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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-5348-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-C3A1-E
Genre: Journal Article

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Hiragami-Hamada, K.1, Author              
Sörös, S.1, Author              
Nikolov, M.2, Author              
Wilkins, B., Author
Kreuz, S.1, Author              
Chen, C., Author
De La Rosa-Velazquez, I. A., Author
Zenn, H. M., Author
Kost, N.1, Author              
Pohl, W.3, Author              
Chernev, A., Author
Schwarzer, D., Author
Jenuwein, T., Author
Lorincz, M., Author
Zimmermann, B., Author
Walla, P. J.3, Author              
Neumann, H., Author
Baubec, T., Author
Urlaub, H.2, Author              
Fischle, W.1, Author              
Affiliations:
1Research Group of Chromatin Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578604              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              
3Research Group of Biomolecular Spectroscopy and Single-Molecule Detection, MPI for biophysical chemistry, Max Planck Society, ou_578565              

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 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.

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Language(s): eng - English
 Dates: 2016-04-19
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms11310
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Title: Nature Communications
Source Genre: Journal
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Pages: 16 Volume / Issue: 7 Sequence Number: 11310 Start / End Page: - Identifier: -