Document Detail


Structural analyses clarify the complex control of mistranslation by tRNA synthetases.
MedLine Citation:
PMID:  22155179     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Proteins are precisely assembled with amino acids by matching the anticodons of charged transfer RNAs to nucleotide triplets in mRNA sequences. Accurate translation depends on the specific coupling of cognate amino acids and tRNAs - a step carried out by aminoacyl-tRNA synthetases (aaRSs) and that generates the genetic code. Owing to their intrinsic similarity, aaRSs developed highly differentiated structures to discriminate between amino acids at the active site for aminoacylation. Because this discrimination is not sufficient to prevent toxic mistranslation, aaRSs developed separate structures to further refine recognition by proofreading. From comprehensive structural studies on aaRSs, many of the molecular details have been elucidated for the recognition of cognate amino acids and for the misactivation and editing of noncognate amino acids, Here we review recent advances in the structural description of the binding, activation and editing of amino acids, which collectively reveal many aspects of the fine-tuned systems that resulted in a robust and universal genetic code.
Authors:
Min Guo; Paul Schimmel
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review     Date:  2011-12-10
Journal Detail:
Title:  Current opinion in structural biology     Volume:  22     ISSN:  1879-033X     ISO Abbreviation:  Curr. Opin. Struct. Biol.     Publication Date:  2012 Feb 
Date Detail:
Created Date:  2012-02-20     Completed Date:  2012-05-17     Revised Date:  2014-09-15    
Medline Journal Info:
Nlm Unique ID:  9107784     Medline TA:  Curr Opin Struct Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  119-26     Citation Subset:  IM    
Copyright Information:
Copyright © 2011 Elsevier Ltd. All rights reserved.
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MeSH Terms
Descriptor/Qualifier:
Amino Acyl-tRNA Synthetases / chemistry*,  metabolism
Aminoacylation
Animals
Humans
Ligands
Protein Biosynthesis*
RNA, Transfer / chemistry*,  metabolism
Substrate Specificity
Grant Support
ID/Acronym/Agency:
23562//PHS HHS; GM 15539/GM/NIGMS NIH HHS; R01 GM015539/GM/NIGMS NIH HHS; R01 GM015539-44/GM/NIGMS NIH HHS; R01 GM015539-44S1/GM/NIGMS NIH HHS; R01 GM023562/GM/NIGMS NIH HHS; R01 GM023562-37/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Ligands; 9014-25-9/RNA, Transfer; EC 6.1.1.-/Amino Acyl-tRNA Synthetases
Comments/Corrections

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