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Gene Review

MES1  -  methionine--tRNA ligase MES1

Saccharomyces cerevisiae S288c

Synonyms: MetRS, Methionine--tRNA ligase, cytoplasmic, Methionyl-tRNA synthetase, YGR264C
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Disease relevance of MES1


High impact information on MES1

  • Arc1p is linked to MetRS and GluRS through its amino-terminal domain, while its middle and carboxy-terminal parts comprise a novel tRNA-binding domain [2].
  • However, when their assembly into a complex is inhibited, significant amounts of MetRS, GluRS and Arc1p can enter the nucleus [3].
  • Thus, Cca1p and Mes1p seem to function in a Los1p-independent tRNA nuclear export pathway [4].
  • The mutation was cloned on a multicopy plasmid by gap repair of a plasmid bearing the wild type MES1 gene for a fragment corresponding to the mes 1 mutation [5].
  • The major MES1 transcript is not affected by the general control or starvation for several different amino acids, including methionine [6].

Chemical compound and disease context of MES1

  • As for Escherichia coli methionine tRNAs, the anticodon triplet of yeast tRNA(Met) plays an important role in the recognition by the yeast methionyl-tRNA synthetase (MetRS), indicating that this determinant for methionine identity is conserved in yeast [1].

Biological context of MES1


Physical interactions of MES1

  • Complementation of yeast Arc1p by the p43 component of the human multisynthetase complex does not require its association with yeast MetRS and GluRS [8].

Other interactions of MES1

  • Arc1p is associated with two proteins which were identified as methionyl-tRNA and glutamyl-tRNA synthetase (MetRS and GluRS) by a new mass spectrometry method [10].

Analytical, diagnostic and therapeutic context of MES1

  • Dissection of the yeast cytoplasmic initiator tRNA(Met) into two helical domains, the T psi C acceptor and anticodon minihelices, failed to show anminoacylation and binding of the acceptor minihelix by the yeast methionyl-tRNA synthetase (MetRS) even in the presence of the anticodon minihelix [11].
  • Using serum albumin as an inhibitor of adhesion of L5 to the microconcentrators which was used to concentrate the final product, a distinct L5 band was detected on SDS-PAGE, the intensity of which was comparable to that of the MetRS band [12].
  • The dissociated MetRS complex fraction was purified by gel filtration followed by tRNA-Sepharose chromatography using partially purified tRNA(met) in Method I, and by hydrophobic interaction chromatography in Method II [12].


  1. Binding of the yeast tRNA(Met) anticodon by the cognate methionyl-tRNA synthetase involves at least two independent peptide regions. Despons, L., Senger, B., Fasiolo, F., Walter, P. J. Mol. Biol. (1992) [Pubmed]
  2. A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases. Simos, G., Sauer, A., Fasiolo, F., Hurt, E.C. Mol. Cell (1998) [Pubmed]
  3. The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p. Galani, K., Grosshans, H., Deinert, K., Hurt, E.C., Simos, G. EMBO J. (2001) [Pubmed]
  4. A Los1p-independent pathway for nuclear export of intronless tRNAs in Saccharomycescerevisiae. Feng, W., Hopper, A.K. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  5. Cloning and characterization of the yeast methionyl-tRNA synthetase mutation mes1. Chatton, B., Winsor, B., Boulanger, Y., Fasiolo, F. J. Biol. Chem. (1987) [Pubmed]
  6. Structure and expression of two aminoacyl-tRNA synthetase genes from Saccharomyces cerevisiae. Meussdoerffer, F., Fink, G.R. J. Biol. Chem. (1983) [Pubmed]
  7. Analysis of an 11.6 kb region from the right arm of chromosome VII of Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals the presence of three new genes. Clemente, M.L., Sartori, G., Cardazzo, B., Carignani, G. Yeast (1997) [Pubmed]
  8. Complementation of yeast Arc1p by the p43 component of the human multisynthetase complex does not require its association with yeast MetRS and GluRS. Golinelli-Cohen, M.P., Zakrzewska, A., Mirande, M. J. Mol. Biol. (2004) [Pubmed]
  9. Importance of structural features for tRNA(Met) identity. Aphasizhev, R., Senger, B., Fasiolo, F. RNA (1997) [Pubmed]
  10. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases. Simos, G., Segref, A., Fasiolo, F., Hellmuth, K., Shevchenko, A., Mann, M., Hurt, E.C. EMBO J. (1996) [Pubmed]
  11. The presence of a D-stem but not a T-stem is essential for triggering aminoacylation upon anticodon binding in yeast methionine tRNA. Senger, B., Aphasizhev, R., Walter, P., Fasiolo, F. J. Mol. Biol. (1995) [Pubmed]
  12. Further study on association of 5SrRNA-L5 protein complex and methionyl-tRNA to methionyl-tRNA synthetase in the macromolecular aminoacyl-tRNA synthetase complex. Ogata, K., Ohno, R., Morioka, S., Terao, K. J. Biochem. (1996) [Pubmed]
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