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Plant and Cell Physiology, 1995, Vol. 36, No. 1 19-27
© 1995

Detection and Characterization of Protein Kinases in Rice Phloem Sap

Shin-ichi Nakamura, Hiroaki Hayashi, Satoshi Mori and Mitsuo Chino

Department of Applied Biological Chemistry, Division of Agriculture and Agricultural Life Sciences, The University of Tokyo Bunkyo-ku, Tokyo, 113 Japan

Calcium-dependent protein kinases were detected and characterized in the phloem sap of rice plants. Protein phosphorylation was activated in the presence of micromolar levels of free Ca2+ ions but was not activated by a polyamine in vitro. Mg2+ ions were essential for protein phosphorylation and K+ ions inhibited the protein phosphorylation. Analysis by two-dimensional polyacrylamide electrophoresis revealed that 17-kDa protein with a pI of 5.0 was the most highly phosphorylated protein in the phloem sap of rice plants. A protein of 65 kDa, which was autophosphorylated, had a Ca2+-dependent protein kinase activity and the mobility of this band in SDS gel was changed in the presence of calcium. These results suggest that a signal-transport system may exist in the sieve tubes of rice plants that operates via the phosphorylation of proteins by calcium dependent protein kinases.

(Received December 20, 1993; Accepted October 8, 1994)
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