GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

Détails

ID Serval
serval:BIB_9E2EAB13539E
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.
Périodique
Nature
Auteur(s)
Goloubinoff P., Gatenby A.A., Lorimer G.H.
ISSN
0028-0836 (Print)
ISSN-L
0028-0836
Statut éditorial
Publié
Date de publication
1989
Volume
337
Numéro
6202
Pages
44-47
Langue
anglais
Résumé
Assembly of foreign prokaryotic ribulose bisphosphate carboxylases (Rubiscos) in Escherichia coli requires both heat-shock proteins groEL and groES. GroEL is related to a chloroplast protein implicated in Rubisco assembly. Bacteria and chloroplasts therefore have a conserved mechanism that uses auxiliary proteins to assist in the assembly of Rubisco.
Mots-clé
Bacterial Proteins/genetics, Bacterial Proteins/pharmacology, Chaperonin 10, Chaperonin 60, Escherichia coli/genetics, Genes, Bacterial, Heat-Shock Proteins/genetics, Heat-Shock Proteins/pharmacology, Mutation, Plasmids, Ribulose-Bisphosphate Carboxylase/biosynthesis, Transformation, Genetic
Pubmed
Web of science
Création de la notice
24/01/2008 20:02
Dernière modification de la notice
20/08/2019 15:04
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