title: Potassium ions and the molecular-chaperone activity of DnaK.
abstract: 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.
authors.affiliation: Biochemisches Institut der Universität Zürich, Switzerland.
authors.forename: B
authors.initials: B
authors.lastname: Feifel
authors.forename: E
authors.initials: E
authors.lastname: Sandmeier
authors.forename: H J
authors.initials: HJ
authors.lastname: Schönfeld
authors.forename: P
authors.initials: P
authors.lastname: Christen
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D002414:Cations, Monovalent; D018833:Chaperonins / Q000378:metabolism*; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D011188:Potassium / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D002414:Cations, Monovalent; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D018833:Chaperonins; C063842:dnaK protein, E coli; D011188:Potassium