The thermosome: archetype of group II chaperonins

被引：51

作者：

Klumpp, M ^{[1
]}

Baumeister, W ^{[1
]}

机构：

[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany

来源：

FEBS LETTERS | 1998年 / 430卷 / 1-2期

关键词：

protein folding; chaperone; TRiC/CCT; archaeon;

D O I：

10.1016/S0014-5793(98)00541-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryotes, known as TRiC or CCT, form a distinct subfamily of the chaperonins that does not depend on a co-chaperonin for protein folding activity. Recent structural data obtained by cryo- electron microscopy and X-ray crystallography provide the first insights into a novel mechanism remarkably different from that of the bacterial GroEL-GroES system. (C) 1998 Federation of European Biochemical Societies.

引用

页码：73 / 77

页数：5

共 49 条

[11]

GOFFEAU A, 1997, NATURE S, V387

[12]

GUAGLIARDI A, 1995, J BIOL CHEM, V270, P28126

[13] THE CHAPERONIN FROM THE ARCHAEON SULFOLOBUS-SOLFATARICUS PROMOTES CORRECT REFOLDING AND PREVENTS THERMAL-DENATURATION IN-VITRO [J].