title: Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
abstract: In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded polypeptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitochondria (hsp60) or chloroplasts (Rubisco sub-unit-binding protein), together with chaperonin-10 from E. coli (groES), and Mg-ATP. Because chaperonins are ubiquitous, a conserved Mg-ATP-dependent mechanism exists that uses the chaperonins to facilitate the folding of some other proteins.
authors.affiliation: Molecular Biology Division, E.I. Du Pont de Nemours & Co., Wilmington, Delaware 19880-0402, USA.
authors.forename: P
authors.initials: P
authors.lastname: Goloubinoff
authors.forename: J T
authors.initials: JT
authors.lastname: Christeller
authors.forename: A A
authors.initials: AA
authors.lastname: Gatenby
authors.forename: G H
authors.initials: GH
authors.lastname: Lorimer
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D018835:Chaperonin 10 / Q000378:metabolism; D018834:Chaperonin 60 / Q000378:metabolism*; D002736:Chloroplasts / Q000201:enzymology; D004926:Escherichia coli; D011487:Protein Conformation; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry* / Q000378:metabolism
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; D000255:Adenosine Triphosphate; D012273:Ribulose-Bisphosphate Carboxylase