Functional expansion of human tRNA synthetases achieved by structural inventions

被引：83

作者：

Guo, Min ^{[1
]}

Schimmel, Paul ^{[1
]}

Yang, Xiang-Lei ^{[1
]}

机构：

[1] Scripps Res Inst, Dept Mol Biol, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

来源：

FEBS LETTERS | 2010年 / 584卷 / 02期

基金：

美国国家卫生研究院;

关键词：

Aminoacyl-tRNA synthetase; Non-canonical function; Human; Structure; Multisynthetase complex; Disease; AMINOACYL-TRANSFER-RNA; ARGINYL-TRANSFER-RNA; ACTIVATING POLYPEPTIDE-II; PROTEIN-PROTEIN INTERACTIONS; METHIONYL-TRANSFER-RNA; N-TERMINAL EXTENSION; INTERACTING MULTIFUNCTIONAL PROTEIN; IMMUNODEFICIENCY-VIRUS TYPE-1; ELONGATION-FACTOR; 1-ALPHA; BINDING DOMAIN;

D O I：

10.1016/j.febslet.2009.11.064

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：

Known as an essential component of the translational apparatus, the aminoacyl-tRNA synthetase family catalyzes the first step reaction in protein synthesis, that is, to specifically attach each amino acid to its cognate tRNA. While preserving this essential role, tRNA synthetases developed other roles during evolution. Human tRNA synthetases, in particular, have diverse functions in different pathways involving angiogenesis, inflammation and apoptosis. The functional diversity is further illustrated in the association with various diseases through genetic mutations that do not affect aminoacylation or protein synthesis. Here we review the accumulated knowledge on how human tRNA synthetases used structural inventions to achieve functional expansions. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：434 / 442

页数：9

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