IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v459y2009i7243d10.1038_nature07861.html
   My bibliography  Save this article

CBP/p300-mediated acetylation of histone H3 on lysine 56

Author

Listed:
  • Chandrima Das

    (Department of Biochemistry and Molecular Genetics,)

  • M. Scott Lucia

    (and)

  • Kirk C. Hansen

    (Cancer Center Proteomics Core, University of Colorado School of Medicine, PO Box 6511, Aurora Colorado 80045, USA)

  • Jessica K. Tyler

    (Department of Biochemistry and Molecular Genetics,)

Abstract

Chromatin packaging: H3K56ac makes its mark An acetylation mark within the core domain of histone H3, on lysine 56 (H3K56ac), has an important role in chromatin assembly during DNA replication and repair in budding yeast, but it has not been studied in multicellular eukaryotes. Here, two histone acetyl transferase enzymes are shown to acetylate H3K56 in Drosophila and human cells. Histones carrying K56ac are enriched at sites of DNA repair and elevated in several types of cancer.

Suggested Citation

  • Chandrima Das & M. Scott Lucia & Kirk C. Hansen & Jessica K. Tyler, 2009. "CBP/p300-mediated acetylation of histone H3 on lysine 56," Nature, Nature, vol. 459(7243), pages 113-117, May.
  • Handle: RePEc:nat:nature:v:459:y:2009:i:7243:d:10.1038_nature07861
    DOI: 10.1038/nature07861
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature07861
    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/nature07861?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. Xiao-Ru Ma & Xudong Zhu & Yujie Xiao & Hui-Min Gu & Shuang-Shuang Zheng & Liang Li & Fan Wang & Zhao-Jun Dong & Di-Xian Wang & Yang Wu & Chenyu Yang & Wenhong Jiang & Ke Yao & Yue Yin & Yang Zhang & C, 2022. "Restoring nuclear entry of Sirtuin 2 in oligodendrocyte progenitor cells promotes remyelination during ageing," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    2. Masaki Kikuchi & Satoshi Morita & Masatoshi Wakamori & Shin Sato & Tomomi Uchikubo-Kamo & Takehiro Suzuki & Naoshi Dohmae & Mikako Shirouzu & Takashi Umehara, 2023. "Epigenetic mechanisms to propagate histone acetylation by p300/CBP," Nature Communications, Nature, vol. 14(1), pages 1-16, 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:459:y:2009:i:7243:d:10.1038_nature07861. 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.