title: Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.
abstract: Chaperonins GroEL and GroES form two types of hetero-oligomers in vitro that can mediate the folding of proteins. Chemical cross-linking and electron microscopy showed that in the presence of adenosine triphosphate (ATP), two GroES7 rings can successively bind a single GroEL14 core oligomer. The symmetric GroEL14(GroES7)2 chaperonin, whose central cavity appears obstructed by two GroES7 rings, can nonetheless stably bind and assist the ATP-dependent refolding of RuBisCO enzyme. Thus, unfolded proteins first bind and possibly fold on the external envelope of the chaperonin hetero-oligomer.
authors.affiliation: Department of Botany, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Israel.
authors.forename: A
authors.initials: A
authors.lastname: Azem
authors.forename: M
authors.initials: M
authors.lastname: Kessel
authors.forename: P
authors.initials: P
authors.lastname: Goloubinoff
mesh_terms: D000255:Adenosine Triphosphate; D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology*; D001704:Biopolymers; D018835:Chaperonin 10; D018834:Chaperonin 60; D003432:Cross-Linking Reagents; D005976:Glutaral; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000502:physiology*; D017510:Protein Folding; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D001704:Biopolymers; D018835:Chaperonin 10; D018834:Chaperonin 60; D003432:Cross-Linking Reagents; D006360:Heat-Shock Proteins; D000255:Adenosine Triphosphate; D012273:Ribulose-Bisphosphate Carboxylase; D005976:Glutaral