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Volume 271, Number 35, Issue of August 30, 1996 pp. 21439-21445
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Analysis of M Phase-specific Phosphorylation of DNA Topoisomerase II

(Received for publication, November 13, 1995, and in revised form, April 3, 1996)

Keiji Kimura , Naohito Nozaki , Takemi Enomoto ^¶ , Masato Tanaka and Akihiko Kikuchi

From the  Mitsubishi Kasei Institute of Life Sciences, Machida, Tokyo 194 and the ^¶ Department of Molecular Cell Biology, Faculty of Pharmaceutical Sciences, Tohoku University, Aoba Aramaki, Aoba-ku, Sendai, Miyagi 980-77, Japan

In mammalian cells, two isoforms of DNA topoisomerase II (topo II), topo II and topo II, are phosphorylated. The phosphorylation of topo II changes its apparent molecular mass determined by SDS-polyacrylamide gel electrophoresis from 180 to 190 kDa in mitotic cells, whereas topo II affects it only slightly (Kimura, K., Nozaki, N., Saijo, M., Kikuchi, A., Ui, M., and Enomoto, T. (1994) J. Biol. Chem. 269, 24523-24526). Here we examined the stability of the protein and the phosphate moiety of each topo II isoform, as the cells progressed from M to G₁ phase. While its protein moiety remained intact, 75% of the phosphates attached to topo II were removed within 4 h after release from mitotic block. On the other hand, 35% of topo II protein and 52% of the attached phosphates disappeared. We verified that M phase-specific phosphorylation had no particular effect on the catalytic activities of both topo II isoforms after extensive phosphatase digestion. We also examined the binding of two isoforms to the nucleus or chromosomes. In logarithmically growing cells, both isoforms were extracted from nuclei at the same concentrations of NaCl. From the mitotic chromosomes, topo II was extracted at much lower concentrations of NaCl than topo II.

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