CHAPERONIN-MEDIATED PROTEIN FOLDING AT THE SURFACE OF GROEL THROUGH A MOLTEN GLOBULE-LIKE INTERMEDIATE

被引：800

作者：

MARTIN, J

LANGER, T

BOTEVA, R

SCHRAMEL, A

HORWICH, AL

HARTL, FU

机构：

[1] UNIV MUNICH,INST PHYSIOL CHEM,GOETHESTR 33,W-8000 MUNICH 2,GERMANY

[2] YALE UNIV,SCH MED,HOWARD HUGHES MED INST,NEW HAVEN,CT 06510

[3] YALE UNIV,SCH MED,DEPT HUMAN GENET,NEW HAVEN,CT 06510

[4] UNIV MUNICH,INST ZOOL,W-8000 MUNICH 2,GERMANY

来源：

NATURE | 1991年 / 352卷 / 6330期

关键词：

RIBULOSE BISPHOSPHATE CARBOXYLASE; LIVER DIHYDROFOLATE-REDUCTASE; HEAT-SHOCK PROTEINS; ESCHERICHIA-COLI; PRECURSOR PROTEINS; RIBULOSEBISPHOSPHATE-CARBOXYLASE; ATP HYDROLYSIS; RHODANESE; HSP60; MITOCHONDRIA;

D O I：

10.1038/352036a0

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：

Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro. The groEL protein stabilizes the polypeptides in a conformation resembling the 'molten globule' state. Mg-ATP and groES then promote the acquisition of ordered tertiary structure at the surface of groEL. Folding requires the hydrolysis of about 100 ATP molecules per protein monomer. This active process of surface-mediated chain folding might represent a general mechanism for the formation of protein structure in vivo.

引用

页码：36 / 42

页数：7

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