Pre-transfer editing of serine hydroxamate within the active site of methanogenic-type seryl-tRNA synthetase
| Autor: | Ita Gruić-Sovulj, Ivana Weygand-Đurašević, Morana Dulic |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences biology Chemistry ved/biology Stereochemistry ved/biology.organism_classification_rank.species Active site Aminoacylation General Chemistry editing proofreading serine hydroxamate seryl-tRNA synthetase 010402 general chemistry 01 natural sciences 0104 chemical sciences Amino acid Serine 03 medical and health sciences Enzyme Biochemistry Transfer RNA biology.protein Protein biosynthesis Methanosarcina barkeri 030304 developmental biology |
| Zdroj: | Croatica Chemica Acta Volume 84 Issue 2 |
| ISSN: | 0011-1643 1334-417X |
| Popis: | 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) |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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