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

FEBS Letters

Anborgh, Pieter H²  Jonák, Jiřı́¹  Parmeggiani, Andrea² 

[1] Laboratory of Protein Biosynthesis, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Flemingovo n. 2, 166 37 Prague 6, Czech Republic;Groupe de Biophysique - Equipe 2, Ecole Polytechnique, 91128 Palaiseau Cedex, France

关键词: Elongation factor Tu;    Elongation factor Tu histidine 118;    Elongation factor Ts;    Elongation factor Tu·elongation factor Ts interaction;    Escherichia coli;    EF-Tu;    elongation factor Tu;    EF-Ts;    elongation factor Ts;    aa-tRNA;    aminoacyl-tRNA;    uH118;    EF-TuHis-118;    sF81;    EF-TsPhe-81;    uH84;    EF-TuHis-84;    sD80;    EF-TsAsp-80;    wt;    wild type;    EF-TuH118G;    EF-Tu whose His-118 was substituted by glycine;   

DOI  :  10.1016/S0014-5793(98)00007-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown