RABBIT TRANSLATION ELONGATION-FACTOR 1-ALPHA STIMULATES THE ACTIVITY OF HOMOLOGOUS AMINOACYL-TRANSFER-RNA SYNTHETASE

Functional and structural sequestration of aminoacyl-tRNA has been rec ently found in eukaryotic cells and the aminoacyl-tRNA channeling has been suggested [B.S. Negrutskii et al., Proc. Natl. Acad. Sci. 91 (199 4) 964-968], but molecular details and mechanism of the process remain ed unclear. In this paper we have verified a possible interaction betw een rabbit aminoacyl-tRNA synthetase and homologous translation elonga tion factor Icl(EF-la), the proteins which may play a role of sequenti al components involved into the transfer of the aminoacyl-tRNA along t he protein synthetic metabolic chain. The stimulation of the phenylala nyl-tRNA synthetase activity by EF-1 alpha is found. The effect is sho wn to be specific towards the origin of tRNA and elongation factor mol ecules. The data obtained favor the direct transfer mechanism of the a minoacyl-tRNA channeling process during eukaryotic protein synthesis.