Biochemical characterization of symmetric GroEL-GroES complexes. Evidence for a role in protein folding

J Biol Chem. 1996 Jan 5;271(1):68-76. doi: 10.1074/jbc.271.1.68.


When chaperonins GroEL and GroES are incubated under functional conditions in the presence of ATP (5 mM) and K+ (150 mM), GroEL-GroES complexes appear in the incubation mixture, that are either asymmetric (1:1 GroEL:GroES oligomer ratio) or symmetric (1:2 GroEL:GroES oligomer ratio). The percentage of symmetric complexes present is directly related to the [ATP]/[ADP] ratio and to the K+ concentration. Kinetic analysis shows that there is a cycle of formation and disappearance of symmetric complexes. A correlation between the presence of symmetric complexes in the incubation mixture and its rhodanese folding activity suggests some active role of these complexes in the protein folding process. Accordingly, under functional conditions, symmetric complexes are found to contain denatured rhodanese. These data suggest that binding of substrate inside the GroEL cavity takes place before the symmetric complex is formed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chaperonin 10 / metabolism*
  • Chaperonin 60 / metabolism*
  • Escherichia coli / metabolism
  • Hydrogen-Ion Concentration
  • Iodine Radioisotopes
  • Protein Binding
  • Protein Folding*
  • Thiosulfate Sulfurtransferase / metabolism


  • Chaperonin 10
  • Chaperonin 60
  • Iodine Radioisotopes
  • Thiosulfate Sulfurtransferase