Pre-transfer Editing of Serine Hydroxamate within the Active Site of Methanogenic-type Seryl-tRNA Synthetase

Gruić-Sovulj, Ita and Dulić, Morana and Weygand-Đurašević, Ivana (2011) Pre-transfer Editing of Serine Hydroxamate within the Active Site of Methanogenic-type Seryl-tRNA Synthetase. Croatica Chemica Acta, 84 (2). pp. 179-184. ISSN 0011-1643

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Abstract

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.

Item Type: Article
Keywords: editing, proofreading, serine hydroxamate, seryl-tRNA synthetase
Date: 2011
Subjects: NATURAL SCIENCES > Chemistry
Divisions: Faculty of Science > Department of Chemistry
Publisher: Hrvatsko kemijsko društvo
Related URLs:
Depositing User: Branka Maravic
Date Deposited: 08 May 2014 16:17
Last Modified: 08 May 2014 16:17
URI: http://digre.pmf.unizg.hr/id/eprint/1072

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