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Gene Review

metG  -  methionyl-tRNA synthetase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2107, JW2101
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Disease relevance of metG


High impact information on metG


Chemical compound and disease context of metG


Biological context of metG


Associations of metG with chemical compounds


Other interactions of metG

  • The regulation of metG expression was investigated by means of fusions to the lacZ gene [11].

Analytical, diagnostic and therapeutic context of metG


  1. Molecular cloning and primary structure of the Escherichia coli methionyl-tRNA synthetase gene. Dardel, F., Fayat, G., Blanquet, S. J. Bacteriol. (1984) [Pubmed]
  2. Methionyl-tRNA synthetase from Bacillus stearothermophilus: structural and functional identities with the Escherichia coli enzyme. Mechulam, Y., Schmitt, E., Panvert, M., Schmitter, J.M., Lapadat-Tapolsky, M., Meinnel, T., Dessen, P., Blanquet, S., Fayat, G. Nucleic Acids Res. (1991) [Pubmed]
  3. Mode of action and biochemical characterization of REP8839, a novel inhibitor of methionyl-tRNA synthetase. Ochsner, U.A., Young, C.L., Stone, K.C., Dean, F.B., Janjic, N., Critchley, I.A. Antimicrob. Agents Chemother. (2005) [Pubmed]
  4. Biochemical and phylogenetic analyses of methionyl-tRNA synthetase isolated from a pathogenic microorganism, Mycobacterium tuberculosis. Kim, S., Jo, Y.J., Lee, S.H., Motegi, H., Shiba, K., Sassanfar, M., Martinis, S.A. FEBS Lett. (1998) [Pubmed]
  5. Proofreading in vivo: editing of homocysteine by methionyl-tRNA synthetase in the yeast Saccharomyces cerevisiae. Jakubowski, H. EMBO J. (1991) [Pubmed]
  6. Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids. Link, A.J., Vink, M.K., Agard, N.J., Prescher, J.A., Bertozzi, C.R., Tirrell, D.A. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  7. Proofreading and the evolution of a methyl donor function. Cyclization of methionine to S-methyl homocysteine thiolactone by Escherichia coli methionyl-tRNA synthetase. Jakubowski, H. J. Biol. Chem. (1993) [Pubmed]
  8. How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding. Serre, L., Verdon, G., Choinowski, T., Hervouet, N., Risler, J.L., Zelwer, C. J. Mol. Biol. (2001) [Pubmed]
  9. Mapping of the zinc binding domain of Escherichia coli methionyl-tRNA synthetase. Fourmy, D., Meinnel, T., Mechulam, Y., Blanquet, S. J. Mol. Biol. (1993) [Pubmed]
  10. Peptides at the tRNA binding site of the crystallizable monomeric form of E. coli methionyl-tRNA synthetase. Schulman, L.H., Pelka, H., Leon, O. Nucleic Acids Res. (1987) [Pubmed]
  11. Transcription and regulation of expression of the Escherichia coli methionyl-tRNA synthetase gene. Dardel, F., Panvert, M., Fayat, G. Mol. Gen. Genet. (1990) [Pubmed]
  12. Mapping of the active site of Escherichia coli methionyl-tRNA synthetase: identification of amino acid residues labeled by periodate-oxidized tRNA(fMet) molecules having modified lengths at the 3'-acceptor end. Hountondji, C., Schmitter, J.M., Beauvallet, C., Blanquet, S. Biochemistry (1990) [Pubmed]
  13. Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment. Barker, D.G., Ebel, J.P., Jakes, R., Bruton, C.J. Eur. J. Biochem. (1982) [Pubmed]
  14. Structural basis for anticodon recognition by methionyl-tRNA synthetase. Nakanishi, K., Ogiso, Y., Nakama, T., Fukai, S., Nureki, O. Nat. Struct. Mol. Biol. (2005) [Pubmed]
  15. Methionyl-tRNA synthetase induced 3'-terminal and delocalized conformational transition in tRNAfMet: steady-state fluorescence of tRNA with a single fluorophore. Ferguson, B.Q., Yang, D.C. Biochemistry (1986) [Pubmed]
  16. Methionyl-tRNA synthetase from E. coli--a review. Meinnel, T., Mechulam, Y., Dardel, F., Schmitter, J.M., Hountondji, C., Brunie, S., Dessen, P., Fayat, G., Blanquet, S. Biochimie (1990) [Pubmed]
  17. Genetic engineering of methionyl-tRNA synthetase: in vitro regeneration of an active synthetase by proteolytic cleavage of a methionyl-tRNA synthetase--beta-galactosidase chimeric protein. Hirel, P.H., Lévêque, F., Mellot, P., Dardel, F., Panvert, M., Mechulam, Y., Fayat, G. Biochimie (1988) [Pubmed]
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