Document Detail

Mutational isolation of a sieve for editing in a transfer RNA synthetase.
MedLine Citation:
PMID:  8146659     Owner:  NLM     Status:  MEDLINE    
Editing reactions are essential for the high fidelity of information transfer in processes such as replication, RNA splicing, and protein synthesis. The accuracy of interpretation of the genetic code is enhanced by the editing reactions of aminoacyl transfer RNA (tRNA) synthetases, whereby amino acids are prevented from being attached to the wrong tRNAs. Amino acid discrimination is achieved through sieves that may overlap with or coincide with the amino acid binding site. With the class I Escherichia coli isoleucine tRNA synthetase, which activates isoleucine and occasionally misactivates valine, as an example, a rationally chosen mutant enzyme was constructed that lacks entirely its normal strong ability to distinguish valine from isoleucine by the initial amino acid recognition sieve. The misactivated valine, however, is still eliminated by hydrolytic editing reactions. These data suggest that there is a distinct sieve for editing that is functionally independent of the amino acid binding site.
E Schmidt; P Schimmel
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Science (New York, N.Y.)     Volume:  264     ISSN:  0036-8075     ISO Abbreviation:  Science     Publication Date:  1994 Apr 
Date Detail:
Created Date:  1994-05-03     Completed Date:  1994-05-03     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0404511     Medline TA:  Science     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  265-7     Citation Subset:  IM    
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
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MeSH Terms
Adenosine Triphosphate / metabolism
Binding Sites
Escherichia coli / enzymology
Isoleucine / metabolism*
Isoleucine-tRNA Ligase / chemistry,  genetics,  metabolism*
Protein Structure, Secondary
RNA Editing*
RNA, Transfer, Ile / metabolism
Valine / metabolism*
Grant Support
Reg. No./Substance:
0/RNA, Transfer, Ile; 56-65-5/Adenosine Triphosphate; 7004-03-7/Valine; 73-32-5/Isoleucine; EC Ligase

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

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