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Goloubinoff P, Gatenby AA, Lorimer GH. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature. 1989;337(6202):44-7doi: 10.1038/337044a0.
Goloubinoff, P., Gatenby, A. A., & Lorimer, G. H. (1989). GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature, 337(6202), 44-7. https://doi.org/10.1038/337044a0
Goloubinoff, P, et al. "GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli." Nature vol. 337,6202 (1989): 44-7. doi: https://doi.org/10.1038/337044a0
Goloubinoff P, Gatenby AA, Lorimer GH. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature. 1989 Jan 05;337(6202):44-7. doi: 10.1038/337044a0. PMID: 2562907.
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Nature. 1989 Jan 05;337(6202):44-7. doi: 10.1038/337044a0.

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

Nature

P Goloubinoff, A A Gatenby, G H Lorimer

Affiliations

  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.

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