Processivity of translation in the eukaryote cell: Role of aminoacyl-tRNA synthetases

被引:37
作者
Mirande, Marc [1 ]
机构
[1] CNRS, Lab Enzymol & Biochim Struct, F-91190 Gif Sur Yvette, France
关键词
Aminoacyl-tRNA synthetase; tRNA-binding domain; Translation; Eukaryote; Processivity; N-TERMINAL EXTENSION; STRUCTURAL BASIS; BINDING DOMAIN; PROTEIN-SYNTHESIS; CRYSTAL-STRUCTURE; COMPLEX; MITOCHONDRIAL; ORGANIZATION; LOCALIZATION; ASSOCIATION;
D O I
10.1016/j.febslet.2009.11.027
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
Several lines of evidence led to the conclusion that mammalian ribosomal protein synthesis is a highly organized biological process in vivo. A wealth of data support the concept according to which tRNA aminoacylation, formation of the ternary complex on EF1A and delivery of aminoacyl-tRNA to the ribosome is a processive mechanism where tRNA is vectorially transferred from one component to another. Polypeptide extensions, referred to as tRBDs (tRNA binding domains), are appended to mammalian and yeast aminoacyl-tRNA synthetases. The involvement of these domains in the capture of deacylated tRNA and in the sequestration of aminoacylated tRNA, suggests that cycling of tRNA in translation is mediated by the processivity of the consecutive steps. The possible origin of the tRBDs is discussed. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:443 / 447
页数:5
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