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Group II chaperonins: new TRiC(k)s and turns of a protein folding machine.

Abstract：

:In the past decade, the eubacterial group I chaperonin GroEL became the paradigm of a protein folding machine. More recently, electron microscopy and X-ray crystallography offered insights into the structure of the thermosome, the archetype of the group II chaperonins which also comprise the chaperonin from the eukaryotic cytosol TRiC. Some structural differences from GroEL were revealed, namely the existence of a built-in lid provided by the helical protrusions of the apical domains instead of a GroES-like co-chaperonin. These structural studies provide a framework for understanding the differences in the mode of action between the group II and the group I chaperonins. In vitro analyses of the folding of non-native substrates coupled to ATP binding and hydrolysis are progressing towards establishing a functional cycle for group II chaperonins. A protein complex called GimC/prefoldin has recently been found to cooperate with TRiC in vivo, and its characterization is under way.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Gutsche I,Essen LO,Baumeister W

doi

10.1006/jmbi.1999.3008

keywords:

subject

Has Abstract

pub_date

1999-10-22 00:00:00

pages

295-312

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(99)93008-5

journal_volume

293

pub_type

杂志文章,评审

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