Document Detail

Novel mutants of elongation factor G.
MedLine Citation:
PMID:  2231719     Owner:  NLM     Status:  MEDLINE    
A novel mutant form of elongation factor G (EF-G) in Escherichia coli is described. This variant EF-G restricts reading frame errors by a factor of 2 to 3 in vivo at two different positions in a lacIZ fusion. In addition, a conventional fusidic acid resistant (fusR) mutant of EF-G was compared with the restrictive mutant. Both mutants were characterized in vitro in a steady-state poly(U) translating system. The data indicate that the restrictive EF-G variant has an altered interaction with the ribosome both in vivo and in vitro. In contrast, the conventional fusR variant is altered in its interaction with GTP, which is evident in vitro.
A A Richter Dahlfors; C G Kurland
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of molecular biology     Volume:  215     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  1990 Oct 
Date Detail:
Created Date:  1990-12-07     Completed Date:  1990-12-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  549-57     Citation Subset:  IM    
Department of Molecular Biology, Biomedical Center, Uppsala, Sweden.
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MeSH Terms
Drug Resistance, Microbial / genetics
Escherichia coli / drug effects,  genetics*
Fusidic Acid / pharmacology
Guanosine Triphosphate / metabolism*
Lac Operon*
Peptide Elongation Factor G
Peptide Elongation Factors / genetics*
Protein Biosynthesis
RNA, Messenger / biosynthesis*
Ribosomes / drug effects,  metabolism*
Reg. No./Substance:
0/Peptide Elongation Factor G; 0/Peptide Elongation Factors; 0/RNA, Messenger; 6990-06-3/Fusidic Acid; 86-01-1/Guanosine Triphosphate

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

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