IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-16750-3.html
   My bibliography  Save this article

Real-time tracking reveals catalytic roles for the two DNA binding sites of Rad51

Author

Listed:
  • Kentaro Ito

    (Tokyo Institute of Technology)

  • Yasuto Murayama

    (Tokyo Institute of Technology
    National Institute of Genetics
    SOKENDAI (The Graduate University for Advanced Studies))

  • Yumiko Kurokawa

    (Tokyo Institute of Technology
    National Institute of Genetics)

  • Shuji Kanamaru

    (Tokyo Institute of Technology
    Tokyo Institute of Technology)

  • Yuichi Kokabu

    (Yokohama City University
    Mitsui Knowledge Industry)

  • Takahisa Maki

    (Tokyo Institute of Technology)

  • Tsutomu Mikawa

    (RIKEN Center for Biosystems Dynamics Research)

  • Bilge Argunhan

    (Tokyo Institute of Technology)

  • Hideo Tsubouchi

    (Tokyo Institute of Technology
    Tokyo Institute of Technology)

  • Mitsunori Ikeguchi

    (Yokohama City University)

  • Masayuki Takahashi

    (Tokyo Institute of Technology)

  • Hiroshi Iwasaki

    (Tokyo Institute of Technology
    Tokyo Institute of Technology)

Abstract

During homologous recombination, Rad51 forms a nucleoprotein filament on single-stranded DNA to promote DNA strand exchange. This filament binds to double-stranded DNA (dsDNA), searches for homology, and promotes transfer of the complementary strand, producing a new heteroduplex. Strand exchange proceeds via two distinct three-strand intermediates, C1 and C2. C1 contains the intact donor dsDNA whereas C2 contains newly formed heteroduplex DNA. Here, we show that the conserved DNA binding motifs, loop 1 (L1) and loop 2 (L2) in site I of Rad51, play distinct roles in this process. L1 is involved in formation of the C1 complex whereas L2 mediates the C1–C2 transition, producing the heteroduplex. Another DNA binding motif, site II, serves as the DNA entry position for initial Rad51 filament formation, as well as for donor dsDNA incorporation. Our study provides a comprehensive molecular model for the catalytic process of strand exchange mediated by eukaryotic RecA-family recombinases.

Suggested Citation

  • Kentaro Ito & Yasuto Murayama & Yumiko Kurokawa & Shuji Kanamaru & Yuichi Kokabu & Takahisa Maki & Tsutomu Mikawa & Bilge Argunhan & Hideo Tsubouchi & Mitsunori Ikeguchi & Masayuki Takahashi & Hiroshi, 2020. "Real-time tracking reveals catalytic roles for the two DNA binding sites of Rad51," Nature Communications, Nature, vol. 11(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16750-3
    DOI: 10.1038/s41467-020-16750-3
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-16750-3
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-020-16750-3?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:11:y:2020:i:1:d:10.1038_s41467-020-16750-3. 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.