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

Details

Serval ID
serval:BIB_9E2EAB13539E
Type
Article: article from journal or magazin.
Collection
Publications
Title
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.
Journal
Nature
Author(s)
Goloubinoff P., Gatenby A.A., Lorimer G.H.
ISSN
0028-0836 (Print)
ISSN-L
0028-0836
Publication state
Published
Issued date
1989
Volume
337
Number
6202
Pages
44-47
Language
english
Abstract
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.
Keywords
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
Create date
24/01/2008 20:02
Last modification date
20/08/2019 15:04
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