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.

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