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. 1998 Jan 30;422(2):189-92. doi: 10.1016/s0014-5793(98)00007-6.


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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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


  • Anti-Bacterial Agents
  • Peptide Elongation Factors
  • Pyridones
  • Recombinant Proteins
  • elongation factor T
  • Guanosine Diphosphate
  • Histidine
  • Peptide Elongation Factor Tu
  • mocimycin
  • Glycine