K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of DnaK x DnaJ complex from Thermus thermophilus

FEBS Lett. 1997 Aug 4;412(3):633-6. doi: 10.1016/s0014-5793(97)00847-8.

Abstract

K+ is an indispensable cofactor for ATPase activity of eukaryotic cytosolic Hsp70 chaperone systems which lack a GrpE homolog. In the case of the bacterial Hsp70 (DnaK) system, GrpE, a nucleotide exchange factor, stimulates ATPase activity but little is known about the effect of K+. Here, we have cloned a grpE gene from a thermophile, Thermus thermophilus, and purified a homodimeric GrpE protein. Using proteins of this bacterium, we found that the GrpE stimulation of ATPase activity of DnaK x DnaJ complex was absolutely dependent on the presence of K+.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / physiology*
  • Cloning, Molecular
  • Dimerization
  • Drug Synergism
  • Escherichia coli Proteins*
  • HSP40 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins / drug effects
  • HSP70 Heat-Shock Proteins / metabolism*
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / drug effects
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism*
  • Heat-Shock Proteins / physiology*
  • Molecular Sequence Data
  • Potassium / physiology*
  • Thermus thermophilus / enzymology*

Substances

  • Bacterial Proteins
  • DnaJ protein, E coli
  • Escherichia coli Proteins
  • GrpE protein, Bacteria
  • HSP40 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Adenosine Triphosphatases
  • dnaK protein, E coli
  • Potassium