IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v427y2004i6974d10.1038_nature02312.html
   My bibliography  Save this article

The conserved kinetochore protein shugoshin protects centromeric cohesion during meiosis

Author

Listed:
  • Tomoya S. Kitajima

    (University of Tokyo)

  • Shigehiro A. Kawashima

    (University of Tokyo)

  • Yoshinori Watanabe

    (University of Tokyo
    SORST, Japan Science and Technology Agency)

Abstract

Meiosis comprises a pair of specialized nuclear divisions that produce haploid germ cells. To accomplish this, sister chromatids must segregate together during the first meiotic division (meiosis I), which requires that sister chromatid cohesion persists at centromeres. The factors that protect centromeric cohesion during meiosis I have remained elusive. Here we identify Sgo1 (shugoshin), a protector of the centromeric cohesin Rec8 in fission yeast. We also identify a homologue of Sgo1 in budding yeast. We provide evidence that shugoshin is widely conserved among eukaryotes. Moreover, we identify Sgo2, a paralogue of shugoshin in fission yeast, which is required for faithful mitotic chromosome segregation. Localization of Sgo1 and Sgo2 at centromeres requires the kinase Bub1, identifying shugoshin as a crucial target for the kinetochore function of Bub1. These findings provide insights into the evolution of meiosis and kinetochore regulation during mitosis and meiosis.

Suggested Citation

  • Tomoya S. Kitajima & Shigehiro A. Kawashima & Yoshinori Watanabe, 2004. "The conserved kinetochore protein shugoshin protects centromeric cohesion during meiosis," Nature, Nature, vol. 427(6974), pages 510-517, February.
  • Handle: RePEc:nat:nature:v:427:y:2004:i:6974:d:10.1038_nature02312
    DOI: 10.1038/nature02312
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature02312
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature02312?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    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:nature:v:427:y:2004:i:6974:d:10.1038_nature02312. 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.