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
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.
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页码:10341 / 10344
页数:4
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