IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v9y2018i1d10.1038_s41467-018-04836-y.html
   My bibliography  Save this article

Dual recognition of H3K4me3 and H3K27me3 by a plant histone reader SHL

Author

Listed:
  • Shuiming Qian

    (University of Wisconsin-Madison
    University of Wisconsin-Madison)

  • Xinchen Lv

    (Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Ray N. Scheid

    (University of Wisconsin-Madison
    University of Wisconsin-Madison)

  • Li Lu

    (University of Wisconsin-Madison
    University of Wisconsin-Madison)

  • Zhenlin Yang

    (Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Wei Chen

    (Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences)

  • Rui Liu

    (Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences)

  • Melissa D. Boersma

    (University of Wisconsin-Madison)

  • John M. Denu

    (University of Wisconsin-Madison
    University of Wisconsin-Madison
    Morgridge Institute for Research)

  • Xuehua Zhong

    (University of Wisconsin-Madison
    University of Wisconsin-Madison)

  • Jiamu Du

    (Shanghai Center for Plant Stress Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences)

Abstract

The ability of a cell to dynamically switch its chromatin between different functional states constitutes a key mechanism regulating gene expression. Histone mark “readers” display distinct binding specificity to different histone modifications and play critical roles in regulating chromatin states. Here, we show a plant-specific histone reader SHORT LIFE (SHL) capable of recognizing both H3K27me3 and H3K4me3 via its bromo-adjacent homology (BAH) and plant homeodomain (PHD) domains, respectively. Detailed biochemical and structural studies suggest a binding mechanism that is mutually exclusive for either H3K4me3 or H3K27me3. Furthermore, we show a genome-wide co-localization of SHL with H3K27me3 and H3K4me3, and that BAH-H3K27me3 and PHD-H3K4me3 interactions are important for SHL-mediated floral repression. Together, our study establishes BAH-PHD cassette as a dual histone methyl-lysine binding module that is distinct from others in recognizing both active and repressive histone marks.

Suggested Citation

  • Shuiming Qian & Xinchen Lv & Ray N. Scheid & Li Lu & Zhenlin Yang & Wei Chen & Rui Liu & Melissa D. Boersma & John M. Denu & Xuehua Zhong & Jiamu Du, 2018. "Dual recognition of H3K4me3 and H3K27me3 by a plant histone reader SHL," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04836-y
    DOI: 10.1038/s41467-018-04836-y
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-018-04836-y
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-018-04836-y?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
    ---><---

    Citations

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


    Cited by:

    1. Ming Wang & Zhenhui Zhong & Javier Gallego-Bartolomé & Suhua Feng & Yuan-Hsin Shih & Mukun Liu & Jessica Zhou & John Curtis Richey & Charmaine Ng & Yasaman Jami-Alahmadi & James Wohlschlegel & Keqiang, 2023. "Arabidopsis TRB proteins function in H3K4me3 demethylation by recruiting JMJ14," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Xiaozhen Zhao & Yiming Wang & Bingqin Yuan & Hanxi Zhao & Yujie Wang & Zheng Tan & Zhiyuan Wang & Huijun Wu & Gang Li & Wei Song & Ravi Gupta & Kenichi Tsuda & Zhonghua Ma & Xuewen Gao & Qin Gu, 2024. "Temporally-coordinated bivalent histone modifications of BCG1 enable fungal invasion and immune evasion," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    3. Mengting Xu & Qi Zhang & Huanbin Shi & Zhongling Wu & Wei Zhou & Fucheng Lin & Yanjun Kou & Zeng Tao, 2024. "A repressive H3K36me2 reader mediates Polycomb silencing," Nature Communications, Nature, vol. 15(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:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04836-y. 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.