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

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, Dirk Schwarzer, Thomas Jenuwein, Matthew Lorincz, Bastian Zimmermann, Peter Jomo Walla, Heinz Neumann, Tuncay Baubec, Henning Urlaub and Wolfgang Fischle ()
Additional contact information
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
Miroslav Nikolov: Laboratory of Chromatin Biochemistry, 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
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
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
Wolfgang Fischle: Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry

Nature Communications, 2016, vol. 7, issue 1, 1-16

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms11310

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