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Related Experiment Videos

DnaK ATPase activity revisited

D R Palleros1, K L Reid, L Shi

  • 1Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064.

FEBS Letters
|December 20, 1993
PubMed
Summary
This summary is machine-generated.

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The ATPase activity of E. coli DnaK (a heat shock protein) is influenced by protein purification. Purified DnaK showed lower activity, suggesting the monomer, not the dimer, is the active form.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Protein Chemistry

Background:

  • DnaK, a 70 kDa heat shock protein from E. coli, exhibits ATPase activity.
  • Previous studies suggested DnaK dimer formation autostimulates ATPase activity with increasing protein concentration.

Purpose of the Study:

  • To investigate the ATPase activity of different DnaK preparations.
  • To determine the active species responsible for DnaK's ATPase activity.

Main Methods:

  • Protein purification using High-Performance Liquid Chromatography (HPLC).
  • Measurement of ATPase turnover number for various DnaK preparations.

Main Results:

  • ATPase turnover number was highly dependent on protein purification methods.

Related Experiment Videos

  • HPLC-purified DnaK exhibited a 20- to 50-fold lower turnover number compared to previously reported values.
  • No evidence of autostimulation was observed with purified DnaK preparations.

    • Conclusions:

    • The monomeric form of DnaK is likely the enzymatically active species.
    • Protein purification significantly impacts the measured ATPase activity of DnaK.