DnaK ATPase activity revisited

FEBS Letters

Fink, Anthony L.¹  Palleros, Daniel R.¹  Shi, Li¹  Reid, Katherine L.¹ 

[1] Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA

关键词: DnaK;    hsp70;    Molecular chaperone;    ATPase;    Oligomer;    BSA;    bovine serum albumin;    DTT;    dithiothreitol;    EDTA;    ethylenediaminetetraacetic acid;    HMWS;    high molecular weight species;    HPLC;    high performance liquid chromatography;    hsp70;    70 kDa heat-shock proteins;    PAGE;    polyacrylamide gel electrophoresis;    RCMLA;    reduced carboxymethylated α-lactalbumin;    SDS;    sodium dodecyl sulfate;    SEC;    size exclusion chromatography;    TLC;    thin-layer chromatography;   

DOI  :  10.1016/0014-5793(93)81624-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown