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  Structural plasticity in human heterochromatin protein 1 beta.

Munari, F., Rezaei-Ghaleh, N., Xiang, S. Q., Fischle, W., & Zweckstetter, M. (2013). Structural plasticity in human heterochromatin protein 1 beta. PLoS One, 8(4): e60887. doi:10.1371/journal.pone.0060887.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-78BE-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-4331-8
Genre: Journal Article

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 Creators:
Munari, F.1, Author              
Rezaei-Ghaleh, N.1, Author              
Xiang, S. Q.1, Author              
Fischle, W.2, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578604              

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 Abstract: As essential components of the molecular machine assembling heterochromatin in eukaryotes, HP1 (Heterochromatin Protein 1) proteins are key regulators of genome function. While several high-resolution structures of the two globular regions of HP1, chromo and chromoshadow domains, in their free form or in complex with recognition-motif peptides are available, less is known about the conformational behavior of the full-length protein. Here, we used NMR spectroscopy in combination with small angle X-ray scattering and dynamic light scattering to characterize the dynamic and structural properties of full-length human HP1 beta (hHP1 beta) in solution. We show that the hinge region is highly flexible and enables a largely unrestricted spatial search by the two globular domains for their binding partners. In addition, the binding pockets within the chromo and chromoshadow domains experience internal dynamics that can be useful for the versatile recognition of different binding partners. In particular, we provide evidence for the presence of a distinct structural propensity in free hHP1 beta that prepares a binding-competent interface for the formation of the intermolecular beta-sheet with methylated histone H3. The structural plasticity of hHP1 beta supports its ability to bind and connect a wide variety of binding partners in epigenetic processes.

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Language(s): eng - English
 Dates: 2013-04-09
 Publication Status: Published online
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1371/journal.pone.0060887
 Degree: -

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Title: PLoS One
Source Genre: Journal
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Pages: - Volume / Issue: 8 (4) Sequence Number: e60887 Start / End Page: - Identifier: -