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Papers In Press, published online ahead of print November 7, 2000
J. Biol. Chem, 10.1074/jbc.M008682200
Submitted on September 22, 2000
Revised on November 7, 2000
Accepted on November 7, 2000

Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs

Karina Deinert, Franco Fasiolo, Eduard C. Hurt, and George Simos

Biochemie-Zentrum Heidelberg (BZH), Heidelberg D-69120

Corresponding Author: cg2{at}ix.urz.uni-heidelberg.de

Eukaryotic aminoacyl-tRNA synthetases, in contrast to their prokaryotic counterparts, are often part of high molecular weight complexes. In yeast, two enzymes, the methionyl- and glutamyl-tRNA synthetases (MetRS and GluRS, respectively) associate in vivo with the tRNA binding protein Arc1p. To study the assembly and function of this complex, we have reconstituted it in vitro from individually purified recombinant proteins. Our results show that Arc1p can readily bind to either or both of the two enzymes, mediating the formation of the respective binary or ternary complexes. Under competition conditions, Arc1p alone exhibits broad specificity and interacts with a defined set of tRNA species. Nevertheless, the in vitro reconstituted Arc1p-containing enzyme complexes can bind only to their cognate tRNAs and tighter than the corresponding monomeric enzymes. These results demonstrate that the organization of aminoacyl-tRNA synthetases together with general tRNA-binding proteins into multimeric complexes can stimulate their catalytic efficiency and, therefore, offer a significant advantage to the eukaryotic cell.


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