RENATURATION OF DENATURED-LAMBDA REPRESSOR REQUIRES HEAT-SHOCK PROTEINS

被引：126

作者：

GAITANARIS, GA

PAPAVASSILIOU, AG

RUBOCK, P

SILVERSTEIN, SJ

GOTTESMAN, ME

机构：

[1] COLUMBIA UNIV COLL PHYS & SURG,INTEGRATED PROGRAM CELLULAR MOLEC & BIOPHYS STUDIES,NEW YORK,NY 10032

[2] COLUMBIA UNIV COLL PHYS & SURG,DEPT MICROBIOL,NEW YORK,NY 10032

[3] COLUMBIA UNIV COLL PHYS & SURG,DEPT BIOCHEM & MOLEC BIOPHYS,NEW YORK,NY 10032

来源：

CELL | 1990年 / 61卷 / 06期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0092-8674(90)90066-N

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 temperature-sensitive bacteriophage λc1857 repressor protein rapidly renatures after thermal inactivation. E. coli mutants in the heat shock protein genes dnaK, dnaJ, and grpE do not efficiently reactivate heat-denatured repressor. Our results suggest that protein refolding is promoted by heat shock proteins and that such a process is the basis of the homeostatic role played by these proteins in the heat shock response. © 1990.

引用

收藏

页码：1013 / 1020

页数：8

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