Chaperone function of Hsp90-associated proteins

被引：313

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

[1] PEPTIDYL-PROLYL CIS-TRANS-ISOMERASE ACTIVITY ASSOCIATED WITH THE LUMEN OF THE ENDOPLASMIC-RETICULUM [J].

BOSE, S ;

FREEDMAN, RB .

BIOCHEMICAL JOURNAL, 1994, 300 :865-870

[2]

BOSE S, UNPUB

[3] Supervising the fold: Functional principles of molecular chaperones [J].

Buchner, J .

FASEB JOURNAL, 1996, 10 (01) :10-19

[4] AN IMMUNOPHILIN THAT BINDS M(R) 90,000 HEAT-SHOCK PROTEIN - MAIN STRUCTURAL FEATURES OF A MAMMALIAN P59 PROTEIN [J].

CALLEBAUT, I ;

RENOIR, JM ;

LEBEAU, MC ;

MASSOL, N ;

BURNY, A ;

BAULIEU, EE ;

MORNON, JP .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (14) :6270-6274

[5]

CHANG HCJ, 1994, J BIOL CHEM, V269, P24983

[6]

EHRNSPERGER M, IN PRESS EMBO J

[7] PEPTIDYL-PROLYL CIS/TRANS ISOMERASES AND THEIR EFFECTORS [J].

FISCHER, G .

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 1994, 33 (14) :1415-1436

[8] Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23 [J].

Freeman, BC ;

Toft, DO ;

Morimoto, RI .

SCIENCE, 1996, 274 (5293) :1718-1720

[9] The human cytosolic molecular chaperones hsp90, Hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding [J].

Freeman, BC ;

Morimoto, RI .

EMBO JOURNAL, 1996, 15 (12) :2969-2979

[10] PROTEIN FOLDING IN THE CELL [J].

GETHING, MJ ;

SAMBROOK, J .

NATURE, 1992, 355 (6355) :33-45

← 1 2 3 →