期刊
FEBS LETTERS
卷 581, 期 26, 页码 5110-5114出版社
WILEY
DOI: 10.1016/j.febslet.2007.09.058
关键词
pre-transfer editing; tRNA-independent; pre-transfer editing; kinetic proofreading; aminoacyl-adenylate hydrolysis; seryl-tRNA synthetase
Aminoacyl-tRNA synthetases, a group of enzymes catalyzing aminoacyl-tRNA formation, may possess inherent editing activity to clear mistakes arising through the selection of non-cognate amino acid. It is generally assumed that both editing substrates, non-cognate aminoacyl-adenylate and misacylated tRNA, are hydrolyzed at the same editing domain, distant from the active site. Here, we present the first example of an aminoacyl-tRNA synthetase (seryl-tRNA synthetase) that naturally lacks an editing domain, but possesses a hydrolytic activity toward non-cognate aminoacyl-adenylates. Our data reveal that tRNA-independent pre-transfer editing may proceed within the enzyme active site without shuttling the non-cognate aminoacyl-adenylate intermediate to the remote editing site. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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