Chaperone function of Hsp90-associated proteins

被引：311

作者：

Bose, S ^{[1
]}

Weikl, T ^{[1
]}

Bugl, H ^{[1
]}

Buchner, J ^{[1
]}

机构：

[1] UNIV REGENSBURG, INST BIOPHYS & PHYS BIOCHEM, D-93040 REGENSBURG, GERMANY

来源：

SCIENCE | 1996年 / 274卷 / 5293期

关键词：

D O I：

10.1126/science.274.5293.1715

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 Hsp90 heat shock protein of eukaryotic cells regulates the activity of proteins involved in signal transduction pathways and may direct intracellular protein folding in general. Hsp90 performs at least part of its function in a complex with a specific set of partner proteins that include members of the prolyl isomerase family. The properties of the major components of the Hsp90 complex were examined through the use of in vitro protein folding assays. Two of the components, FKBP52 and p23, functioned as mechanistically distinct molecular chaperones. These results suggest the existence of a super-chaperone complex in the cytosol of eukaryotic cells.

引用

页码：1715 / 1717

页数：3

共 28 条

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