferred by computational analysis [GOA06, GOA01a]

MultiFun Terms: cell processes adaptations temperature extremes
cell processes cell cycle physiology
cell processes cell division
information transfer protein related chaperoning, repair (refolding)
information transfer protein related turnover, degradation
metabolism degradation of macromolecules proteins/peptides/glycopeptides
regulation type of regulation posttranscriptional proteases, cleavage of compounds

Essentiality data for hslU knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of: HslVU protease

Subunit composition of HslVU protease = [(HslU)6]2[(HslV)6]2
         HslU hexamer = (HslU)6
                 ATPase component of the HslVU protease = HslU
         HslV hexamer = (HslV)6
                 peptidase component of the HslVU protease = HslV

The HslVU protease exhibits ATP-stimulated activity similar to that of the chymotrypsin-like activity of the eukaryotic proteasome [Rohrwild96].

HslU and HslV form ring shaped complexes [Rohrwild96] of protein hexamers [Kessel96] that stack into a four-ring cylinder with HslU rings on each end and HslV rings in the center [Rohrwild97].

Molecular Weight: 820 kD (experimental) [Bochtler00]

Sequence Features

Protein sequence of ATPase component of the HslVU protease with features indicated

Feature Class Location Attached Group Citations Comment
Amino-Acid-Sites-That-Bind 18  
UniProt: ATP; via amide nitrogen and carbonyl oxygen.
Nucleotide-Phosphate-Binding-Region 60 -> 65 ATP
UniProt: ATP.
Mutagenesis-Variant 63  
[Shin96, UniProt11]
UniProt: Can neither bind nor hydrolyze ATP. Do not form multimers, but stays as monomer.
Mutagenesis-Variant 80  
[Song00, UniProt11]
UniProt: Some effect on protease activity.
Mutagenesis-Variant 88  
[Song00, UniProt11]
UniProt: Severly reduced protease activity.
Mutagenesis-Variant 91  
[Song00, UniProt11]
UniProt: Partial loss of protease activity.
Mutagenesis-Variant 92  
[Song00, UniProt11]
UniProt: Partial loss of protease activity.
Mutagenesis-Variant 93  
[Song00, UniProt11]
UniProt: Almost no protease or ATP hydrolysis activity.
Mutagenesis-Variant 95  
[Song00, UniProt11]
UniProt: Partial loss of protease activity.
Amino-Acid-Sites-That-Bind 256  
UniProt: ATP.
Mutagenesis-Variant 262  
[Yoo98, UniProt11]
UniProt: No effect on ATP hydrolysis. Can support HslV-mediated proteolysis at wild-type levels.
Mutagenesis-Variant 266  
[Song00, UniProt11]
UniProt: No effect.
Mutagenesis-Variant 286  
[Song00, UniProt11]
UniProt: Reduced protease activity.
Mutagenesis-Variant 288  
[Yoo98, UniProt11]
UniProt: No ATP hydrolysis activity. Binds ATP with lower affinity than wild-type. Can support HslV-mediated proteolysis to some extent.
Mutagenesis-Variant 312  
[Song00, UniProt11]
UniProt: No effect.
Amino-Acid-Sites-That-Bind 321  
UniProt: ATP.
Mutagenesis-Variant 321  
[Song00, UniProt11]
UniProt: Complete loss of activity.
Mutagenesis-Variant 325  
[Song00, UniProt11]
UniProt: Complete loss of activity. Forms wild-type complexes with HslV and is able to bind ATP.
Mutagenesis-Variant 385  
[Song00, UniProt11]
UniProt: No effect.
Amino-Acid-Sites-That-Bind 393  
UniProt: ATP.
Mutagenesis-Variant 393  
[Song00, UniProt11]
UniProt: Complete loss of activity.
Mutagenesis-Variant 436  
UniProt: Partial loss of protease activity; when associated with K-437.
Mutagenesis-Variant 437  
UniProt: Partial loss of protease activity; when associated with K-436.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b3931 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11881; confirmed by SwissProt match.


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Becker96: Becker J, Brendel M (1996). "Molecular characterization of the xerC gene of Lactobacillus leichmannii encoding a site-specific recombinase and two adjacent heat shock genes." Curr Microbiol 32(4);232-6. PMID: 8867465

Bochtler00: Bochtler M, Hartmann C, Song HK, Bourenkov GP, Bartunik HD, Huber R (2000). "The structures of HsIU and the ATP-dependent protease HsIU-HsIV." Nature 403(6771);800-5. PMID: 10693812

Bochtler01: Bochtler M, Song HK, Hartmann C, Ramachandran R, Huber R (2001). "The quaternary arrangement of HslU and HslV in a cocrystal: a response to Wang, Yale." J Struct Biol 135(3);281-93. PMID: 11722168

Bogyo97: Bogyo M, McMaster JS, Gaczynska M, Tortorella D, Goldberg AL, Ploegh H (1997). "Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors." Proc Natl Acad Sci U S A 94(13);6629-34. PMID: 9192616

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

Chuang93: Chuang SE, Burland V, Plunkett G, Daniels DL, Blattner FR (1993). "Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli." Gene 1993;134(1);1-6. PMID: 8244018

Chuang93a: Chuang SE, Blattner FR (1993). "Characterization of twenty-six new heat shock genes of Escherichia coli." J Bacteriol 175(16);5242-52. PMID: 8349564

Couvreur02: Couvreur B, Wattiez R, Bollen A, Falmagne P, Le Ray D, Dujardin JC (2002). "Eubacterial HslV and HslU subunits homologs in primordial eukaryotes." Mol Biol Evol 19(12);2110-7. PMID: 12446803

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

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

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."

Goldberg97: Goldberg AL, Akopian TN, Kisselev AF, Lee DH, Rohrwild M (1997). "New insights into the mechanisms and importance of the proteasome in intracellular protein degradation." Biol Chem 378(3-4);131-40. PMID: 9165063

Gottesman93: Gottesman S, Clark WP, de Crecy-Lagard V, Maurizi MR (1993). "ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities." J Biol Chem 1993;268(30);22618-26. PMID: 8226770

Hsieh11: Hsieh FC, Chen CT, Weng YT, Peng SS, Chen YC, Huang LY, Hu HT, Wu YL, Lin NC, Wu WF (2011). "Stepwise activity of ClpY (HslU) mutants in the processive degradation of Escherichia coli ClpYQ (HslUV) protease substrates." J Bacteriol 193(19);5465-76. PMID: 21803990

Huang97: Huang H, Goldberg AL (1997). "Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis." J Biol Chem 272(34);21364-72. PMID: 9261150

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

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

Kang01: Kang MS, Lim BK, Seong IS, Seol JH, Tanahashi N, Tanaka K, Chung CH (2001). "The ATP-dependent CodWX (HslVU) protease in Bacillus subtilis is an N-terminal serine protease." EMBO J 20(4);734-42. PMID: 11179218

Karata01: Karata K, Verma CS, Wilkinson AJ, Ogura T (2001). "Probing the mechanism of ATP hydrolysis and substrate translocation in the AAA protease FtsH by modelling and mutagenesis." Mol Microbiol 39(4);890-903. PMID: 11251810

Katayama96a: Katayama T, Kubota T, Takata M, Akimitsu N, Sekimizu K (1996). "Disruption of the hslU gene, which encodes an ATPase subunit of the eukaryotic 26S proteasome homolog in Escherichia coli, suppresses the temperature-sensitive dnaA46 mutation." Biochem Biophys Res Commun 229(1);219-24. PMID: 8954109

Kessel96: Kessel M, Wu W, Gottesman S, Kocsis E, Steven AC, Maurizi MR (1996). "Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY." FEBS Lett 398(2-3);274-8. PMID: 8977122

Khattar97: Khattar MM (1997). "Overexpression of the hslVU operon suppresses SOS-mediated inhibition of cell division in Escherichia coli." FEBS Lett 414(2);402-4. PMID: 9315728

Kwon03: Kwon AR, Kessler BM, Overkleeft HS, McKay DB (2003). "Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome." J Mol Biol 330(2);185-95. PMID: 12823960

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Lee03: Lee YY, Chang CF, Kuo CL, Chen MC, Yu CH, Lin PI, Wu WF (2003). "Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid system." J Bacteriol 185(8);2393-401. PMID: 12670962

Lien09: Lien HY, Shy RS, Peng SS, Wu YL, Weng YT, Chen HH, Su PC, Ng WF, Chen YC, Chang PY, Wu WF (2009). "Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system." J Bacteriol 191(13);4218-31. PMID: 19395483

Lin01: Lin M, Li Y (2001). "PCR genome walking identifies a genetic locus comprising two heat shock genes (hslV and hslU) from Leptospira borgpetersenii serovar hardjobovis." Curr Microbiol 43(6);452-6. PMID: 11685516

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

Missiakas96: Missiakas D, Schwager F, Betton JM, Georgopoulos C, Raina S (1996). "Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli." EMBO J 15(24);6899-909. PMID: 9003766

Peruski94: Peruski LF, Neidhardt FC (1994). "Identification of a conditionally essential heat shock protein in Escherichia coli." Biochim Biophys Acta 1207(2);165-72. PMID: 8075150

Rohrwild96: Rohrwild M, Coux O, Huang HC, Moerschell RP, Yoo SJ, Seol JH, Chung CH, Goldberg AL (1996). "HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome." Proc Natl Acad Sci U S A 93(12);5808-13. PMID: 8650174

Rohrwild97: Rohrwild M, Pfeifer G, Santarius U, Muller SA, Huang HC, Engel A, Baumeister W, Goldberg AL (1997). "The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome." Nat Struct Biol 4(2);133-9. PMID: 9033594

Seol97: Seol JH, Yoo SJ, Shin DH, Shim YK, Kang MS, Goldberg AL, Chung CH (1997). "The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase." Eur J Biochem 247(3);1143-50. PMID: 9288941

Seong00: Seong IS, Oh JY, Lee JW, Tanaka K, Chung CH (2000). "The HslU ATPase acts as a molecular chaperone in prevention of aggregation of SulA, an inhibitor of cell division in Escherichia coli." FEBS Lett 477(3);224-9. PMID: 10908725

Seong02: Seong IS, Kang MS, Choi MK, Lee JW, Koh OJ, Wang J, Eom SH, Chung CH (2002). "The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase." J Biol Chem 277(29);25976-82. PMID: 12011053

Seong99: Seong IS, Oh JY, Yoo SJ, Seol JH, Chung CH (1999). "ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli." FEBS Lett 456(1);211-4. PMID: 10452560

Shin96: Shin DH, Yoo SJ, Shim YK, Seol JH, Kang MS, Chung CH (1996). "Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli." FEBS Lett 398(2-3);151-4. PMID: 8977096

Slominska03: Slominska M, Wahl A, Wegrzyn G, Skarstad K (2003). "Degradation of mutant initiator protein DnaA204 by proteases ClpP, ClpQ and Lon is prevented when DNA is SeqA-free." Biochem J 370(Pt 3);867-71. PMID: 12479794

Smith99b: Smith CK, Baker TA, Sauer RT (1999). "Lon and Clp family proteases and chaperones share homologous substrate-recognition domains." Proc Natl Acad Sci U S A 96(12);6678-82. PMID: 10359771

Song00: Song HK, Hartmann C, Ramachandran R, Bochtler M, Behrendt R, Moroder L, Huber R (2000). "Mutational studies on HslU and its docking mode with HslV." Proc Natl Acad Sci U S A 97(26);14103-8. PMID: 11114186

Song03: Song HK, Bochtler M, Azim MK, Hartmann C, Huber R, Ramachandran R (2003). "Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV." Biophys Chem 100(1-3);437-52. PMID: 12646382

Sousa00: Sousa MC, Trame CB, Tsuruta H, Wilbanks SM, Reddy VS, McKay DB (2000). "Crystal and solution structures of an HslUV protease-chaperone complex." Cell 103(4);633-43. PMID: 11106733

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Wang01a: Wang J, Song JJ, Franklin MC, Kamtekar S, Im YJ, Rho SH, Seong IS, Lee CS, Chung CH, Eom SH (2001). "Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism." Structure (Camb) 9(2);177-84. PMID: 11250202

Wang01b: Wang J (2001). "A corrected quaternary arrangement of the peptidase HslV and atpase HslU in a cocrystal structure." J Struct Biol 134(1);15-24. PMID: 11469873

Wang01c: Wang J, Song JJ, Seong IS, Franklin MC, Kamtekar S, Eom SH, Chung CH (2001). "Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU." Structure (Camb) 9(11);1107-16. PMID: 11709174

Wang03a: Wang J (2003). "A second response in correcting the HslV-HslU quaternary structure." J Struct Biol 141(1);7-8. PMID: 12576015

Wu99: Wu WF, Zhou Y, Gottesman S (1999). "Redundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV) protease." J Bacteriol 181(12);3681-7. PMID: 10368141

Yoo96: Yoo SJ, Seol JH, Shin DH, Rohrwild M, Kang MS, Tanaka K, Goldberg AL, Chung CH (1996). "Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli." J Biol Chem 271(24);14035-40. PMID: 8662828

Yoo96a: Yoo SJ, Seol JH, Kang MS, Chung CH (1996). "Poly-L-lysine activates both peptide and ATP hydrolysis by the ATP-dependent HslVU protease in Escherichia coli." Biochem Biophys Res Commun 229(2);531-5. PMID: 8954932

Yoo97: Yoo SJ, Shim YK, Seong IS, Seol JH, Kang MS, Chung CH (1997). "Mutagenesis of two N-terminal Thr and five Ser residues in HslV, the proteolytic component of the ATP-dependent HslVU protease." FEBS Lett 412(1);57-60. PMID: 9257689

Yoo97a: Yoo SJ, Seol JH, Seong IS, Kang MS, Chung CH (1997). "ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli." Biochem Biophys Res Commun 238(2);581-5. PMID: 9299555

Yoo98: Yoo SJ, Kim HH, Shin DH, Lee CS, Seong IS, Seol JH, Shimbara N, Tanaka K, Chung CH (1998). "Effects of the cys mutations on structure and function of the ATP-dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in HslU uncouples the ATP-dependent proteolysis by HslvU from ATP hydrolysis." J Biol Chem 273(36);22929-35. PMID: 9722513

Other References Related to Gene Regulation

Lien09a: Lien HY, Yu CH, Liou CM, Wu WF (2009). "Regulation of clpQY (hslVU) Gene Expression in Escherichia coli." Open Microbiol J 3;29-39. PMID: 19440251

Nonaka06: Nonaka G, Blankschien M, Herman C, Gross CA, Rhodius VA (2006). "Regulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress." Genes Dev 20(13);1776-89. PMID: 16818608

Wade06: Wade JT, Roa DC, Grainger DC, Hurd D, Busby SJ, Struhl K, Nudler E (2006). "Extensive functional overlap between sigma factors in Escherichia coli." Nat Struct Mol Biol 13(9);806-14. PMID: 16892065

Wagner09: Wagner MA, Zahrl D, Rieser G, Koraimann G (2009). "Growth phase- and cell division-dependent activation and inactivation of the {sigma}32 regulon in Escherichia coli." J Bacteriol 191(5);1695-702. PMID: 19114495

Zahrl06: Zahrl D, Wagner M, Bischof K, Koraimann G (2006). "Expression and assembly of a functional type IV secretion system elicit extracytoplasmic and cytoplasmic stress responses in Escherichia coli." J Bacteriol 188(18);6611-21. PMID: 16952953

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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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