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J. Biol. Chem., Vol. 277, Issue 31, 28340-28350, August 2, 2002
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From the Department of Plant Sciences, University of Arizona,
Tucson, Arizona 85721
The Arabidopsis SOS2 (Salt Overly
Sensitive 2)-like protein kinases (PKS) are novel protein kinases that
contain an SNF1-like catalytic domain with a putative activation loop
and a regulatory domain with an FISL motif that binds calcium sensors.
Very little biochemical and functional information is currently
available on this family of kinases. Here we report on the expression
of the PKS11 gene, activation and characterization of the
gene product, and transgenic evaluation of its function in plants.
PKS11 transcript was preferentially expressed in roots of
Arabidopsis plants. Recombinant glutathione
S-transferase fusion protein of PKS11 was inactive in
substrate phosphorylation. However, the kinase can be highly activated
by a threonine 161 to aspartate substitution (designated PKS11T161D) in
the putative activation loop. Interestingly, PKS11 can also be
activated by substitution of either a serine or tyrosine with aspartate
within the activation loop. Deletion of the FISL motif also resulted in
a slight activation of PKS11. PKS11T161D displayed an uncommon
preference for Mn2+ over Mg2+ for substrate
phosphorylation and autophosphorylation. The optimal pH and temperature
values of PKS11T161D were determined to be 7.5 and 30 °C,
respectively. The activated kinase showed substrate specificity, high
affinity, and catalytic efficiency for a peptide substrate p3 and for
ATP. AMP or ADP at concentrations from 10 µM to 1 mM did not activate PKS11T161D. Transgenic
Arabidopsis plants expressing PKS11T161D were
more resistant to high concentrations of glucose, suggesting the
involvement of this protein kinase in sugar signaling in plants. These
results provide insights into the function as well as regulation and
biochemical properties of the PKS protein kinase.
Biochemical and Functional Characterization of PKS11,
a Novel Arabidopsis Protein Kinase*
*
This work was supported by National Institutes of Health
Grant R01GM59138 (to J.-K. Z.).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 Plant
Sciences, University of Arizona, Tucson, AZ 85721. Tel.: 520-626-2229; Fax: 520-621-7186; E-mail: jkzhu@ag.arizona.edu.
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