HIGH SELECTIVITY WITH LOW SPECIFICITY - HOW SECB HAS SOLVED THE PARADOX OF CHAPERONE BINDING

被引：120

作者：

RANDALL, LL ^{[1
]}

HARDY, SJS ^{[1
]}

机构：

[1] UNIV YORK,DEPT BIOL,YORK YO1 5DD,N YORKSHIRE,ENGLAND

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1995年 / 20卷 / 02期

关键词：

D O I：

10.1016/S0968-0004(00)88959-8

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：

Fundamental to the function of all molecular chaperones is their amazing ability to selectively and rapidly bind proteins in non-native states. Chaperones modulate a kinetic partitioning among the alternative pathways open to polypeptides within a cell, so that the proper pathway is taken. Here we review studies of SecB, a chaperone in Escherichia coli dedicated to facilitation of protein export, and emphasize the features that enable it to bind rapidly with high affinity and selectivity in the absence of consensus in sequence. The concepts discussed are likely to be generally applicable to chaperones.

引用

页码：65 / 70

页数：6

共 30 条

[1] INVITRO STUDIES ON THE FOLDING CHARACTERISTICS OF THE ESCHERICHIA-COLI PRECURSOR PROTEIN PREPHOE - EVIDENCE THAT SECB PREVENTS THE PRECURSOR FROM AGGREGATING BY FORMING A FUNCTIONAL COMPLEX [J].