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J. Biol. Chem., Vol. 279, Issue 6, 4551-4559, February 6, 2004

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Cell Cycle-dependent Phosphorylation, Nuclear Localization, and Activation of Human Condensin^*

Ai Takemoto¶, Keiji Kimura¶, Shigeyuki Yokoyama||, and Fumio Hanaoka**

From the Cellular Physiology Laboratory, Discovery Research Institute, RIKEN and Core Research for Evolutional Sciences and Technology (CREST), Japan Science and Technology Corp., 2-1 Hirosawa, Wako, Saitama 351-0198, Japan, the Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyoku, Tokyo 113-0033, Japan, ^||RIKEN Genomic Sciences Center, 1-7-22, Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan, and the ^**Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565-0871, Japan

Condensin, one of the most abundant components of mitotic chromosomes, is a conserved protein complex composed of two structural maintenance of chromosomes (SMC) subunits (SMC2- and SMC4-type) and three non-SMC subunits, and it plays an essential role in mitotic chromosome condensation. Purified condensin reconfigures DNA structure using energy provided by ATP hydrolysis. To know the regulation of condensin in somatic cells, the expression level, subcellular localization, and phosphorylation status of human condensin were examined during the cell cycle. The levels of condensin subunits were almost constant throughout the cell cycle, and the three non-SMC subunits were phosphorylated at specific sites in mitosis and dephosphorylated upon the completion of mitosis. Subcellular fractionation studies revealed that a proportion of condensin was tightly bound to mitotic chromosomes and that this form was phosphorylated at specific sites. Condensin purified from mitotic cells had much stronger supercoiling activity than that purified from interphase cells. These results suggest that condensin functions in somatic cells are regulated by phosphorylation in two ways during the cell cycle; the phosphorylation of specific sites correlates with the chromosomal targeting of condensin, and its biochemical activity is stimulated by phosphorylation.

Received for publication, October 3, 2003 , and in revised form, November 6, 2003.

^* This work was supported by grants from the Ministry of Education, Culture, Sports, Science, and Technology of Japan, a grant from the Core Research for Evolutional Sciences and Technology (CREST), Japan Science, and Technology of Japan, and a grant from the Bioarchitect Research Project of RIKEN. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Contributed equally to this work.

To whom correspondence should be addressed: Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-7975; Fax: 81-6-6877-9382; E-mail: fhanaoka{at}fbs.osaka-u.ac.jp.

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