Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

Détails

ID Serval
serval:BIB_147E9294FCBD
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
Périodique
Nature
Auteur(s)
Goloubinoff P., Christeller J.T., Gatenby A.A., Lorimer G.H.
ISSN
0028-0836 (Print)
ISSN-L
0028-0836
Statut éditorial
Publié
Date de publication
1989
Volume
342
Numéro
6252
Pages
884-889
Langue
anglais
Résumé
In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded polypeptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitochondria (hsp60) or chloroplasts (Rubisco sub-unit-binding protein), together with chaperonin-10 from E. coli (groES), and Mg-ATP. Because chaperonins are ubiquitous, a conserved Mg-ATP-dependent mechanism exists that uses the chaperonins to facilitate the folding of some other proteins.
Mots-clé
Adenosine Triphosphate/metabolism, Chaperonin 10/metabolism, Chaperonin 60/metabolism, Chloroplasts/enzymology, Escherichia coli, Protein Conformation, Ribulose-Bisphosphate Carboxylase/chemistry, Ribulose-Bisphosphate Carboxylase/metabolism
Pubmed
Web of science
Création de la notice
24/01/2008 21:02
Dernière modification de la notice
20/08/2019 13:43
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