PMID:9490003

Citation	Jonák, J, Anborgh, PH and Parmeggiani, A (1998) Interaction of EF-Tu with EF-Ts: substitution of His-118 in EF-Tu destabilizes the EF-Tu x EF-Ts complex but does not prevent EF-Ts from stimulating the release of EF-Tu-bound GDP. FEBS Lett. 422:189-92
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.
Links	PubMed
Keywords	Amino Acid Substitution; Anti-Bacterial Agents/metabolism; Binding Sites; Binding, Competitive; Chromatography, Ion Exchange; Cloning, Molecular; Drug Stability; Escherichia coli; Glycine; Guanosine Diphosphate/metabolism; Histidine; Kinetics; Peptide Elongation Factor Tu/chemistry; Peptide Elongation Factor Tu/metabolism; Peptide Elongation Factors/metabolism; Pyridones/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Thermodynamics
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