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Interaction of EF-Tu with EF-Ts: substitution of His-118 in EF-Tu destabilizes the EF-Tu·EF-Ts complex but does not prevent EF-Ts from stimulating the release of EF-Tu-bound GDP

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
422
Issue
2
Identifiers
DOI: 10.1016/s0014-5793(98)00007-6
Keywords
  • Elongation Factor Tu
  • Elongation Factor Tu Histidine 118
  • Elongation Factor Ts
  • Elongation Factor Tu·Elongation Factor Ts Interaction
  • Escherichia Coli

Abstract

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·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·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.

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