(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL

Nature. 1990 Nov 22;348(6299):339-42. doi: 10.1038/348339a0.


The important Escherichia coli heat-shock protein GroEL of relative molecular mass 57,259 is a typical molecular chaperone. It possesses ATPase activity and interacts in ATP-driven reactions with non-folded proteins to stimulate their correct folding and/or assembly by preventing the formation of improper protein structures or aggregates. As GroEL is isolated and functions as a 20-25S tetradecameric particle (GroELp), the question arises--what is the mechanism of its own assembly? Here we show the (Mg-ATP)-dependent self-stimulation ('self-chaperoning') in vitro of GroELp reassembly from its monomeric state.

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Chaperonin 60
  • Circular Dichroism
  • Escherichia coli / metabolism*
  • Heat-Shock Proteins / isolation & purification
  • Heat-Shock Proteins / metabolism*
  • Kinetics
  • Macromolecular Substances
  • Molecular Weight
  • Protein Conformation
  • Thermodynamics


  • Bacterial Proteins
  • Chaperonin 60
  • Heat-Shock Proteins
  • Macromolecular Substances
  • Adenosine Triphosphate