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Nucleic Acids Research 2005 33(18):5809-5818; doi:10.1093/nar/gki883
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Published online 12 October 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

DNA topoisomerase II interacts with Lim15/Dmc1 in meiosis

Kazuki Iwabata, Akiyo Koshiyama, Taiki Yamaguchi, Hiroko Sugawara, Fumika N. Hamada, Satoshi H. Namekawa, Satomi Ishii, Takashi Ishizaki, Hiroyuki Chiku, Takayuki Nara and Kengo Sakaguchi*

Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science 2641 Yamazaki, Noda, Chiba 278-8510, Japan

*To whom correspondence should be addressed. Tel: +81 4 7124 1501 (Ext. 3409); Fax: +81 4 7123 9767; Email: kengo{at}rs.noda.tus.ac.jp

Received April 14, 2005. Revised July 3, 2005. Accepted September 19, 2005.

Lim15/Dmc1 is a meiosis specific RecA-like protein. Here we propose its participation in meiotic chromosome pairing-related events along with DNA topoisomerase II. Analysis of protein–protein interactions using in vitro binding assays provided evidence that Coprinus cinereus DNA topoisomerase II (CcTopII) specifically interacts with C.cinereus Lim15/Dmc1 (CcLim15). Co-immunoprecipitation experiments also indicated that the CcLim15 protein interacts with CcTopII in vivo. Furthermore, a significant proportion of CcLim15 and CcTopII could be shown to co-localize on chromosomes from the leptotene to the zygotene stage. Interestingly, CcLim15 can potently activate the relaxation/catenation activity of CcTopII in vitro, and CcTopII suppresses CcLim15-dependent strand transfer activity. On the other hand, while enhancement of CcLim15's DNA-dependent ATPase activity by CcTopII was found in vitro, the same enzyme activity of CcTopII was inhibited by adding CcLim15. The interaction of CcLim15 and CcTopII may facilitate pairing of homologous chromosomes.

DDBJ/EMBL/GenBank accession no. AB185148


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