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Journal Article

Methylation of K9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1β with the nucleosome.

MPS-Authors
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Munari,  F.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Soeroes,  S.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Schomburg,  A.
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;

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

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Rezaei-Ghaleh,  N.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Stützer,  A.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Gelato,  K. A.
Research Group of Chromatin Biochemistry, 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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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Schwarzer,  D.
Research Group of Reaction Dynamics, 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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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

External Ressource
Fulltext (public)

1539277.pdf
(Publisher version), 3MB

Supplementary Material (public)

1539277_Supplement_1.pdf
(Supplementary material), 3MB

Citation

Munari, F., Soeroes, S., Zenn, H. M., Schomburg, A., Kost, N., Schröder, S., et al. (2012). Methylation of K9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1β with the nucleosome. Journal of Biological Chemistry, 287(40), 33756-33765. doi:10.1074/jbc.M112.390849.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000F-EBAF-E
Abstract
Binding of heterochromatin protein 1 (HP1) to the histone H3 lysine 9 trimethylation (H3K9me3) mark is a hallmark of establishment and maintenance of heterochromatin. Although genetic and cell biological aspects have been elucidated, the molecular details of HP1 binding to H3K9me3 nucleosomes are unknown. Using a combination of NMR spectroscopy and biophysical measurements on fully defined recombinant experimental systems, we demonstrate that H3K9me3 works as an on/off switch regulating distinct binding modes of hHP1β to the nucleosome. The methyl-mark determines a highly flexible and very dynamic interaction of the chromodomain of hHP1β with the H3-tail. There are no other constraints of interaction or additional multimerization interfaces. In contrast, in the absence of methylation, the hinge region and the N-terminal tail form weak nucleosome contacts mainly with DNA. In agreement with the high flexibility within the hHP1β-H3K9me3 nucleosome complex, the chromoshadow domain does not provide a direct binding interface. Our results report the first detailed structural analysis of a dynamic protein-nucleosome complex directed by a histone modification and provide a conceptual framework for understanding similar interactions in the context of chromatin.