COOPERATION OF GROEL/GROES AND DNAK/DNAJ HEAT-SHOCK PROTEINS IN PREVENTING PROTEIN MISFOLDING IN ESCHERICHIA-COLI

被引：196

作者：

GRAGEROV, A ^{[1
]}

NUDLER, E ^{[1
]}

KOMISSAROVA, N ^{[1
]}

GAITANARIS, GA ^{[1
]}

GOTTESMAN, ME ^{[1
]}

NIKIFOROV, V ^{[1
]}

机构：

[1] COLUMBIA UNIV COLL PHYS & SURG,INST CANC RES,NEW YORK,NY 10032

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1992年 / 89卷 / 21期

关键词：

PROTEIN AGGREGATION; PROTEIN FOLDING; CHAPERONES; RPOH MUTANTS;

D O I：

10.1073/pnas.89.21.10341

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Newly synthesized proteins aggregate extensively in Escherichia coli rpoH mutants, which are deficient in the heat shock proteins (hsp). Overproduction of either GroEL and GroES or DnaK and DnaJ prevents aggregation. If expressed together, the four hsp are effective at physiological concentrations. Our data suggest that the GroEL and GroES proteins and the DnaK and Dnaj proteins have complementary functions in the folding and assembly of most proteins.

引用

页码：10341 / 10344

页数：4

共 29 条

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