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

P Goloubinoff; A A Gatenby; G H Lorimer

doi:10.1038/337044a0

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

Nature. 1989 Jan 5;337(6202):44-7. doi: 10.1038/337044a0.

Authors

P Goloubinoff¹, A A Gatenby, G H Lorimer

Affiliation

¹ Central Research and Development Department, E.I. DuPont de Nemours and Co., Wilmington, Delaware 19880-0402.

PMID: 2562907
DOI: 10.1038/337044a0

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
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

Substances

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