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Dynamic and flexible H3K9me3 bridging via HP1β dimerization establishes a plastic state of condensed chromatin

Author

Listed:
  • Kyoko Hiragami-Hamada

    (Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry)

  • Szabolcs Soeroes

    (Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry
    Present address: Oxford Nanopore Technologies LTD, Oxford, UK.)

  • Miroslav Nikolov

    (Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry
    Bioanalytical Mass Spectrometry, Max Planck Institute for Biophysical Chemistry)

  • Bryan Wilkins

    (Applied Synthetic Biology, Institute for Microbiology and Genetics, Georg-August University Göttingen)

  • Sarah Kreuz

    (Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry)

  • Carol Chen

    (Life Sciences Institute, The University of British Columbia)

  • Inti A. De La Rosa-Velázquez

    (Max Planck Institute of Immunobiology and Epigenetics)

  • Hans Michael Zenn

    (Biaffin GmbH & Co KG)

  • Nils Kost

    (Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry)

  • Wiebke Pohl

    (Biomolecular Spectroscopy and Single-Molecule Detection, Max Planck Institute for Biophysical Chemistry)

  • Aleksandar Chernev

    (Bioanalytical Mass Spectrometry, Max Planck Institute for Biophysical Chemistry
    Bioanalytics, Institute for Clinical Chemistry, University Medical Center Göttingen)

  • Dirk Schwarzer

    (Interfaculty Institute of Biochemistry, University of Tübingen)

  • Thomas Jenuwein

    (Max Planck Institute of Immunobiology and Epigenetics)

  • Matthew Lorincz

    (Life Sciences Institute, The University of British Columbia)

  • Bastian Zimmermann

    (Biaffin GmbH & Co KG)

  • Peter Jomo Walla

    (Biomolecular Spectroscopy and Single-Molecule Detection, Max Planck Institute for Biophysical Chemistry
    Technische Universität Braunschweig)

  • Heinz Neumann

    (Applied Synthetic Biology, Institute for Microbiology and Genetics, Georg-August University Göttingen)

  • Tuncay Baubec

    (University of Zürich)

  • Henning Urlaub

    (Bioanalytical Mass Spectrometry, Max Planck Institute for Biophysical Chemistry
    Bioanalytics, Institute for Clinical Chemistry, University Medical Center Göttingen)

  • Wolfgang Fischle

    (Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry)

Abstract

Histone H3 trimethylation of lysine 9 (H3K9me3) and proteins of the heterochromatin protein 1 (HP1) family are hallmarks of heterochromatin, a state of compacted DNA essential for genome stability and long-term transcriptional silencing. The mechanisms by which H3K9me3 and HP1 contribute to chromatin condensation have been speculative and controversial. Here we demonstrate that human HP1β is a prototypic HP1 protein exemplifying most basal chromatin binding and effects. These are caused by dimeric and dynamic interaction with highly enriched H3K9me3 and are modulated by various electrostatic interfaces. HP1β bridges condensed chromatin, which we postulate stabilizes the compacted state. In agreement, HP1β genome-wide localization follows H3K9me3-enrichment and artificial bridging of chromatin fibres is sufficient for maintaining cellular heterochromatic conformation. Overall, our findings define a fundamental mechanism for chromatin higher order structural changes caused by HP1 proteins, which might contribute to the plastic nature of condensed chromatin.

Suggested Citation

  • Kyoko Hiragami-Hamada & Szabolcs Soeroes & Miroslav Nikolov & Bryan Wilkins & Sarah Kreuz & Carol Chen & Inti A. De La Rosa-Velázquez & Hans Michael Zenn & Nils Kost & Wiebke Pohl & Aleksandar Chernev, 2016. "Dynamic and flexible H3K9me3 bridging via HP1β dimerization establishes a plastic state of condensed chromatin," Nature Communications, Nature, vol. 7(1), pages 1-16, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11310
    DOI: 10.1038/ncomms11310
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