Histidine‐118 of elongation factor Tu: its role in aminoacyl‐tRNA binding and regulation of the GTPase activity

FEBS Letters

Jonák, Jiři¹  Parmeggiani, Andrea²  Anborgh, Pieter H.² 

[1] Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Flemingovo n. 2, 16637 Prague 6, Czech Republic;Laboratoire de Biochimie, Ecole Polytechnique, 91128 Palaiseau Cedex, France

关键词: Elongation factor Tu;    Histidine 118;    Aminoacyl-tRNA;    GTPase activity;    Escherichia coli;   

DOI  :  10.1016/0014-5793(94)80614-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The function of His¹¹⁸ in elongation factor (EF)-Tu from Escherichia coli was investigated by its substitution with glycine. The substitution had a differential effect on individual functions of the protein. The affinity for aminoacyl (aa)-tRNA and the intrinsic GTPase activity of the mutant EF-Tu were decreased whereas the response of its GTPase center to aa-tRNA was strongly increased. These results suggest that the region around His¹¹⁸ is involved in the binding of aa-tRNA and in the transmission of a turn-off signal generated by the interaction with aa-tRNA and directed to the GTPase center of EF-Tu.

【 授权许可】

Unknown