PROTEIN FOLDING IN THE CELL - FUNCTIONS OF 2 FAMILIES OF MOLECULAR CHAPERONE, HSP 60 AND TF55-TCP1

被引：106
作者：
HORWICH, AL
WILLISON, KR
机构：
[1] CHESTER BEATTY LABS, INST CANC RES, LONDON SW3 6JB, ENGLAND
[2] YALE UNIV, SCH MED, HOWARD HUGHES MED INST, NEW HAVEN, CT 06510 USA
来源：
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES | 1993年 / 339卷 / 1289期
关键词：
D O I：
10.1098/rstb.1993.0030
中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Two families of molecular chaperone, the hsp 60-GroEL family and the TF55-TCP1 family, have been discovered in evolutionarily related cellular compartments. A member of one of these families, hsp 60, has been shown to play a global role in polypeptide chain folding in mitochondria. We review here studies of both hsp 60 and other family members, discussing their essential physiological roles and mechanism of action.
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页码：313 / 326
页数：14
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