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J. Biol. Chem., Vol. 281, Issue 9, 5575-5581, March 3, 2006

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Stimulation of DNA Strand Exchange by the Human TBPIP/Hop2-Mnd1 Complex^*

Rima Enomoto, Takashi Kinebuchi, Makoto Sato^¶, Hideshi Yagi, Hitoshi Kurumizaka^||1, and Shigeyuki Yokoyama^**2

From the RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan, the Division of Cell Biology and Neuroscience, Department of Morphological and Physiological Sciences, Faculty of Medical Sciences, University of Fukui, 23-3 Shimoaizuki, Matsuoka-cho, Fukui 910-1193 Japan, the ^¶Solution Oriented Research for Science and Technology (SORST), Japan Science and Technology Agency (JST), 4-1-8 Honcho Kawaguchi-shi, Saitama 332-0012, Japan, the ^||Graduate School of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan, the ^**RIKEN Harima Institute at SPring-8, 1-1-1 Kohto, Mikazuki-cho, Sayo, Hyogo 679-5148, Japan, and the Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

In Saccharomyces cerevisiae, the Hop2 protein forms a complex with the Mnd1 protein and is required for the alignment of homologous chromosomes during meiosis, probably through extensive homology matching between them. The Rad51 and Dmc1 proteins, the eukaryotic RecA orthologs, promote strand exchange and may function in the extensive matching of homology within paired DNA molecules. In the present study, we purified the human TBPIP/Hop2-Mnd1 complex and found that it significantly stimulates the Dmc1- and Rad51-mediated strand exchange. The human Hop2-Mnd1 complex preferentially binds to a three-stranded DNA branch, which mimics the strand-exchange intermediate. These findings are consistent with genetic data, which showed that the Hop2 and Mnd1 proteins are required for homology matching between homologous chromosomes. Therefore, the human TBPIP/Hop2-Mnd1 complex may ensure proper pairing between homologous chromosomes through its stimulation of strand exchange during meiosis.

Received for publication, June 15, 2005 , and in revised form, December 20, 2005.

^* This work was supported by the RIKEN Structural Genomics/Proteomics Initiative (RSGI); the National Project on Protein Structural and Functional Analyses; grants-in-aid from the Japanese Society for the Promotion of Science (JSPS); the Ministry of Education, Sports, Culture, Science, and Technology, Japan; and the Japan Health Sciences Foundation. 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.

¹ To whom correspondence may be addressed. Tel.: 81-3-5286-8189; Fax: 81-3-5292-9211; E-mail: kurumizaka{at}waseda.jp. ² To whom correspondence may be addressed. Tel.: 81-45-503-9197; Fax: 81-3-503-9195; E-mail: yokoyama{at}biochem.s.u-tokyo.ac.jp.

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