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Nucleic Acids Research 2004 32(11):3325-3339; doi:10.1093/nar/gkh654
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Published online 21 June 2004

Nucleic Acids Research, Vol. 32 No. 11 © Oxford University Press 2004; all rights reserved

Mcp7, a meiosis-specific coiled-coil protein of fission yeast, associates with Meu13 and is required for meiotic recombination

Takamune T. Saito, Takahiro Tougan, Takashi Kasama, Daisuke Okuzaki and Hiroshi Nojima*

Department of Molecular Genetics, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan

* To whom correspondence should be addressed. Tel: +81 6 6875 3980; Fax: +81 6 6875 5192; Email: snj-0212{at}biken.osaka-u.ac.jp

Received April 22, 2004; Revised and Accepted May 26, 2004

We previously showed that Meu13 of Schizosaccharomyces pombe functions in homologous pairing and recombination at meiosis I. Here we show that a meiosis-specific gene encodes a coiled-coil protein that complexes with Meu13 during meiosis in vivo. This gene denoted as mcp7+ (after meiotic coiled-coil protein) is an ortholog of Mnd1 of Saccharomyces cerevisiae. Mcp7 proteins are detected on meiotic chromatin. The phenotypes of mcp7{Delta} cells are similar to those of meu13{Delta} cells as they show reduced recombination rates and spore viability and produce spores with abnormal morphology. However, a delay in initiation of meiosis I chromosome segregation of mcp7{Delta} cells is not so conspicuous as meu13{Delta} cells, and no meiotic delay is observed in mcp7{Delta}meu13{Delta} cells. Mcp7 and Meu13 proteins depend on each other differently; Mcp7 becomes more stable in meu13{Delta} cells, whereas Meu13 becomes less stable in mcp7{Delta} cells. Genetic analysis shows that Mcp7 acts in the downstream of Dmc1, homologs of Escherichia coli RecA protein, for both recombination and subsequent sporulation. Taken together, we conclude that Mcp7 associates with Meu13 and together they play a key role in meiotic recombination.


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