Protein folding: Versatility of the cytosolic chaperonin TRIC/CCT

Authors
Leroux, MR Hartl, FU
Citation
Mr. Leroux et Fu. Hartl, Protein folding: Versatility of the cytosolic chaperonin TRIC/CCT, CURR BIOL, 10(7), 2000, pp. R260-R264
Citations number
22
Categorie Soggetti
Experimental Biology
Journal title
CURRENT BIOLOGY
ISSN journal
09609822 → ACNP
Volume
10
Issue
7
Year of publication
2000
Pages
R260 - R264
Database
ISI
SICI code
0960-9822(20000406)10:7<R260:PFVOTC>2.0.ZU;2-P
Abstract
Efficient de novo folding of actins and tubulins requires two molecular cha perones, the chaperonin TRiC (or CCT) and its novel cofactor GimC (or prefo ldin). Recent studies indicate that TRiC is exquisitely adapted for this ta sk, yet has the ability to interact with and assist the folding of numerous other cellular proteins. (C) 2000 Elsevier Science Ltd. All rights reserve d.