title: GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.
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.
authors.affiliation: Central Research and Development Department, E.I. DuPont de Nemours and Co., Wilmington, Delaware 19880-0402.
authors.forename: P
authors.initials: P
authors.lastname: Goloubinoff
authors.forename: A A
authors.initials: AA
authors.lastname: Gatenby
authors.forename: G H
authors.initials: GH
authors.lastname: Lorimer
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000494:pharmacology*; D018835:Chaperonin 10; D018834:Chaperonin 60; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial; D006360:Heat-Shock Proteins / Q000235:genetics / Q000494:pharmacology*; D009154:Mutation; D010957:Plasmids; D012273:Ribulose-Bisphosphate Carboxylase / Q000096:biosynthesis*; D014170:Transformation, Genetic
chemical_list: D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D012273:Ribulose-Bisphosphate Carboxylase