IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v4y2013i1d10.1038_ncomms2678.html
   My bibliography  Save this article

A new protein complex promoting the assembly of Rad51 filaments

Author

Listed:
  • 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)

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.

Suggested Citation

  • Hiroyuki Sasanuma & Maki S. Tawaramoto & Jessica P. Lao & Harumi Hosaka & Eri Sanda & Mamoru Suzuki & Eiki Yamashita & Neil Hunter & Miki Shinohara & Atsushi Nakagawa & Akira Shinohara, 2013. "A new protein complex promoting the assembly of Rad51 filaments," Nature Communications, Nature, vol. 4(1), pages 1-13, June.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2678
    DOI: 10.1038/ncomms2678
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms2678
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms2678?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2678. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.