IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v453y2008i7196d10.1038_nature06906.html
   My bibliography  Save this article

Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation

Author

Listed:
  • Robert K. McGinty

    (Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, New York 10065, USA)

  • Jaehoon Kim

    (Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10065, USA)

  • Champak Chatterjee

    (Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, New York 10065, USA)

  • Robert G. Roeder

    (Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10065, USA)

  • Tom W. Muir

    (Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, New York 10065, USA)

Abstract

Chemical ubiquitylation of histones Previous studies have suggested that histone H2B ubiquitylation and H3 K79 methylation are correlated; however, the underlying mechanism of this crosstalk is not understood, in a large part due to the difficulty of isolating homogenously ubiquitylated H2B (uH2B). McGinty et al. overcame this obstacle by developing a synthetic route to obtain uH2B, employing two traceless chemical ligation strategies. Incorporation of this protein into chemically defined nucleosomes has allowed the demonstration that ubiquitylation of H2B directly stimulates methylation of H3 K79 by the methyltransferase hDot1L in an intranucleosomal fashion.

Suggested Citation

  • Robert K. McGinty & Jaehoon Kim & Champak Chatterjee & Robert G. Roeder & Tom W. Muir, 2008. "Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation," Nature, Nature, vol. 453(7196), pages 812-816, June.
    • Handle: RePEc:nat:nature:v:453:y:2008:i:7196:d:10.1038_nature06906
    DOI: 10.1038/nature06906
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature06906
    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/nature06906?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.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Shuhei Onishi & Kotone Uchiyama & Ko Sato & Chikako Okada & Shunsuke Kobayashi & Keisuke Hamada & Tomohiro Nishizawa & Osamu Nureki & Kazuhiro Ogata & Toru Sengoku, 2024. "Structure of the human Bre1 complex bound to the nucleosome," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Anfeng Luo & Jingwei Kong & Jun Chen & Xue Xiao & Jie Lan & Xiaorong Li & Cuifang Liu & Peng-Ye Wang & Guohong Li & Wei Li & Ping Chen, 2023. "H2B ubiquitination recruits FACT to maintain a stable altered nucleosome state for transcriptional activation," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    3. Xiao Chen & Yinglu Li & Fang Zhu & Xinjing Xu & Brian Estrella & Manuel A. Pazos & John T. McGuire & Dimitris Karagiannis & Varun Sahu & Mustafo Mustafokulov & Claudio Scuoppo & Francisco J. Sánchez-R, 2023. "Context-defined cancer co-dependency mapping identifies a functional interplay between PRC2 and MLL-MEN1 complex in lymphoma," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

    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:453:y:2008:i:7196:d:10.1038_nature06906. 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.