Role of chaperonins in protein folding

Détails

ID Serval
serval:BIB_2AE65042B4C1
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Titre
Role of chaperonins in protein folding
Périodique
ACS Symposium Series
Auteur(s)
Goloubinoff P., Gatenby A.A., Lorimer G.H.
ISSN
0097-6156
Statut éditorial
Publié
Date de publication
1991
Peer-reviewed
Oui
Volume
470
Pages
110-118
Langue
anglais
Résumé
The chaperonin proteins, groEL and groES belong to a ubiquitous sub-family of heat-shock molecular chaperones, found in prokaryotes and in eukaryotic organelles. The chaperonins assist the folding of nascent, organelle-imported or stress-destabilized polypeptides. Using the photosynthetic enzyme Rubisco as a folding substrate, we demonstrate in vitro that this process requires firstly the formation of a binary-complex between an unstable Rubisco folding-intermediate with the oligomeric form of groEL. The second step, resulting in the formation of active Rubisco, consists of an ATP- and K+-dependent discharge of the groEL-Rubisco binary complex. GroES is required as a coupling factor between the ATP hydrolysis and the Rubisco refolding reactions which take place on the groEL oligomer. At 25-degrees-C, chaperonins assist Rubisco refolding by preventing its aggregation and not by rescuing misfolded proteins.
Mots-clé
ribulose bisphosphate carboxylase subunit binding-protein escherichia-coli heat-shock groe gene identification suppression product DNA atp
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Création de la notice
24/01/2008 21:02
Dernière modification de la notice
20/08/2019 14:10
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