IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v9y2018i1d10.1038_s41467-018-06377-w.html
   My bibliography  Save this article

The chromatin remodeler RSF1 controls centromeric histone modifications to coordinate chromosome segregation

Author

Listed:
  • Ho-Soo Lee

    (Ajou University School of Medicine
    Genomic Instability Research Center, Ajou University School of Medicine)

  • Zhonghui Lin

    (University of Texas Southwestern Medical Center
    College of Chemistry, Fuzhou University)

  • Sunyoung Chae

    (Institute of Medical Science, Ajou University School of Medicine)

  • Young-Suk Yoo

    (Ajou University School of Medicine
    Genomic Instability Research Center, Ajou University School of Medicine)

  • Byung-Gyu Kim

    (Center for Genomic Integrity, Institute for Basic Science, UNIST)

  • Youngsoo Lee

    (Genomic Instability Research Center, Ajou University School of Medicine)

  • Jared L. Johnson

    (Weill Cornell Medical College)

  • You-Sun Kim

    (Ajou University School of Medicine)

  • Lewis C. Cantley

    (Weill Cornell Medical College)

  • Chang-Woo Lee

    (Sungkyunkwan University School of Medicine)

  • Hongtao Yu

    (University of Texas Southwestern Medical Center)

  • Hyeseong Cho

    (Ajou University School of Medicine
    Genomic Instability Research Center, Ajou University School of Medicine)

Abstract

Chromatin remodelers regulate the nucleosome barrier during transcription, DNA replication, and DNA repair. The chromatin remodeler RSF1 is enriched at mitotic centromeres, but the functional consequences of this enrichment are not completely understood. Shugoshin (Sgo1) protects centromeric cohesion during mitosis and requires BuB1-dependent histone H2A phosphorylation (H2A-pT120) for localization. Loss of Sgo1 at centromeres causes chromosome missegregation. Here, we show that RSF1 regulates Sgo1 localization to centromeres through coordinating a crosstalk between histone acetylation and phosphorylation. RSF1 interacts with and recruits HDAC1 to centromeres, where it counteracts TIP60-mediated acetylation of H2A at K118. This deacetylation is required for the accumulation of H2A-pT120 and Sgo1 deposition, as H2A-K118 acetylation suppresses H2A-T120 phosphorylation by Bub1. Centromeric tethering of HDAC1 prevents premature chromatid separation in RSF1 knockout cells. Our results indicate that RSF1 regulates the dynamics of H2A histone modifications at mitotic centromeres and contributes to the maintenance of chromosome stability.

Suggested Citation

  • Ho-Soo Lee & Zhonghui Lin & Sunyoung Chae & Young-Suk Yoo & Byung-Gyu Kim & Youngsoo Lee & Jared L. Johnson & You-Sun Kim & Lewis C. Cantley & Chang-Woo Lee & Hongtao Yu & Hyeseong Cho, 2018. "The chromatin remodeler RSF1 controls centromeric histone modifications to coordinate chromosome segregation," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06377-w
    DOI: 10.1038/s41467-018-06377-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-018-06377-w
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-018-06377-w?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:9:y:2018:i:1:d:10.1038_s41467-018-06377-w. 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.