Document Detail


tRNA-independent pretransfer editing by class I leucyl-tRNA synthetase.
MedLine Citation:
PMID:  19068478     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Aminoacyl-tRNA synthetases catalyze the formation of aminoacyl-tRNA in a two-step reaction starting with amino acid activation followed by aminoacyl group transfer to tRNA. To clear mistakes that occasionally occur, some of these enzymes carry out editing activities, acting on the misactivated amino acid (pretransfer editing) or after the transfer on the tRNA (post-transfer editing). The post-transfer editing pathway of leucyl-tRNA synthetase has been extensively studied by structural and biochemical approaches. Here, we report the finding of a tRNA-independent pretransfer editing pathway in leucyl-tRNA synthetases from Aquifex aeolicus. Using a CP1-mutant defective in its post-transfer editing function, we showed that this new editing pathway is distinct from the post-transfer editing site and may occur at the synthetic catalytic site, as recently proposed for other aminoacyl-tRNA synthetases.
Authors:
Bin Zhu; Peng Yao; Min Tan; Gilbert Eriani; En-Duo Wang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-12-09
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  284     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2009 Feb 
Date Detail:
Created Date:  2009-02-02     Completed Date:  2009-04-06     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3418-24     Citation Subset:  IM    
Affiliation:
State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Graduate School of the Chinese Academy of Sciences, Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China.
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MeSH Terms
Descriptor/Qualifier:
Bacteria / enzymology*,  genetics
Bacterial Proteins / genetics,  metabolism*
Catalytic Domain / physiology
Leucine-tRNA Ligase / genetics,  metabolism*
RNA Editing / physiology*
RNA, Bacterial / genetics,  metabolism*
RNA, Transfer / genetics,  metabolism*
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/RNA, Bacterial; 9014-25-9/RNA, Transfer; EC 6.1.1.4/Leucine-tRNA Ligase

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