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

Nature ·Vol. 337 ·No. 6202 ·1989-01-05 ·Pages 44-7

Goloubinoff P, Gatenby AA, Lorimer GH

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.

MeSH Terms

Bacterial Proteins/genetics,pharmacology Chaperonin 10 Chaperonin 60 Escherichia coli/genetics Genes, Bacterial Heat-Shock Proteins/genetics,pharmacology Mutation Plasmids Ribulose-Bisphosphate Carboxylase/biosynthesis Transformation, Genetic

Chemicals

Bacterial Proteins Chaperonin 10 Chaperonin 60 Heat-Shock Proteins Ribulose-Bisphosphate Carboxylase

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Goloubinoff P

Central Research and Development Department, E.I. DuPont de Nemours and Co., Wilmington, Delaware 19880-0402.

Gatenby A A

Lorimer G H

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/337044a0

Published

1989-01-05

Pages

44-7

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/337044a0 View journal details

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

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