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Plant Physiol, May 2000, Vol. 123, pp. 403-412
Regulation of a Plant SNF1-Related Protein Kinase by
Glucose-6-Phosphate1
Dikran
Toroser,
Zvi
Plaut,2 and
Steven C.
Huber*
United States Department of Agriculture, Agricultural Research
Service, and Departments of Crop Science and Botany, North Carolina
State University, Raleigh, North Carolina, 27695-7631
One of the major protein kinases (PKIII) that
phosphorylates serine-158 of spinach sucrose-phosphate synthase (SPS),
which is responsible for light/dark modulation of activity, is known to
be a member of the SNF1-related family of protein kinases. In the
present study, we have developed a fluorescence-based continuous assay
for measurement of PKIII activity. Using the continuous assay, along with the fixed-time-point 32P-incorporation
assay, we demonstrate that PKIII activity is inhibited by
glucose-6-phosphate (Glc-6-P). Relative inhibition by Glc-6-P was
increased by decreasing pH from 8.5 to 5.5 and by reducing the
concentration of Mg2+ in the assay from 10 to 2 mM. Under likely physiological conditions (pH 7.0 and 2 mM Mg2+), 10 mM Glc-6-P inhibited
kinase activity approximately 70%. Inhibition by Glc-6-P could not be
ascribed to contaminants in the commercial preparations. Other
metabolites inhibited PKIII in the following order:
Glc-6-P > mannose-6-P, fructose-1,6P2 > ribose-5-P, 3-PGA, fructose-6-P. Inorganic phosphate, Glc, and AMP were
not inhibitory, and free Glc did not reverse the inhibition by Glc-6-P.
Because SNF1-related protein kinases are thought to function broadly in
the regulation of enzyme activity and gene expression, Glc-6-P
inhibition of PKIII activity potentially provides a
mechanism for metabolic regulation of the reactions catalyzed by these
important protein kinases.
1
This work was supported by the U.S. Department
of Energy (DE-AI05-91ER20031 to S.C.H.). This research represents
co-operative investigations of the U.S. Department of Agriculture,
Agricultural Research Service, and the North Carolina Agricultural
Research Service.
2
Present address: Department of Environmental
Physiology, Agricultural Research Organization, P.O. Box 6, Bet-Dagan,
Israel 50250.
*
Corresponding author; e-mail steve_huber{at}ncsu.edu; fax
919-856-4598.
© 2000 American Society of Plant Physiologists
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