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Escherichia coli K-12 substr. MG1655 Enzyme: methionyl-tRNA synthetase



Gene: metG Accession Numbers: EG10586 (EcoCyc), b2114, ECK2107

Synonyms: MetRS

Regulation Summary Diagram: ?

Regulation summary diagram for metG

Subunit composition of methionyl-tRNA synthetase = [MetG]2
         methionyl-tRNA synthetase = MetG

Summary:
Methionyl-tRNA synthetase (MetRS) is a member of the family of aminoacyl-tRNA synthetases, which interpret the genetic code by covalently linking amino acids to their specific tRNA molecules. The reaction is driven by ATP hydrolysis. MetRS belongs to the Class I aminoacyl-tRNA synthetases; apart from sequence motifs whithin the active site, the different enzymes show little similarity in their primary amino acid sequences [Eriani90, Landes95].

The biochemical properties and reaction mechanism of MetRS have been studied extensively; e.g. [Lemoine68, Blanquet72, Blanquet73, Blanquet73a, Lawrence73, Lawrence73a, Lawrence74, Fayat74, Blanquet74, Blanquet75, Hyafil76, Hyafil77, Old77, Fayat77, Hyafil78, Fayat80, Smith82, Mayaux82, Lowe83, Rosevear88, McArdell89, Williams91]. MetRS acylates both initiator tRNAfMet and elongator tRNAMet; acylation of tRNAfMet appears to be more efficient [Ron78]. MetRS contains one zinc atom per active site that is coordinated by four cysteine residues which are essential for activity [Landro93, Fourmy93, Fourmy93a, Xu93].

Crystal structures of MetRS have been determined [Risler81, Zelwer82, Blow83, Brunie90, Mechulam99, Serre01, Crepin03, Schmitt09]. The structural domains can be expressed separately and can reconstitute active MetRS enzyme [Burbaum91, Kim98]. The C-terminal domain can function independently for specific binding of the tRNA anticodon stem-loop [Gale95]. The ATP binding site was identified by affinity labeling [Hountondji90]. Catalysis is proposed to involve an induced fit mechanism [Alexander99]. The evaluation of enzymes containing point mutations in residues that may link the anticodon binding motif to the catalytic domain [Alexander99, Banerjee09] as well as comparisons between crystal structures of the apo- and methionine-bound enzyme [Serre01] support this hypothesis. Molecular dynamics simulations confirm significant motility of the enzyme, suggesting that Trp461 mediates the distribution of structural ensembles [Budiman07] and confirming the pathways of communication between distant sites [Ghosh07, Ghosh08]. The methionine binding site was predicted [Datta04], and non-hydrolyzable ATP analogues and methionine and methionyl adenylate analogues have been used to study conformational changes during catalysis [Williams91a, Crepin03, Vaughan05].

Regions within MetRS that interact with tRNAfMet [Hountondji85, Valenzuela86, Leon87, Leon87a, Schulman87, Hountondji90a] and tRNAMet [Leon87b] have been determined [Kim94]. The Trp461 residue may interact directly with the tRNA anticodon loop [Ghosh90]; Asp391 may interact directly with U36 [Kim93]. Suppressor enzymes that are able to aminoacylate methionine amber tRNA carry mutations in the vicinity of Trp461 [Meinnel91, Schmitt93].

Site-directed mutagenesis and analysis of the mutant enzymes has been used to study the domain structure, catalytic properties and the roles of active site residues of the enzyme [Mellot89, Starzyk89, Casina11]. Lys335 is required for methionine activation [Mechulam91]; Tyr358 [Ghosh91] contributes to the ATP-PPi exchange reaction. All residues within the 332KMSKS336 motif [Schmitt94] and His21 and His24 within the N-terminal HLGH motif [Schmitt95] are important for methionyl adenylate formation. Asp55 and Arg233 appear to play a role in stabilizing the transition state for formation of the methionine adenylate [Ghosh91a]. His301 and Trp305 are required for the interaction with methionine [Ghosh91a, Fourmy91], and Trp305 and Tyr15 serve to discriminate against homocysteine [Kim93a]. The conserved Pro14 within the nucleotide binding fold may open an amino acid binding cleft [Burbaum92], and a Leu13Gly [Link06] and other selected mutations [Tanrikulu09] allow use of azidonorleucine as a substrate [Schmitt09]. Arg395 [Ghosh91b], Asp391 [Kim93], Asp449 and Asp456 [Schmitt93] play roles in tRNA recognition. Mutations in the C-terminal domain peptide appendix affect interactions with the acceptor stem of tRNAfMet and enzyme dimerization [Kim93b, Crepin02]. Ile29 appears to be involved in discrimination against tRNAThrGGU [Kim98a]. Residues within the CP1 domain that contains the zinc-binding peptide contribute to the stabilization of the transition state [Fourmy95].

Specificity determinants within tRNAfMet that are important for recognition by MetRS have been investigated [Schulman73, Dube73, Bruton74, Wetzel77, Schulman77, Jacques77, Schulman83, Ohtsuka83, Schulman83a, Petersen84, Schulman84, Doi85, Doi85a, Schulman85, Ferguson86, Pelka86, Perreault89, Chattapadhyay90, Meinnel91a, Meinnel92, Meinnel93, Gale96, Jones11]. The acceptor stem [Meinnel93] and the anticodon loop including the wobble base play an essential role. Unlike CysRS and other Class I tRNA synthethases, MetRS does not discriminate against an unpaired C-A that is unique to the 1-72 position of tRNAfMet [Liu11a].

MetRS can reject misactivated homocysteine by tRNA-independent pre-transfer editing [Fersht79, Jakubowski81, Jakubowski90, Jakubowski93, Jakubowski93a, Kim93a, Jakubowski96]. The homocysteine-AMP intermediate is destroyed in an intramolecular cyclization reaction in which the thiolate side chain of homocysteine displaces the AMP group, forming homocysteine-thiolactone [Jakubowski81]. A C-terminal region of MetRS is suggested to play a role in editing in vivo [Gao94].

MetRS expression is upregulated under methionine-limited growth conditions [Archibold72] and by reduced acylation levels of tRNAfMet [Cassio75]. MetRS levels are coupled to the growth rate [Cassio75a].

The metG gene encoding MetRS has been cloned [Barker82, Dardel84]. Overproduction of MetRS leads to increased levels of adenylylated bis(5'-nucleosidyl) tetraphosphates (Ap4N) in the cell [Brevet89]. A transposon insertion into the the C-terminal coding region of metG results in a 10,000-fold higher frequency of persister formation than wild type [Girgis12].

Inhibitors of MetRS activity [Lee98, Lee99, Lee01, Lee03, Kim03, Kim05, Kim06], L-methionine analogs that can be activated by MetRS [Kiick01, Kiick02], and tRNAs that can be mischarged by MetRS [Jones11] have been identified.

Reviews: [Meinnel90, Mans91, Meinnel93a, Jakubowski94, Schmitt96, Vaughan02, Jakubowski11, Perona12]

Citations: [Svensson67, Cassio68, Cassio68a, Svensson68, Cassio70, Bruton70, Cassio71, Cassio71a, Waller71, Osumi71, RobertGero72, Bruton74a, Monteilhet74, Armstrong75, Bruton75, Gulik76, Blanquet76, Fayat77a, Kalogerakos79, Posorske79, Fayat79, Hountondji79, YamashiroMatsum81, Schulman81, Dessen82, Valenzuela84, Dessen85, Hountondji86, Urbanowski87, Walker88, Hirel88, Berne90, Dardel91, Graffe92, Shepard92, Romby92, Varshney92, Old93, Kalogerakos94, Kim97, Gillet97, Jakubowski00, Jakubowski02, Kabir01, Abdeljabbar09, Sikora09, Truong12, Strom14]

Gene Citations: [Dardel90]

Locations: cytosol, membrane

Map Position: [2,192,322 -> 2,194,355] (47.25 centisomes, 170°)
Length: 2034 bp / 677 aa

Molecular Weight of Polypeptide: 76.255 kD (from nucleotide sequence), 85.0 kD (experimental) [Koch74 ]

Molecular Weight of Multimer: 173.0 kD (experimental) [Lemoine68]

Unification Links: ASAP:ABE-0006991 , CGSC:510 , DIP:DIP-10194N , EchoBASE:EB0581 , EcoGene:EG10586 , EcoliWiki:b2114 , ModBase:P00959 , OU-Microarray:b2114 , PortEco:metG , PR:PRO_000023213 , Pride:P00959 , Protein Model Portal:P00959 , RefSeq:NP_416617 , RegulonDB:EG10586 , SMR:P00959 , String:511145.b2114 , Swiss-Model:P00959 , UniProt:P00959

Relationship Links: InterPro:IN-FAMILY:IPR001412 , InterPro:IN-FAMILY:IPR002547 , InterPro:IN-FAMILY:IPR004495 , InterPro:IN-FAMILY:IPR009080 , InterPro:IN-FAMILY:IPR012340 , InterPro:IN-FAMILY:IPR014729 , InterPro:IN-FAMILY:IPR014758 , InterPro:IN-FAMILY:IPR015413 , InterPro:IN-FAMILY:IPR023458 , InterPro:IN-FAMILY:IPR029038 , PDB:Structure:1F4L , PDB:Structure:1MEA , PDB:Structure:1MED , PDB:Structure:1P7P , PDB:Structure:1PFU , PDB:Structure:1PFV , PDB:Structure:1PFW , PDB:Structure:1PFY , PDB:Structure:1PG0 , PDB:Structure:1PG2 , PDB:Structure:1QQT , PDB:Structure:3H97 , PDB:Structure:3H99 , PDB:Structure:3H9B , PDB:Structure:3H9C , Pfam:IN-FAMILY:PF01588 , Pfam:IN-FAMILY:PF09334 , Prints:IN-FAMILY:PR01041 , Prosite:IN-FAMILY:PS00178 , Prosite:IN-FAMILY:PS50886

In Paralogous Gene Group: 7 (4 members) , 150 (2 members) , 378 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006431 - methionyl-tRNA aminoacylation Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Archibold73, Gaudet10]
GO:0006412 - translation Inferred by computational analysis [UniProtGOA11a]
GO:0006418 - tRNA aminoacylation for protein translation Inferred by computational analysis [GOA01a]
Molecular Function: GO:0004825 - methionine-tRNA ligase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Lemoine68, Gaudet10]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06]
GO:0008270 - zinc ion binding Inferred from experiment [Mayaux81]
GO:0042803 - protein homodimerization activity Inferred from experiment [Koch74]
GO:0000049 - tRNA binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0004812 - aminoacyl-tRNA ligase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a]

MultiFun Terms: information transfer protein related amino acid -activation

Essentiality data for metG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Credits:
Last-Curated ? 21-Apr-2015 by Keseler I , SRI International


Enzymatic reaction of: methionyl-tRNA synthetase

EC Number: 6.1.1.10

initiator tRNAmet + L-methionine + ATP + H+ <=> an L-methionyl-[initiator tRNAmet] + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: tRNA charging

Cofactors or Prosthetic Groups: Mg2+ [Blanquet73a], Zn2+ [Mayaux82, Mayaux81, Posorske79, Xu93, Landro93, Fourmy93a, Fourmy93]

Inhibitors (Unknown Mechanism): adenosine [Lawrence73a]


Enzymatic reaction of: methionyl-tRNA synthetase

EC Number: 6.1.1.10

elongator tRNAmet + L-methionine + ATP + H+ <=> an L-methionyl-[elongator tRNAmet] + AMP + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: tRNA charging

Cofactors or Prosthetic Groups: Mg2+ [Lawrence73], Zn2+ [Mayaux82, Mayaux81, Posorske79, Xu93, Landro93, Fourmy93a, Fourmy93]

Kinetic Parameters:

Substrate
Km (μM)
Citations
L-methionine
40.0
[Lemoine68]
L-methionine
78.0
[Armstrong75, BRENDA14]
ATP
300.0
[Lemoine68]


Sequence Features

Protein sequence of methionyl-tRNA synthetase with features indicated

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[UniProt15]
UniProt: Removed.
Chain 2 -> 677
[UniProt09]
UniProt: Methionyl-tRNA synthetase;
Protein-Segment 15 -> 25
[UniProt15]
UniProt: "HIGH" region; Sequence Annotation Type: short sequence motif.
Metal-Binding-Site 146
[UniProt15]
UniProt: Zinc.
Metal-Binding-Site 149
[UniProt15]
UniProt: Zinc.
Metal-Binding-Site 159
[UniProt15]
UniProt: Zinc.
Metal-Binding-Site 162
[UniProt15]
UniProt: Zinc.
Protein-Segment 333 -> 337
[UniProt15]
UniProt: "KMSKS" region; Sequence Annotation Type: short sequence motif.
Amino-Acid-Sites-That-Bind 336
[UniProt15]
UniProt: ATP.
Mutagenesis-Variant 336
[Fourmy91, Fourmy93, UniProt11]
K → A, E, Q or R: Loss of activity.
Conserved-Region 575 -> 677
[UniProt09]
UniProt: tRNA-binding;


Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Notes:

History:
10/20/97 Gene b2114 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10586; confirmed by SwissProt match.


References

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Alexander99: Alexander RW, Schimmel P (1999). "Evidence for breaking domain-domain functional communication in a synthetase-tRNA complex." Biochemistry 38(49);16359-65. PMID: 10587461

Archibold72: Archibold ER, Williams LS (1972). "Regulation of synthesis of methionyl-, prolyl-, and threonyl-transfer ribonucleic acid synthetases of Escherichia coli." J Bacteriol 109(3);1020-6. PMID: 4551738

Archibold73: Archibold ER, Williams LS (1973). "Regulation of methionyl-transfer ribonucleic acid synthetase formation in Escherichia coli and Salmonella typhimurium." J Bacteriol 114(3);1007-13. PMID: 4576394

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

Armstrong75: Armstrong JB, Fairfield JA (1975). "A new method for the isolation of methionyl transfer RNA synthetase mutants from Escherichia coli." Can J Microbiol 21(6);754-8. PMID: 1097064

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

Banerjee09: Banerjee P, Warf MB, Alexander R (2009). "Effect of a domain-spanning disulfide on aminoacyl-tRNA synthetase activity." Biochemistry 48(42);10113-9. PMID: 19772352

Barker82: Barker DG, Ebel JP, Jakes R, Bruton CJ (1982). "Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment." Eur J Biochem 127(3);449-57. PMID: 6756915

Berne90: Berne PF, Schmitter JM, Blanquet S (1990). "Peptide and protein carboxyl-terminal labeling through carboxypeptidase Y-catalyzed transpeptidation." J Biol Chem 265(32);19551-9. PMID: 2246241

Blanquet72: Blanquet S, Fayat G, Waller JP, Iwatsubo M (1972). "The mechanism of reaction of methionyl-tRNA synthetase from Escherichia coli. Interaction of the enzyme with ligands of the amino-acid-activation reaction." Eur J Biochem 24(3);461-9. PMID: 4621706

Blanquet73: Blanquet S, Iwatsubo M, Waller JP (1973). "The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. 1. Fluorescence studies on tRNAMet binding as a function of ligands, ions and pH." Eur J Biochem 36(1);213-26. PMID: 4581817

Blanquet73a: Blanquet S, Petrissant G, Waller JP (1973). "The mechanism of action of methionyl-tRNA synthetase. 2. Interaction of the enzyme with specific and unspecific tRNAs." Eur J Biochem 36(1);227-33. PMID: 4581818

Blanquet74: Blanquet S, Fayat G, Waller JP (1974). "The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Mechanism of the amino-acid activation reaction catalyzed by the native and the trypsin-modified enzymes." Eur J Biochem 44(2);343-51. PMID: 4365501

Blanquet75: Blanquet S, Fayat G, Poiret M, Waller JP (1975). "The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Inhibition by adenosine and 8-aminoadenosine of the amino-acid activation reaction." Eur J Biochem 51(2);567-71. PMID: 168070

Blanquet76: Blanquet S, Dessen P (1976). "Antico-operative binding of bacterial and mammalian initiator tRNAMet to methionyl-tRNA synthetase from escherichia coli." J Mol Biol 103(4);765-84. PMID: 781286

Blow83: Blow DM, Bhat TN, Metcalfe A, Risler JL, Brunie S, Zelwer C (1983). "Structural homology in the amino-terminal domains of two aminoacyl-tRNA synthetases." J Mol Biol 171(4);571-6. PMID: 6363712

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Brevet89: Brevet A, Chen J, Leveque F, Plateau P, Blanquet S (1989). "In vivo synthesis of adenylylated bis(5'-nucleosidyl) tetraphosphates (Ap4N) by Escherichia coli aminoacyl-tRNA synthetases." Proc Natl Acad Sci U S A 86(21);8275-9. PMID: 2554306

Brunie90: Brunie S, Zelwer C, Risler JL (1990). "Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP." J Mol Biol 216(2);411-24. PMID: 2254937

Bruton70: Bruton CJ, Hartley BS (1970). "Chemical studies on methionyl-tRNA synthetase from Escherichia coli." J Mol Biol 52(2);165-78. PMID: 4922213

Bruton74: Bruton CJ, Clark BF (1974). "The role of the anticodon in the interaction between methionyl-tRNA synthetase and bacterial initiator tRNA." Nucleic Acids Res 1(2);217-21. PMID: 4607244

Bruton74a: Bruton CJ, Jakes R, Koch GL (1974). "Repeated sequences in methionyl-tRNA synthetase from E. coli." FEBS Lett 45(1);26-8. PMID: 4607017

Bruton75: Bruton C, Jakes R, Atkinson T (1975). "Gram-scale purification of methionyl-tRNA and tyrosyl-tRNA synthetases from Escherichia coli." Eur J Biochem 59(2);327-33. PMID: 1107028

Budiman07: Budiman ME, Knaggs MH, Fetrow JS, Alexander RW (2007). "Using molecular dynamics to map interaction networks in an aminoacyl-tRNA synthetase." Proteins 68(3);670-89. PMID: 17510965

Burbaum91: Burbaum JJ, Schimmel P (1991). "Assembly of a class I tRNA synthetase from products of an artificially split gene." Biochemistry 30(2);319-24. PMID: 1988033

Burbaum92: Burbaum JJ, Schimmel P (1992). "Amino acid binding by the class I aminoacyl-tRNA synthetases: role for a conserved proline in the signature sequence." Protein Sci 1(5);575-81. PMID: 1304356

Casina11: Casina VC, Lobashevsky AA, McKinney WE, Brown CL, Alexander RW (2011). "Role for a conserved structural motif in assembly of a class I aminoacyl-tRNA synthetase active site." Biochemistry 50(5);763-9. PMID: 21175197

Cassio68: Cassio D (1968). "[Study of methionyl tRNA synthetase of Escherichia coli. 2. Selective and reversible inactivation of the capacity to activate tRNA]." Eur J Biochem 4(2);222-4. PMID: 4871905

Cassio68a: Cassio D, Waller JP (1968). "[Study of methionyl-tRNA synthetase from Escherichia coli. 3. Dissociation into active subunits by the action of an extrinsic factor]." Eur J Biochem 5(1);33-41. PMID: 4876744

Cassio70: Cassio D, Lawrence F, Lawrence DA (1970). "Level of methionyl-tRNA synthetase in merodiploids of Escherichia coli K12." Eur J Biochem 15(2);331-4. PMID: 4926130

Cassio71: Cassio D, Waller J (1971). "Purification and properties of methionyl-tRNA synthetase from E. coli K 12 carrying the F32 episome." FEBS Lett 12(6);309-312. PMID: 11945606

Cassio71a: Cassio D, Waller JP (1971). "Modification of methionyl-tRNA synthetase by proteolytic cleavage and properties of the trypsin-modified enzyme." Eur J Biochem 20(2);283-300. PMID: 4934682

Cassio75: Cassio D (1975). "Role of methionyl-transfer ribonucleic acid in the regulation of methionyl-transfer ribonucleic acid synthetase of Escherichia coli K-12." J Bacteriol 123(2);589-97. PMID: 1097419

Cassio75a: Cassio D, Mathien Y, Waller JP (1975). "Enhanced level and metabolic regulation of methionyl-transfer ribonucleic acid synthetase in different strains of Escherichia coli K-12." J Bacteriol 123(2);580-8. PMID: 1097418

Chattapadhyay90: Chattapadhyay R, Pelka H, Schulman LH (1990). "Initiation of in vivo protein synthesis with non-methionine amino acids." Biochemistry 29(18);4263-8. PMID: 2112406

Crepin02: Crepin T, Schmitt E, Blanquet S, Mechulam Y (2002). "Structure and function of the C-terminal domain of methionyl-tRNA synthetase." Biochemistry 41(43);13003-11. PMID: 12390027

Crepin03: Crepin T, Schmitt E, Mechulam Y, Sampson PB, Vaughan MD, Honek JF, Blanquet S (2003). "Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase." J Mol Biol 332(1);59-72. PMID: 12946347

Dardel84: Dardel F, Fayat G, Blanquet S (1984). "Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene." J Bacteriol 160(3);1115-22. PMID: 6094501

Dardel90: Dardel F, Panvert M, Fayat G (1990). "Transcription and regulation of expression of the Escherichia coli methionyl-tRNA synthetase gene." Mol Gen Genet 223(1);121-33. PMID: 2259334

Dardel91: Dardel F, Panvert M, Blanquet S, Fayat G (1991). "Locations of the metG and mrp genes on the physical map of Escherichia coli." J Bacteriol 173(11);3273. PMID: 1675209

Datta04: Datta D, Vaidehi N, Zhang D, Goddard WA (2004). "Selectivity and specificity of substrate binding in methionyl-tRNA synthetase." Protein Sci 13(10);2693-705. PMID: 15388861

Dessen82: Dessen P, Fayat G, Zaccai G, Blanquet S (1982). "Neutron-scattering studies of the binding of initiator tRNAMet to escherichia coli trypsin modified methionyl-tRNA synthetase." J Mol Biol 154(4);603-13. PMID: 7045381

Dessen85: Dessen P, Zaccai G, Blanquet S (1985). "Methionyl-tRNA synthetase from E. coli: direct evidence for exchange of protomers in the dimeric enzyme by using deuteration and small-angle neutron scattering." Biochimie 67(6);637-41. PMID: 3902100

Doi85: Doi T, Yamane A, Matsugi J, Ohtsuka E, Ikehara M (1985). "Replacement and insertion of nucleotides at the anticodon loop of E. coli tRNAMetf by ligation of chemically synthesized ribooligonucleotides." Nucleic Acids Res 13(10);3685-97. PMID: 3892480

Doi85a: Doi T, Morioka H, Matsugi J, Ohtsuka E, Ikehara M (1985). "Modification of the amino acid acceptor stem of E. coli tRNAMetf by ligation of chemically synthesized ribooligonucleotides." FEBS Lett 190(1);125-8. PMID: 2412892

Dube73: Dube SK (1973). "Evidence of "three point" attachment of tRNA to methionyl tRNA synthetase." Nat New Biol 243(125);103-5. PMID: 4575301

Eriani90: Eriani G, Delarue M, Poch O, Gangloff J, Moras D (1990). "Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs." Nature 347(6289);203-6. PMID: 2203971

Fayat74: Fayat G, Waller JP (1974). "The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Equilibrium-dialysis studies on the binding of methionine, ATP and ATP-Mg2+ by the native and trypsin-modified enzymes." Eur J Biochem 44(2);335-42. PMID: 4600363

Fayat77: Fayat G, Fromant M, Blanquet S (1977). "Couplings between the sites for methionine and adenosine 5'-triphosphate in the amino acid activation reaction catalyzed by trypsin-modified methionyl-transfer RNA synthetase from Escherichia coli." Biochemistry 16(11);2570-9. PMID: 193563

Fayat77a: Fayat G, Fromant M, Kahn D, Blanquet S (1977). "Affinity chromatography on agarose-hexyl-adenosine-5'-phosphate of methionyl-tRNA synthetase from Escherichia coli. Application of the couplings between the methionine and ATP sites." Eur J Biochem 78(2);333-6. PMID: 334536

Fayat79: Fayat G, Hountondji C, Blanquet S (1979). "Methionyl-tRNA synthetase from Escherichia coli. Inactivation and labeling by periodate-treated initiator tRNA." Eur J Biochem 96(1);87-92. PMID: 222589

Fayat80: Fayat G, Blanquet S, Nageswara Rao BD, Cohn M (1980). "31P NMR of the reversible methionine activation reaction catalyzed by methionyl-tRNA synthetase of Escherichia coli. Equilibrium, interconversion rates, and NMR parameters of the enzyme-bound species." J Biol Chem 255(17);8164-9. PMID: 6997291

Ferguson86: Ferguson BQ, Yang DC (1986). "Methionyl-tRNA synthetase induced 3'-terminal and delocalized conformational transition in tRNAfMet: steady-state fluorescence of tRNA with a single fluorophore." Biochemistry 25(3);529-39. PMID: 3513829

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Other References Related to Gene Regulation

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305


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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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