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J Biol Chem, Vol. 274, Issue 51, 36670-36678, December 17, 1999
From the Department of Biology, Massachusetts Institute of
Technology, Cambridge, Massachusetts 02139
Preparations of Escherichia coli DnaK
from our lab as well as preparations of DnaK and other HSP70 proteins
from several major labs in the field produce a stoichiometric initial
burst of [
Inferences Concerning the ATPase Properties of DnaK and Other
HSP70s Are Affected by the ADP Kinase Activity of Copurifying
Nucleoside-diphosphate Kinase*
-32P]ADP when incubated with
[-32P]ATP and contain an ADP kinase activity. We
determined that the initial burst activity results from the transfer of
-phosphate from the radiolabeled substrate
[-32P]ATP to unlabeled ADP bound by the DnaK and is
the same activity that results in ADP phosphorylation. The purification
of DnaK from E. coli cells that carry a disrupted
ndk gene, ndk::km, results in
preparations with greatly reduced ADP kinase activities compared with
preparations of DnaK purified from ndk+ cells.
The reduction in the amount of ADP kinase activity in preparations of
DnaK purified from ndk::km cells shows that
nucleoside-diphosphate kinase (NDP kinase) is responsible for most of
the ADP kinase activity present in DnaK preparations isolated from
ndk+ cells. The remaining ADP kinase activity
in preparations from ndk::km cells, which varies
between preparations, is also a property of NDP kinase, which is most
likely expressed because of a low frequency reversion of the disrupted
ndk gene. A weak, but measurable physical interaction
exists between DnaK and NDP kinase and may be at least partially
responsible for the co-purification of NDP kinase with DnaK. The
presence of contaminating NDP kinase can explain the range of
kcat values reported for the ATPase activity of
DnaK as well as recent reports of initial burst kinetics by DnaK
(Banecki, B., and Zylicz, M. (1996) J. Biol. Chem.
271, 6137-6143) and an ADP-ATP exchange activity of DnaK (Hiromura,
M., Yano, M., Mori, H., Inoue, M., and Kido, H. (1998) J. Biol. Chem. 273, 5435-5438).
*
This work was supported by National Institutes of Health
Grants GM28988 and CA21615.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biology,
68-633, Massachusetts Institute of Technology, 77 Massachusetts Ave.,
Cambridge, MA 02139. Tel.: (617) 253-6716; Fax: (617) 253-2643; E-mail:
gwalker@mit.edu.
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