Abstract
Elongation factor Tu from Escherichia coli with His-118 substituted by glycine (EF-TuH118G) was found to be defective in complex formation with EF-Ts. EF-Ts in excess failed to dissociate kirromycin from the EF-TuH118G x kirromycin complex and to form a stable complex with EF-TuH118G on column chromatography. However, the stimulatory effect of EF-Ts on GDP dissociation from EF-TuH118G x GDP and on poly(U)-directed poly(Phe) synthesis catalyzed by EF-TuH118G was only partially influenced. These results indicate that His-118, while very important for the formation of a stable EF-Tu-EF-Ts complex, is not essential for the transmission of the EF-Ts-dependent signal accelerating the release of the EF-Tu-bound GDP.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Substitution
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Anti-Bacterial Agents / metabolism
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Binding Sites
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Binding, Competitive
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Chromatography, Ion Exchange
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Cloning, Molecular
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Drug Stability
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Escherichia coli
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Glycine
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Guanosine Diphosphate / metabolism*
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Histidine
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Kinetics
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Peptide Elongation Factor Tu / chemistry
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Peptide Elongation Factor Tu / metabolism*
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Peptide Elongation Factors / metabolism*
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Pyridones / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Thermodynamics
Substances
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Anti-Bacterial Agents
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Peptide Elongation Factors
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Pyridones
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Recombinant Proteins
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elongation factor T
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Guanosine Diphosphate
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Histidine
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Peptide Elongation Factor Tu
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mocimycin
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Glycine