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Nucleic Acids Research Advance Access published online on June 26, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn405
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Filament formation and robust strand exchange activities of the rice DMC1A and DMC1B proteins

Isao Sakane1, Chiaki Kamataki2, Yoshimasa Takizawa2, Marina Nakashima3, Seiichi Toki3, Hiroaki Ichikawa3, Shukuko Ikawa4, Takehiko Shibata4 and Hitoshi Kurumizaka1,2,*

1Consolidated Research Institute for Advanced Science and Medical Care, Waseda University, 513 Wasedatsurumaki-cho, Shinjuku-ku, Tokyo 162-0041, 2Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, 3Division of Plant Sciences, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602 and 4RIKEN Advanced Research Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan

*To whom correspondence should be addressed. Tel: +81 3 5369 7315; Fax: +81 3 5367 2820; Email: kurumizaka{at}waseda.jp

Received June 6, 2008. Accepted June 9, 2008.

The DMC1 protein, a meiosis-specific DNA recombinase, catalyzes strand exchange between homologous chromosomes. In rice, two Dmc1 genes, Dmc1A and Dmc1B, have been reported. Although the Oryza sativa DMC1A protein has been partially characterized, however the biochemical properties of the DMC1B protein have not been defined. In the present study, we expressed the Oryza sativa DMC1A and DMC1B proteins in bacteria and purified them. The purified DMC1A and DMC1B proteins formed helical filaments along single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA), and promoted robust strand exchange between ssDNA and dsDNA over five thousand base pairs in the presence of RPA, as a co-factor. The DMC1A and DMC1B proteins also promoted strand exchange in the absence of RPA with long DNA substrates containing several thousand base pairs. In contrast, the human DMC1 protein strictly required RPA to promote strand exchange with these long DNA substrates. The strand-exchange activity of the Oryza sativa DMC1A protein was much higher than that of the DMC1B protein. Consistently, the DNA-binding activity of the DMC1A protein was higher than that of the DMC1B protein. These biochemical differences between the DMC1A and DMC1B proteins may provide important insight into their functional differences during meiosis in rice.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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