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ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression

Author

Listed:
  • Xiaobing Shi

    (Stanford University)

  • Tao Hong

    (Stanford University School of Medicine)

  • Kay L. Walter

    (Stanford University)

  • Mark Ewalt

    (Stanford University)

  • Eriko Michishita

    (Stanford University School of Medicine)

  • Tiffany Hung

    (Stanford University)

  • Dylan Carney

    (Stanford University)

  • Pedro Peña

    (University of Colorado Health Sciences Center)

  • Fei Lan

    (Harvard Medical School)

  • Mohan R. Kaadige

    (University of Utah)

  • Nicolas Lacoste

    (Laval University Cancer Research Center)

  • Christelle Cayrou

    (Laval University Cancer Research Center)

  • Foteini Davrazou

    (University of Colorado Health Sciences Center)

  • Anjanabha Saha

    (University of Utah)

  • Bradley R. Cairns

    (University of Utah)

  • Donald E. Ayer

    (University of Utah)

  • Tatiana G. Kutateladze

    (University of Colorado Health Sciences Center)

  • Yang Shi

    (Harvard Medical School)

  • Jacques Côté

    (Laval University Cancer Research Center)

  • Katrin F. Chua

    (Stanford University School of Medicine
    Geriatric Research, Education and Clinical Center, VA Palo Alto Health Care System)

  • Or Gozani

    (Stanford University)

Abstract

Histones decoded Four papers in this issue tackle the hot topic of chromatin remodelling, specifically, how methyl marks on chromatin are 'read' by the proteins that interact with them. Two report on BPTF (bromodomain and PHD domain transcription factor), a subunit of NURF, the nucleosome remodelling factor. It contains a domain known as a PHD finger, which is shown to bind to histone H3 trimethylated at lysine 4 (H3K4) and to maintain proper activity at developmentally critical HOX genes. The accompanying structural study of the complex explains how the site specificity for H3K4 is achieved. The two other papers reveal that the PHD domain of tumour suppressor ING2 also recognizes trimethylated H3K4, and link the histone mark to repression of transcription. The four papers together establish certain PHD finger domains as previously unrecognized chromatin-binding modules. In a News and Views piece, Peter B. Becker discusses what these papers tell us about the function of the chemical modifications of histone tails.

Suggested Citation

  • Xiaobing Shi & Tao Hong & Kay L. Walter & Mark Ewalt & Eriko Michishita & Tiffany Hung & Dylan Carney & Pedro Peña & Fei Lan & Mohan R. Kaadige & Nicolas Lacoste & Christelle Cayrou & Foteini Davrazou, 2006. "ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression," Nature, Nature, vol. 442(7098), pages 96-99, July.
    • Handle: RePEc:nat:nature:v:442:y:2006:i:7098:d:10.1038_nature04835
    DOI: 10.1038/nature04835
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    Cited by:

    1. Steffen Mueller & Gail Dennison & Shujun Liu, 2021. "An Assessment on Ethanol-Blended Gasoline/Diesel Fuels on Cancer Risk and Mortality," IJERPH, MDPI, vol. 18(13), pages 1-23, June.
    2. Dimitrios Spiliotopoulos & Andrea Spitaleri & Giovanna Musco, 2012. "Exploring PHD Fingers and H3K4me0 Interactions with Molecular Dynamics Simulations and Binding Free Energy Calculations: AIRE-PHD1, a Comparative Study," PLOS ONE, Public Library of Science, vol. 7(10), pages 1-13, October.
    3. Amy L. Hughes & Aleksander T. Szczurek & Jessica R. Kelley & Anna Lastuvkova & Anne H. Turberfield & Emilia Dimitrova & Neil P. Blackledge & Robert J. Klose, 2023. "A CpG island-encoded mechanism protects genes from premature transcription termination," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    4. Qi Yu & Xuanyunjing Gong & Yue Tong & Min Wang & Kai Duan & Xinyu Zhang & Feng Ge & Xilan Yu & Shanshan Li, 2022. "Phosphorylation of Jhd2 by the Ras-cAMP-PKA(Tpk2) pathway regulates histone modifications and autophagy," Nature Communications, Nature, vol. 13(1), pages 1-19, December.

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