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

Research output: Contribution to journalArticle

54 Citations (Scopus)

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 languageEnglish (US)
Article number1676
JournalNature Communications
Volume4
DOIs
StatePublished - 2013

Fingerprint

Nucleoproteins
Single-Stranded DNA
filaments
deoxyribonucleic acid
assembly
Mediator Complex
proteins
Saccharomycetales
Homologous Recombination
DNA
Meiosis
Accessories
Dimers
Yeast
Genetic Recombination
Proteins
Nucleotides
Stabilization
Crystal structure
accessories

ASJC Scopus subject areas

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

Cite this

Sasanuma, H., Tawaramoto, M. S., Lao, J. P., Hosaka, H., Sanda, E., Suzuki, M., ... Shinohara, A. (2013). A new protein complex promoting the assembly of Rad51 filaments. Nature Communications, 4, [1676]. https://doi.org/10.1038/ncomms2678

A new protein complex promoting the assembly of Rad51 filaments. / Sasanuma, Hiroyuki; Tawaramoto, Maki S.; Lao, Jessica P.; Hosaka, Harumi; Sanda, Eri; Suzuki, Mamoru; Yamashita, Eiki; Hunter, Neil; Shinohara, Miki; Nakagawa, Atsushi; Shinohara, Akira.

In: Nature Communications, Vol. 4, 1676, 2013.

Research output: Contribution to journalArticle

Sasanuma, H, Tawaramoto, MS, Lao, JP, Hosaka, H, Sanda, E, Suzuki, M, Yamashita, E, Hunter, N, Shinohara, M, Nakagawa, A & Shinohara, A 2013, 'A new protein complex promoting the assembly of Rad51 filaments', Nature Communications, vol. 4, 1676. https://doi.org/10.1038/ncomms2678
Sasanuma H, Tawaramoto MS, Lao JP, Hosaka H, Sanda E, Suzuki M et al. A new protein complex promoting the assembly of Rad51 filaments. Nature Communications. 2013;4. 1676. https://doi.org/10.1038/ncomms2678
Sasanuma, Hiroyuki ; Tawaramoto, Maki S. ; Lao, Jessica P. ; Hosaka, Harumi ; Sanda, Eri ; Suzuki, Mamoru ; Yamashita, Eiki ; Hunter, Neil ; Shinohara, Miki ; Nakagawa, Atsushi ; Shinohara, Akira. / A new protein complex promoting the assembly of Rad51 filaments. In: Nature Communications. 2013 ; Vol. 4.
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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.",
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