Potassium ions and the molecular-chaperone activity of DnaK

Eur J Biochem. 1996 Apr 1;237(1):318-21. doi: 10.1111/j.1432-1033.1996.0318n.x.


Potassium ions stabilize the DnaK.ADP complex that forms on incubation of nucleotide-free DnaK with ADP or ATP. Generation of the crystallographically defined Mg2+ cluster [Wilbanks, S.M. & McKay, D.B. (1995) J. Biol. Chem. 270, 2251-2257], in which two K+ and the nucleotide are bound together with Mg2+ in the ATPase site, appears to be essential for the ATP-induced acceleration of binding of peptide ligands, the ATP-induced release of peptide ligands and for the peptide-induced increase in ATPase activity. Thus, K+ is instrumental in signal transmission between the ATPase site and the peptide-binding site.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Cations, Monovalent
  • Chaperonins / metabolism*
  • Escherichia coli Proteins*
  • HSP70 Heat-Shock Proteins / metabolism*
  • Molecular Sequence Data
  • Potassium / metabolism*
  • Protein Binding


  • Cations, Monovalent
  • Escherichia coli Proteins
  • HSP70 Heat-Shock Proteins
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Adenosine Triphosphatases
  • Chaperonins
  • dnaK protein, E coli
  • Potassium