IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v466y2010i7303d10.1038_nature09139.html
   My bibliography  Save this article

Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b

Author

Listed:
  • Lei Zeng

    (Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA)

  • Qiang Zhang

    (Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA)

  • SiDe Li

    (Mount Sinai School of Medicine)

  • Alexander N. Plotnikov

    (Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA)

  • Martin J. Walsh

    (Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA
    Mount Sinai School of Medicine)

  • Ming-Ming Zhou

    (Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA)

Abstract

Reading histone acetylation Histone lysine acetylation or methylation helps to regulate chromatin functions during gene transcription. Histone acetylation marks are typically recognized by proteins containing bromodomains, but recently, an alternative mechanism of acetyl-lysine binding was recognized in the tandem plant homeodomain (PHD) finger of human DPF3b, a protein that functions in gene activation. The three-dimensional solution structures of DPF3b bound to a lysine 14-acetylated histone H3 peptide have now been determined, offering mechanistic insight into the way the protein recognizes acetylation marks.

Suggested Citation

  • Lei Zeng & Qiang Zhang & SiDe Li & Alexander N. Plotnikov & Martin J. Walsh & Ming-Ming Zhou, 2010. "Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b," Nature, Nature, vol. 466(7303), pages 258-262, July.
  • Handle: RePEc:nat:nature:v:466:y:2010:i:7303:d:10.1038_nature09139
    DOI: 10.1038/nature09139
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09139
    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/nature09139?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. Kwangbeom Hyun & Jihye Ahn & Hyoungmin Kim & Jihyun Kim & Yong-In Kim & Hee-Sung Park & Robert G. Roeder & J. Eugene Lee & Jaehoon Kim, 2024. "The BAF complex enhances transcription through interaction with H3K56ac in the histone globular domain," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Huanhuan Cui & Hongyang Yi & Hongyu Bao & Ying Tan & Chi Tian & Xinyao Shi & Diwen Gan & Bin Zhang & Weizheng Liang & Rui Chen & Qionghua Zhu & Liang Fang & Xin Gao & Hongda Huang & Ruijun Tian & Silk, 2022. "The SWI/SNF chromatin remodeling factor DPF3 regulates metastasis of ccRCC by modulating TGF-β signaling," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    3. Lunying Wu & Xiaohui Jing & Baolan Zhang & Shoujun Chen & Ran Xu & Penggen Duan & Danni Zou & Shengjian Huang & Tingbo Zhou & Chengcai An & Yuehua Luo & Yunhai Li, 2022. "A natural allele of OsMS1 responds to temperature changes and confers thermosensitive genic male sterility," Nature Communications, Nature, vol. 13(1), pages 1-15, 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:466:y:2010:i:7303:d:10.1038_nature09139. 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.