tRNA synthetase: tRNA aminoacylation and beyond

被引：125

作者：

Pang, Yan Ling Joy ^{[1
]}

Poruri, Kiranmai ^{[1
]}

Martinis, Susan A. ^{[1
]}

机构：

[1] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

来源：

WILEY INTERDISCIPLINARY REVIEWS-RNA | 2014年 / 5卷 / 04期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

PROLYL-TRANSFER-RNA; MOSAIC-VIRUS RNA; I TRANSFER-RNA; INTERACTING MULTIFUNCTIONAL PROTEIN; RIBONUCLEIC-ACID SYNTHETASE; ACTIVATING POLYPEPTIDE-II; ESCHERICHIA-COLI; AMINO-ACID; CRYSTAL-STRUCTURE; PSEUDOMONIC ACID;

D O I：

10.1002/wrna.1224

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The aminoacyl-tRNA synthetases are prominently known for their classic function in the first step of protein synthesis, where they bear the responsibility of setting the genetic code. Each enzyme is exquisitely adapted to covalently link a single standard amino acid to its cognate set of tRNA isoacceptors. These ancient enzymes have evolved idiosyncratically to host alternate activities that go far beyond their aminoacylation role and impact a wide range of other metabolic pathways and cell signaling processes. The family of aminoacyl-tRNA synthetases has also been suggested as a remarkable scaffold to incorporate new domains that would drive evolution and the emergence of new organisms with more complex function. Because they are essential, the tRNA synthetases have served as pharmaceutical targets for drug and antibiotic development. The recent unfolding of novel important functions for this family of proteins offers new and promising pathways for therapeutic development to treat diverse human diseases. (C) 2014 John Wiley & Sons, Ltd.

引用

页码：461 / 480

页数：20

共 248 条

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