Positive cooperativity in the functioning of molecular chaperone GroEL

J Biol Chem. 1992 Apr 5;267(10):6796-800.

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.

MeSH terms

  • Adenine Nucleotides / metabolism
  • Adenosine Triphosphate / metabolism
  • Bacterial Proteins / metabolism*
  • Chaperonin 10
  • Chaperonin 60
  • Escherichia coli / metabolism*
  • Heat-Shock Proteins / metabolism*
  • Hydrolysis
  • Ligands
  • Protein Conformation
  • Thiosulfate Sulfurtransferase / metabolism

Substances

  • Adenine Nucleotides
  • Bacterial Proteins
  • Chaperonin 10
  • Chaperonin 60
  • Heat-Shock Proteins
  • Ligands
  • Adenosine Triphosphate
  • Thiosulfate Sulfurtransferase