Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.
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.
Azem
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A
Department of Botany, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Israel.
Kessel
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M
Goloubinoff
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P
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
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