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Journal Article

Dynamic and flexible H3K9me3 bridging via HP1beta dimerization establishes a plastic state of condensed chromatin.

MPS-Authors
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Hiragami-Hamada,  K.
Research Group of Chromatin Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Sörös,  S.
Research Group of Chromatin Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Nikolov,  M.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Kreuz,  S.
Research Group of Chromatin Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Kost,  N.
Research Group of Chromatin Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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Pohl,  W.
Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society;

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Walla,  P. J.
Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Fischle,  W.
Research Group of Chromatin Biochemistry, MPI for Biophysical Chemistry, Max Planck Society;

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2281455.pdf
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2281455_Suppl_2.xlsx
(Supplementary material), 57KB

Citation

Hiragami-Hamada, K., Sörös, S., Nikolov, M., Wilkins, B., Kreuz, S., Chen, C., et al. (2016). Dynamic and flexible H3K9me3 bridging via HP1beta dimerization establishes a plastic state of condensed chromatin. Nature Communications, 7: 11310. doi:10.1038/ncomms11310.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-5348-B
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 HP1beta 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. HP1beta bridges condensed chromatin, which we postulate stabilizes the compacted state. In agreement, HP1beta 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.