DnaK ATPase activity revisited
- 20 December 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 336 (1) , 124-128
- https://doi.org/10.1016/0014-5793(93)81624-9
Abstract
It has recently been reported that the ATPase activity of DnaK, a 70 kDa heat shock protein from E. Coli, is autostimulated by increasing protein concentration [(1993) FEBS Lett. 322, 277-279], suggesting that the DnaK dimer may be the enzymatically active species. In this paper we investigated the ATPase activity of different DnaK preparations; we found that the turnover number was very dependent on protein purification. With HPLC-purified DnaK we found a turnover number 20- to 50-fold lower than typical values previously published and no evidence of autostimulation, indicating that the monomer is the active species.Keywords
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