Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.

Détails

ID Serval
serval:BIB_C5F1A955BE75
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.
Périodique
Science
Auteur(s)
Azem A., Kessel M., Goloubinoff P.
ISSN
0036-8075 (Print)
ISSN-L
0036-8075
Statut éditorial
Publié
Date de publication
1994
Volume
265
Numéro
5172
Pages
653-656
Langue
anglais
Résumé
Chaperonins GroEL and GroES form two types of hetero-oligomers in vitro that can mediate the folding of proteins. Chemical cross-linking and electron microscopy showed that in the presence of adenosine triphosphate (ATP), two GroES7 rings can successively bind a single GroEL14 core oligomer. The symmetric GroEL14(GroES7)2 chaperonin, whose central cavity appears obstructed by two GroES7 rings, can nonetheless stably bind and assist the ATP-dependent refolding of RuBisCO enzyme. Thus, unfolded proteins first bind and possibly fold on the external envelope of the chaperonin hetero-oligomer.
Mots-clé
Adenosine Triphosphate, Bacterial Proteins/chemistry, Bacterial Proteins/physiology, Biopolymers, Chaperonin 10, Chaperonin 60, Cross-Linking Reagents, Glutaral, Heat-Shock Proteins/chemistry, Heat-Shock Proteins/physiology, Protein Folding, Ribulose-Bisphosphate Carboxylase/chemistry
Pubmed
Web of science
Création de la notice
24/01/2008 21:02
Dernière modification de la notice
20/08/2019 16:41
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