Positive cooperativity in the functioning of molecular chaperone GroEL.
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.
Institute of Protein Research, Academy of Sciences of Russia, Moscow Region.
E S
ES
Bochkareva
N M
NM
Lissin
G C
GC
Flynn
J E
JE
Rothman
A S
AS
Girshovich
D000227:Adenine Nucleotides / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D018835:Chaperonin 10; D018834:Chaperonin 60; D004926:Escherichia coli / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006868:Hydrolysis; D008024:Ligands; D011487:Protein Conformation; D013884:Thiosulfate Sulfurtransferase / Q000378:metabolism
D000227:Adenine Nucleotides; D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D008024:Ligands; D000255:Adenosine Triphosphate; D013884:Thiosulfate Sulfurtransferase