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; Akira Shinohara

doi:10.1038/ncomms2678

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, Akira Shinohara

Cell Biology and Human Anatomy

Research output: Contribution to journal › Article › peer-review

61 Scopus citations

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.

Original language	English (US)
Article number	1676
Journal	Nature Communications
Volume	4
DOIs	https://doi.org/10.1038/ncomms2678
State	Published - 2013

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Chemistry(all)
Physics and Astronomy(all)

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10.1038/ncomms2678

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title = "A new protein complex promoting the assembly of Rad51 filaments",

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.",

author = "Hiroyuki Sasanuma and Tawaramoto, {Maki S.} and Lao, {Jessica P.} and Harumi Hosaka and Eri Sanda and Mamoru Suzuki and Eiki Yamashita and Neil Hunter and Miki Shinohara and Atsushi Nakagawa and Akira Shinohara",

year = "2013",

doi = "10.1038/ncomms2678",

language = "English (US)",

volume = "4",

journal = "Nature Communications",

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publisher = "Nature Publishing Group",

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T1 - A new protein complex promoting the assembly of Rad51 filaments

AU - Sasanuma, Hiroyuki

AU - Tawaramoto, Maki S.

AU - Lao, Jessica P.

AU - Hosaka, Harumi

AU - Sanda, Eri

AU - Suzuki, Mamoru

AU - Yamashita, Eiki

AU - Hunter, Neil

AU - Shinohara, Miki

AU - Nakagawa, Atsushi

AU - Shinohara, Akira

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

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