HISTIDINE-118 OF ELONGATION-FACTOR TU - ITS ROLE IN AMINOACYL-TRANSFER-RNA BINDING AND REGULATION OF THE GTPASE ACTIVITY

被引：18

作者：

JONAK, J ^{[1
]}

ANBORGH, PH ^{[1
]}

PARMEGGIANI, A ^{[1
]}

机构：

[1] ECOLE POLYTECH,BIOCHIM LAB,F-91128 PALAISEAU,FRANCE

来源：

FEBS LETTERS | 1994年 / 343卷 / 01期

关键词：

ELONGATION FACTOR TU; HISTIDINE; 118; AMINOACYL-TRANSFER-RNA; GTPASE ACTIVITY; ESCHERICHIA COLI;

D O I：

10.1016/0014-5793(94)80614-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The function of His(118) 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 His(118) 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.

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页码：94 / 98

页数：5

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