The Escherichia coli trigger factor

被引：55

作者：

Hesterkamp, T ^{[1
]}

Bukau, B ^{[1
]}

机构：

[1] UNIV HEIDELBERG,ZENTRUM MOLEK BIOL,D-69120 HEIDELBERG,GERMANY

来源：

FEBS LETTERS | 1996年 / 389卷 / 01期

关键词：

ribosome; prolyl isomerase; chaperone; protein folding; translocation; proteolysis;

D O I：

10.1016/0014-5793(96)00582-0

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：

E. coli trigger factor is an abundant cytosolic protein originally identified by its ability to maintain the precursor of a secretory protein in a translocation competent form. Recent studies shed new light on the function of this protein. Trigger factor was found to be a peptidyl-prolyl-cis/trans-isomerase capable of catalysing protein folding in vitro, to associate with nascent cytosolic and secretory polypeptide chains, and to cooperate with the GroEL chaperone in promoting proteolysis of an unstable polypeptide in vivo. These findings suggest roles for trigger factor in various folding processes of secretory as well as cytosolic proteins.

引用

页码：32 / 34

页数：3

共 21 条

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