Rabbit translation elongation factor 1 alpha stimulates the activity of homologous aminoacyl-tRNA synthetase

被引：28

作者：

Negrutskii, BS ^{[1
]}

Budkevich, TV ^{[1
]}

Shalak, VF ^{[1
]}

Turkovskaya, GV ^{[1
]}

ElSkaya, AV ^{[1
]}

机构：

[1] NATL ACAD SCI UKRAINE, INST MOLEC BIOL & GENET, KIEV 252143, UKRAINE

来源：

FEBS LETTERS | 1996年 / 382卷 / 1-2期

关键词：

aminoacyl-tRNA synthetase; elongation factor; protein-protein interaction; channeling; rabbit liver;

D O I：

10.1016/0014-5793(96)00128-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Functional and structural sequestration of aminoacyl-tRNA has been recently found in eukaryotic cells and the aminoacyl-tRNA channeling has been suggested [B.S. Negrutskii et al., Proc. Natl. Acad. Sci. 91 (1994) 964-968], but molecular details and mechanism of the process remained unclear. In this paper we have verified a possible interaction between rabbit aminoacyl-tRNA synthetase and homologous translation elongation factor Icl(EF-la), the proteins which may play a role of sequential components involved into the transfer of the aminoacyl-tRNA along the protein synthetic metabolic chain. The stimulation of the phenylalanyl-tRNA synthetase activity by EF-1 alpha is found. The effect is shown to be specific towards the origin of tRNA and elongation factor molecules. The data obtained favor the direct transfer mechanism of the aminoacyl-tRNA channeling process during eukaryotic protein synthesis.

引用

页码：18 / 20

页数：3

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