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Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer
A Azem1, M Kessel, P Goloubinoff
1Department of Botany, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Israel.
Science (New York, N.Y.)
|July 29, 1994
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.