FEBS Letters | |
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 | |
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
【 预 览 】
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