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Gene Review

GUS1  -  glutamate--tRNA ligase GUS1

Saccharomyces cerevisiae S288c

Synonyms: (c)ERS, G0583, GluRS, Glutamate--tRNA ligase, cytoplasmic, Glutamyl-tRNA synthetase, ...
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High impact information on GUS1

  • We show here that association of Arc1p with MetRS and GluRS is required in vivo for effective recruitment of the corresponding cognate tRNAs within this complex [1].
  • 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 [1].
  • The GluRS apoenzyme fails to show significant kinetics of tRNA aminoacylation and charges unfractionated yeast tRNA at a level 10-fold reduced compared to Arc1p-bound GluRS [2].

Biological context of GUS1

  • Because Arc1p also interacts with yeast GluRS, restoration of cell growth could be due at least in part to its role of cofactor for that enzyme [3].
  • Two yeast enzymes that catalyze aminoacylation of tRNAs, MetRS and GluRS, form a complex with the protein Arc1p [1].
  • The structures reveal that all three domains adopt a glutathione S-transferase (GST)-like fold and that simultaneous interaction of Arc1p with GluRS and MetRS is mediated by the use of a novel interface in addition to a classical GST dimerization interaction [4].

Other interactions of GUS1

  • Complementation of yeast Arc1p by the p43 component of the human multisynthetase complex does not require its association with yeast MetRS and GluRS [3].
  • In this work, in order to localize free Arc1 we abolished complex assembly by deleting the appended domains from both MetRS and GluRS [5].


  1. A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases. Simos, G., Sauer, A., Fasiolo, F., Hurt, E.C. Mol. Cell (1998) [Pubmed]
  2. Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity. Graindorge, J.S., Senger, B., Tritch, D., Simos, G., Fasiolo, F. Biochemistry (2005) [Pubmed]
  3. 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]
  4. Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes. Simader, H., Hothorn, M., Köhler, C., Basquin, J., Simos, G., Suck, D. Nucleic Acids Res. (2006) [Pubmed]
  5. The tRNA aminoacylation co-factor Arc1p is excluded from the nucleus by an Xpo1p-dependent mechanism. Galani, K., Hurt, E., Simos, G. FEBS Lett. (2005) [Pubmed]
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