Plant Physiol. Drug Metab Dispos
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First published online July 10, 2003; 10.1104/pp.103.024273

Plant Physiology 132:2108-2115 (2003)
© 2003 American Society of Plant Biologists

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CELL BIOLOGY AND SIGNAL TRANSDUCTION

Pea DNA Topoisomerase I Is Phosphorylated and Stimulated by Casein Kinase 2 and Protein Kinase C

Narendra Tuteja*, Malireddy Kodandarami Reddy, Yashwanti Mudgil, Badam Singh Yadav, Meena Rani Chandok and Sudhir Kumar Sopory

International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, P.O. Box 10504, New Delhi 110 067, India

DNA topoisomerase I catalyzes the relaxation of superhelical DNA tension and is vital for DNA metabolism; therefore, it is essential for growth and development of plants. Here, we have studied the phosphorylation-dependent regulation of topoisomerase I from pea (Pisum sativum). The purified enzyme did not show autophosphorylation but was phosphorylated in an Mg2+-dependent manner by endogenous protein kinases present in pea nuclear extracts. This phosphorylation was abolished with calf intestinal alkaline phosphatase and lambda phosphatase. It was also phosphorylated by exogenous casein kinase 2 (CK2), protein kinase C (PKC; from animal sources), and an endogenous pea protein, which was purified using a novel phorbol myristate acetate affinity chromatography method. All of these phosphorylations were inhibited by heparin (inhibitor of CK2) and calphostin (inhibitor of PKC), suggesting that pea topoisomerase I is a bona fide substrate for these kinases. Spermine and spermidine had no effect on the CK2-mediated phosphorylation, suggesting that it is polyamine independent. Phospho-amino acid analysis showed that only serine residues were phosphorylated, which was further confirmed using antiphosphoserine antibody. The topoisomerase I activity increased after phosphorylation with exogenous CK2 and PKC. This study shows that these kinases may contribute to the physiological regulation of DNA topoisomerase I activity and overall DNA metabolism in plants.

* Corresponding author; e-mail narendra{at}icgeb.res.in; fax 91–11–26162316.

Received March 26, 2003; returned for revision April 23, 2003; accepted May 4, 2003.


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