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Originally published In Press as doi:10.1074/jbc.M005179200 on August 14, 2000

J. Biol. Chem., Vol. 275, Issue 44, 34710-34718, November 3, 2000
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Mitotic Phosphorylation of DNA Topoisomerase II alpha  by Protein Kinase CK2 Creates the MPM-2 Phosphoepitope on Ser-1469*

Alexandre E. EscargueilDagger §, Sergei Y. PlisovDagger §, Odile Filhol, Claude Cochet, and Annette K. LarsenDagger ||

From the Dagger  Laboratoire de Biologie et Pharmacologie des Tumeurs, CNRS UMR 8532, Institut Gustave-Roussy PR2, Villejuif 94805 Cedex, France and  Laboratoire de Biochimie des Régulations Cellulaires Endocrine, INSERM U 244, CEA Grenoble, 38054 Grenoble Cedex 9, France

DNA topoisomerase IIalpha is required for chromatin condensation during prophase. This process is temporally linked with the appearance of mitosis-specific phosphorylation sites on topoisomerase IIalpha including one recognized by the MPM-2 monoclonal antibody. We now report that the ability of mitotic extracts to create the MPM-2 epitope on human topoisomerase IIalpha is abolished by immunodepletion of protein kinase CK2. Furthermore, the MPM-2 phosphoepitope on topoisomerase IIalpha can be generated by purified CK2. Phosphorylation of C-truncated topoisomerase IIalpha mutant proteins conclusively shows, that the MPM-2 epitope is present in the last 163 amino acids. Use of peptides containing all conserved CK2 consensus sites in this region indicates that only the peptide containing Arg-1466 to Ala-1485 is able to compete with topoisomerase IIalpha for binding of the MPM-2 antibody. Replacement of Ser-1469 with Ala abolishes the ability of the phosphorylated peptide to bind to the MPM-2 antibody while a peptide containing phosphorylated Ser-1469 binds tightly. Surprisingly, the MPM-2 phosphoepitope influences neither the catalytic activity of topoisomerase IIalpha nor its ability to form molecular complexes with CK2 in vitro. In conclusion, we have identified protein kinase CK2 as a new MPM-2 kinase able to phosphorylate an important mitotic protein, topoisomerase IIalpha , on Ser-1469.

* This work was supported by the Association pour la Recherche sur le Cancer.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Fellow of the Fondation pour la Recherche Medicale.

|| To whom correspondence should be addressed. Tel.: 33-1-42-11-45-93; Fax: 33-1-42-11-52-76; E-mail: aklarsen@igr.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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