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A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling

Author

Listed:
  • Joanna Wysocka

    (Laboratory of Chromatin Biology)

  • Tomek Swigut

    (Laboratory of Molecular Vertebrate Embryology)

  • Hua Xiao

    (National Cancer Institute, NIH)

  • Thomas A. Milne

    (Laboratory of Chromatin Biology)

  • So Yeon Kwon

    (University of Birmingham)

  • Joe Landry

    (National Cancer Institute, NIH)

  • Monika Kauer

    (Laboratory of Chromatin Biology)

  • Alan J. Tackett

    (The Rockefeller University)

  • Brian T. Chait

    (The Rockefeller University)

  • Paul Badenhorst

    (University of Birmingham)

  • Carl Wu

    (National Cancer Institute, NIH)

  • C. David Allis

    (Laboratory of Chromatin Biology)

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

  • Joanna Wysocka & Tomek Swigut & Hua Xiao & Thomas A. Milne & So Yeon Kwon & Joe Landry & Monika Kauer & Alan J. Tackett & Brian T. Chait & Paul Badenhorst & Carl Wu & C. David Allis, 2006. "A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling," Nature, Nature, vol. 442(7098), pages 86-90, July.
    • Handle: RePEc:nat:nature:v:442:y:2006:i:7098:d:10.1038_nature04815
    DOI: 10.1038/nature04815
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    Cited by:

    1. Yi Zhang & Guojia Xie & Ji-Eun Lee & Mohamad Zandian & Deepthi Sudarshan & Benjamin Estavoyer & Caroline Benz & Tiina Viita & Golareh Asgaritarghi & Catherine Lachance & Clémence Messmer & Leandro Sim, 2024. "ASXLs binding to the PHD2/3 fingers of MLL4 provides a mechanism for the recruitment of BAP1 to active enhancers," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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