THE REACTION CYCLE OF GROEL AND GROES IN CHAPERONIN-ASSISTED PROTEIN-FOLDING

被引：260

作者：

MARTIN, J ^{[1
]}

MAYHEW, M ^{[1
]}

LANGER, T ^{[1
]}

HARTL, FU ^{[1
]}

机构：

[1] MEM SLOAN KETTERING CANC CTR, CELLULAR BIOCHEM & BIOPHYS PROGRAM, 1275 YORK AVE, NEW YORK, NY 10021 USA

来源：

NATURE | 1993年 / 366卷 / 6452期

关键词：

D O I：

10.1038/366228a0

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：

The reaction mechanism of protein folding by the chaperonin GroEL and its regulator GroES has been defined. GroES and substrate protein counteract each other's effects on GroEL: whereas GroES stabilizes GroEL in the ADP-bound state, binding of unfolded polypeptide within the cavity of the GroEL cylinder triggers ADP and GroES release. Upon ADP-ATP exchange, GroES reassociates with GroEL and ATP hydrolysis discharges the bound protein for folding. Partially folded protein rebinds to the chaperonin, thus perpetuating the cycle until folding is complete.

引用

页码：228 / 233

页数：6

共 31 条

[1]

BOCHKAREVA ES, 1992, J BIOL CHEM, V267, P6796

[2]

BOCHKAREVA ES, 1992, J BIOL CHEM, V267, P25672

[3] A POLYPEPTIDE BOUND BY THE CHAPERONIN GROEL IS LOCALIZED WITHIN A CENTRAL CAVITY [J].