Positive cooperativity in the functioning of molecular chaperone GroEL.
作者信息
Bochkareva E S, Lissin N M, Flynn G C, Rothman J E, Girshovich A S
机构信息
Institute of Protein Research, Academy of Sciences of Russia, Moscow Region.
出版信息
J Biol Chem. 1992 Apr 5;267(10):6796-800.
PMID:1348056
Abstract
In the presence of its partner, GroES, the tetradecameric molecular chaperone GroEL binds 14 ATP molecules, half of which are hydrolyzed in a cooperative manner. Moreover GroEL can bind, with a positive cooperativity, more than two molecules of nonfolded protein rhodanese. The role of the cooperative mechanism in the functioning of GroEL is discussed.
摘要
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