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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

Nature volume 333, pages 330–334 (1988)Cite this article

Abstract

An abundant chloroplast protein is implicated in the assembly of the oligomeric enzyme ribulose bisphosphate carboxylase-oxygenase, which catalyses photosynthetic CO2-fixation in higher plants. The product of the Escherichia coli groEL gene is essential for cell viability and is required for the assembly of bacteriophage capsids. Sequencing of the groEL gene and the complementary cDNA encoding the chloroplast protein has revealed that these proteins are evolutionary homologues which we term 'chaperonins'. Chaperonins comprise a class of molecular chaperones that are found in chloroplasts, mitochondria and prokaryotes. Assisted post-translational assembly of oligomeric protein structures is emerging as a general cellular phenomenon.

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Author information

Authors and Affiliations

  1. Plant Biotechnology Institute, National Research Council, Saskatoon, Saskatchewan, S7N OW9, Canada

    Sean M. Hemmingsen

  2. Department of Biological Sciences, Carnegie-Mellon University, Pittsburgh, Pennsylvania, 15213, USA

    Carol Woolford

  3. Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK

    Saskia M. van der Vies & R. John Ellis

  4. Laboratory of Biochemistry, NCI-NIH, Bethesda, Maryland, 20892, USA

    Kit Tilly

  5. Department of Biology, Queen's University, Kingston, Ontario, K7L3N6, Canada

    David T. Dennis

  6. Department of Cellular, Viral, and Molecular Biology, University of Utah Medical Center, Salt Lake City, Utah, 84132, USA

    Costa P. Georgopoulos

  7. Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania, 15260, USA

    Roger W. Hendrix

Authors
  1. Sean M. Hemmingsen
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  2. Carol Woolford
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  3. Saskia M. van der Vies
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  4. Kit Tilly
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  6. Costa P. Georgopoulos
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  7. Roger W. Hendrix
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  8. R. John Ellis
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Hemmingsen, S., Woolford, C., van der Vies, S. et al. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333, 330–334 (1988). https://doi.org/10.1038/333330a0

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