Facilitated release of substrate protein from prefoldin by chaperonin.
FEBS Lett
; 579(17): 3718-24, 2005 Jul 04.
Article
em En
| MEDLINE
| ID: mdl-15967441
ABSTRACT
Prefoldin is a chaperone that captures a protein-folding intermediate and transfers it to the group II chaperonin for correct folding. However, kinetics of interactions between prefoldin and substrate proteins have not been investigated. In this study, dissociation constants and dissociation rate constants of unfolded proteins with prefoldin were firstly measured using fluorescence microscopy. Our results suggest that binding and release of prefoldin from hyperthermophilic archaea with substrate proteins were in a dynamic equilibrium. Interestingly, the release of substrate proteins from prefoldin was facilitated when chaperonin was present, supporting a handoff mechanism of substrate proteins from prefoldin to the chaperonin.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Chaperonas Moleculares
/
Chaperoninas
/
Proteínas Arqueais
/
Pyrococcus horikoshii
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Japão