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Plant and Cell Physiology, 1993, Vol. 34, No. 6 927-933
© 1993

Protein Phosphorylation in the Sieve Tubes of Rice Plants

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

Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo Bunkyo-ku, Tokyo, 113 Japan

Proteins and their phosphorylation were examined in rice phloem sap that had been collected by the insect laser technique. Analysis by SDS-PAGE indicated that rice phloem sap contained over 150 proteins. The total protein concentration was 150–200 ng µl-1. Analysis of proteins extracted from leaves, roots and seeds revealed that several major low-molecular-weight proteins were confined to the rice phloem sap. Maintenance of rice plants under stable environmental conditions was associated with a constant complement of proteins in the phloem sap.

Phosphorylation and dephosphorylation of proteins were detected in the sieve tubes and occurred in a light dependent manner when [{gamma}--32P]ATP was supplied to leaf blades. In darkness, 17-kDa and 24-kDa proteins were phosphorylated. When plants were transferred to the light, 17-kDa and 21-kDa proteins were phosphorylated. Proteins in the rice phloem sap were also phosphorylated in vitro. The phosphorylation was Ca2+ -dependent and was inhibited by a protein kinase inhibitor.

These results indicate that a signal-transport system that involves phosphorylation of proteins may exist in rice sieve tubes.

(Received May 10, 1993; Accepted June 23, 1993)
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