Homologous plant and bacterial proteins chaperone oligomeric protein assembly

Nature. 1988 May 26;333(6171):330-4. doi: 10.1038/333330a0.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / genetics*
  • Amino Acid Sequence
  • Bacterial Proteins / genetics*
  • Base Sequence
  • Chaperonin 60
  • Chaperonins
  • Escherichia coli / enzymology
  • Escherichia coli / genetics*
  • Genes*
  • Genes, Bacterial*
  • Heat-Shock Proteins / genetics*
  • Molecular Sequence Data
  • Plants / enzymology
  • Plants / genetics*
  • Ribulose-Bisphosphate Carboxylase / genetics*
  • Sequence Homology, Nucleic Acid
  • Species Specificity


  • Bacterial Proteins
  • Chaperonin 60
  • Heat-Shock Proteins
  • Adenosine Triphosphatases
  • Chaperonins
  • Ribulose-Bisphosphate Carboxylase

Associated data

  • GENBANK/X07850
  • GENBANK/X07851
  • GENBANK/X07852