Document Detail

Structural analyses clarify the complex control of mistranslation by tRNA synthetases.
MedLine Citation:
PMID:  22155179     Owner:  NLM     Status:  MEDLINE    
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.
Min Guo; Paul Schimmel
Related Documents :
2119269 - Effects of polytherapy with phenytoin, carbamazepine, and stiripentol on formation of 4...
122539 - Treatment of postanoxic intention myoclonus with valproic acid.
24043219 - Uva irradiation of fatty acids and their oxidized products substantially increases thei...
23256819 - Hr-mas nmr spectroscopy of reconstructed human epidermis: potential for the in situ inv...
14572819 - Protease inhibitors in the treatment of hereditary angioedema.
15032379 - Effects of valproic acid on longitudinal bone growth.
1111389 - Bovine spastic paralysis: cerebrospinal fluid concentrations of homovanillic acid and 5...
1467999 - Genetically variable taste sensitivity to d-amino acids in mice.
15703599 - Gastric secretion.
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.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acyl-tRNA Synthetases / chemistry*,  metabolism
Protein Biosynthesis*
RNA, Transfer / chemistry*,  metabolism
Substrate Specificity
Grant Support
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
Reg. No./Substance:
0/Ligands; 9014-25-9/RNA, Transfer; EC 6.1.1.-/Amino Acyl-tRNA Synthetases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Structural basis of transcription by bacterial and eukaryotic RNA polymerases.
Next Document:  The two faces of Janus: functional interactions and protein aggregation.