Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.

Détails

ID Serval
serval:BIB_1C49BF304168
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.
Périodique
Biochemistry
Auteur(s)
Viitanen P.V., Lubben T.H., Reed J., Goloubinoff P., O'Keefe D.P., Lorimer G.H.
ISSN
0006-2960 (Print)
ISSN-L
0006-2960
Statut éditorial
Publié
Date de publication
1990
Volume
29
Numéro
24
Pages
5665-5671
Langue
anglais
Résumé
Both the chaperonin- and MgATP-dependent reconstitution of unfolded ribulosebisphosphate carboxylase (Rubisco) and the uncoupled ATPase activity of chaperonin 60 (groEL) require ionic potassium. The spontaneous, chaperonin-independent reconstitution of Rubisco, observed at 15 but not at 25 degrees C, requires no K+ and is actually inhibited by chaperonin 60, with which the unfolded or partly folded Rubisco forms a stable binary complex. The chaperonin-dependent reconstitution of Rubisco involves the formation of a complex between chaperonin 60 and chaperonin 10 (groES). Formation of this complex almost completely inhibits the uncoupled ATPase activity of chaperonin 60. Furthermore, although the formation of the chaperonin 60-chaperonin 10 complex requires the presence of MgATP, hydrolysis of ATP may not be required, since complex formation occurs in the absence of K+. The interaction of chaperonin 60 with unfolded or partly folded Rubisco does not require MgATP, K+, or chaperonin 10. However, discharge of the complex of chaperonin 60-Rubisco, which leads to the formation of active Rubisco dimers, requires chaperonin 10 and a coupled, K(+)-dependent hydrolysis of ATP. We propose that a role of chaperonin 10 is to couple the K(+)-dependent hydrolysis of ATP to the release of the folded monomers of the target protein from chaperonin 60.
Mots-clé
Adenosine Triphosphatases/metabolism, Adenosine Triphosphate/pharmacology, Bacterial Proteins/metabolism, Chaperonins, Escherichia coli/drug effects, Escherichia coli/metabolism, Hydrolysis, Potassium/pharmacology, Protein Conformation, Proteins/metabolism, Ribulose-Bisphosphate Carboxylase/metabolism, Temperature
Pubmed
Web of science
Création de la notice
24/01/2008 21:02
Dernière modification de la notice
20/08/2019 13:52
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