A new protein complex promoting the assembly of Rad51 filaments

Hiroyuki Sasanuma, Maki S. Tawaramoto, Jessica P. Lao, Harumi Hosaka, Eri Sanda, Mamoru Suzuki, Eiki Yamashita, Neil Hunter, Miki Shinohara, Atsushi Nakagawa () and Akira Shinohara ()
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Hiroyuki Sasanuma: Institute for Protein Research, Graduate School of Science, Osaka University
Maki S. Tawaramoto: Institute for Protein Research, Graduate School of Science, Osaka University
Jessica P. Lao: Molecular and Cellular Biology and Cell biology and Human Anatomy, Howard Hughes Medical Institute, University of California
Harumi Hosaka: Institute for Protein Research, Graduate School of Science, Osaka University
Eri Sanda: Institute for Protein Research, Graduate School of Science, Osaka University
Mamoru Suzuki: Institute for Protein Research, Graduate School of Science, Osaka University
Eiki Yamashita: Institute for Protein Research, Graduate School of Science, Osaka University
Neil Hunter: Molecular and Cellular Biology and Cell biology and Human Anatomy, Howard Hughes Medical Institute, University of California
Miki Shinohara: Institute for Protein Research, Graduate School of Science, Osaka University
Atsushi Nakagawa: Institute for Protein Research, Graduate School of Science, Osaka University
Akira Shinohara: Institute for Protein Research, Graduate School of Science, Osaka University

Nature Communications, 2013, vol. 4, issue 1, 1-13

Abstract: Abstract During homologous recombination, eukaryotic RecA homologue Rad51 assembles into a nucleoprotein filament on single-stranded DNA to catalyse homologous pairing and DNA-strand exchange with a homologous template. Rad51 nucleoprotein filaments are highly dynamic and regulated via the coordinated actions of various accessory proteins including Rad51 mediators. Here, we identify a new Rad51 mediator complex. The PCSS complex, comprising budding yeast Psy3, Csm2, Shu1 and Shu2 proteins, binds to recombination sites and is required for Rad51 assembly and function during meiosis. Within the hetero-tetramer, Psy3-Csm2 constitutes a core sub-complex with DNA-binding activity. In vitro, purified Psy3-Csm2 stabilizes the Rad51–single-stranded DNA complex independently of nucleotide cofactor. The mechanism of Rad51 stabilization is inferred by our high-resolution crystal structure, which reveals Psy3-Csm2 to be a structural mimic of the Rad51-dimer, a fundamental unit of the Rad51-filament. Together, these results reveal a novel molecular mechanism for this class of Rad51-mediators, which includes the human Rad51 paralogues.

Date: 2013
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DOI: 10.1038/ncomms2678

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