GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP.

Détails

ID Serval
serval:BIB_4D6CE1BE6422
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATP.
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur(s)
Priya S., Sharma S.K., Sood V., Mattoo R.U., Finka A., Azem A., De Los Rios P., Goloubinoff P.
ISSN
1091-6490 (Electronic)
ISSN-L
0027-8424
Statut éditorial
Publié
Date de publication
2013
Volume
110
Numéro
18
Pages
7199-7204
Langue
anglais
Résumé
Chaperonins are cage-like complexes in which nonnative polypeptides prone to aggregation are thought to reach their native state optimally. However, they also may use ATP to unfold stably bound misfolded polypeptides and mediate the out-of-cage native refolding of large proteins. Here, we show that even without ATP and GroES, both GroEL and the eukaryotic chaperonin containing t-complex polypeptide 1 (CCT/TRiC) can unfold stable misfolded polypeptide conformers and readily release them from the access ways to the cage. Reconciling earlier disparate experimental observations to ours, we present a comprehensive model whereby following unfolding on the upper cavity, in-cage confinement is not needed for the released intermediates to slowly reach their native state in solution. As over-sticky intermediates occasionally stall the catalytic unfoldase sites, GroES mobile loops and ATP are necessary to dissociate the inhibitory species and regenerate the unfolding activity. Thus, chaperonin rings are not obligate confining antiaggregation cages. They are polypeptide unfoldases that can iteratively convert stable off-pathway conformers into functional proteins.
Pubmed
Web of science
Open Access
Oui
Création de la notice
13/06/2013 18:12
Dernière modification de la notice
20/08/2019 15:02
Données d'usage