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PLANT PHYSIOLOGY , Vol 108, Issue 2 787-793, Copyright © 1995 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
A Rice Membrane Calcium-Dependent Protein Kinase Is Induced by Gibberellin
M. Abo-El-Saad and R. Wu
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853
A rice (Oryza sativa) seed plasma-membrane calcium-dependent
serine/threonine protein kinase (CDPK) has been partially purified.
Comparing results in seeds that were treated with and without the plant
hormone gibberellin (GA) for 10 min showed that rice CDPK was highly
induced by GA. After separating solubilized membrane proteins by sodium
dodecyl sulfate-gel electrophoresis, followed by renaturation, a
radiolabeled phosphoprotein band of approximately 58 kD was detected, and
it was apparently produced by autophosphorylation. There are five aspects
of the rice CDPK that show similarity to mammalian protein kinase C (PKC)
and to other plant CDPKs: (a) Histone IIIS and PKC peptide-ser25 (19-31)
are phosphorylated by rice CDPK. (b) The phosphorylation reaction is
strictly dependent on calcium. (c) The activity of the rice CDPK is
inhibited by either staurosporine or the PKC inhibitory peptide (19-36).
(d) Addition of calmodulin has no effect on the activity of the enzyme;
however, the CDPK is inhibited by the calmodulin antagonists
trifluoperazine and W-7. (e) The rice CDPK reacts with a mammalian anti-PKC
antibody in immunoblotting analysis. However, there is one major difference
between the rice CDPK and other CDPKs: the rice CDPK is induced by GA,
whereas no mammalian PKC or other plant CDPKs are known to be induced by
any hormone.
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