CHARACTERIZATION OF A FUNCTIONAL GROEL(14)(GROES(7))(2) CHAPERONIN HETERO-OLIGOMER
CHARACTERIZATION OF A FUNCTIONAL GROEL(14)(GROES(7))(2) CHAPERONIN HETERO-OLIGOMER
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DOI：
10.1126/science.7913553
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发表时间：
1994-07-29
期刊：
影响因子：
56.9
通讯作者：
GOLOUBINOFF, P
中科院分区：
文献类型：
--
作者：
AZEM, A;KESSEL, M;GOLOUBINOFF, P
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 GroES(7) rings can successively bind a single GroEL(14) core oligomer. The symmetric GroEL(14)(GroES(7))(2) chaperonin, whose central cavity appears obstructed by two GroES(7) 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.
