%0 Journal Article
%T Pre-transfer Editing of Serine Hydroxamate within the Active Site of Methanogenic-type Seryl-tRNA Synthetase
%A Duli£¿
%A Morana
%A Grui£¿-Sovulj
%A Ita
%A Weygand-£¿ura£¿evi£¿
%A Ivana
%J -
%D 2011
%R 10.5562/cca1823
%X Sa£¿etak Aminoacyl-tRNA synthetases (aaRSs) maintain fidelity of protein synthesis by matching only cognate amino acid-tRNA pairs. Aminoacylation occurs through activation of amino acid to yield aminoacyl- adenylate followed by transfer of acyl-moiety to tRNA. Error-prone aaRSs achieve high level of accuracy using inherent hydrolytic activities towards noncognate aminoacyl-adenylate or misacylated tRNA (pre- and post-transfer editing). Seryl-tRNA synthetases can be divided into two structurally different types: canonical and methanogenic- type. Both types have been shown to efficiently activate serine analogue serine hydroxamate (SerHX). Moreover, this analogue has been also eliminated by pre-transfer editing within the canonical synthetic site of yeast SerRS. Here we show that methanogenic-type SerRS from Methanosarcina barkeri clears misactivated SerHX similarly as the yeast enzyme: SerHX-adenylate is not expelled into solution, but is enzymatically hydrolyzed in a tRNA-independent manner. Since the enzyme lacks domain specialized in editing, this shows that methanogenic-type catalytic core is also capable to perform pre-transfer editing. (doi: 10.5562/cca1823
%K editing
%K proofreading
%K serine hydroxamate
%K seryl-tRNA synthetase
%U https://hrcak.srce.hr/index.php?show=clanak&id_clanak_jezik=107215