Structural plasticity in human heterochromatin protein 1β.

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...

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Main Authors: Francesca Munari, Nasrollah Rezaei-Ghaleh, Shengqi Xiang, Wolfgang Fischle, Markus Zweckstetter
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23585859/pdf/?tool=EBI
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spelling doaj-94f925db5f664815a27736b73ce193fd2021-03-03T23:29:25ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0184e6088710.1371/journal.pone.0060887Structural plasticity in human heterochromatin protein 1β.Francesca MunariNasrollah Rezaei-GhalehShengqi XiangWolfgang FischleMarkus ZweckstetterAs 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 HP1β (hHP1β) 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 hHP1β that prepares a binding-competent interface for the formation of the intermolecular β-sheet with methylated histone H3. The structural plasticity of hHP1β supports its ability to bind and connect a wide variety of binding partners in epigenetic processes.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23585859/pdf/?tool=EBI
collection DOAJ
language English
format Article
sources DOAJ
author Francesca Munari
Nasrollah Rezaei-Ghaleh
Shengqi Xiang
Wolfgang Fischle
Markus Zweckstetter
spellingShingle Francesca Munari
Nasrollah Rezaei-Ghaleh
Shengqi Xiang
Wolfgang Fischle
Markus Zweckstetter
Structural plasticity in human heterochromatin protein 1β.
PLoS ONE
author_facet Francesca Munari
Nasrollah Rezaei-Ghaleh
Shengqi Xiang
Wolfgang Fischle
Markus Zweckstetter
author_sort Francesca Munari
title Structural plasticity in human heterochromatin protein 1β.
title_short Structural plasticity in human heterochromatin protein 1β.
title_full Structural plasticity in human heterochromatin protein 1β.
title_fullStr Structural plasticity in human heterochromatin protein 1β.
title_full_unstemmed Structural plasticity in human heterochromatin protein 1β.
title_sort structural plasticity in human heterochromatin protein 1β.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2013-01-01
description 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 HP1β (hHP1β) 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 hHP1β that prepares a binding-competent interface for the formation of the intermolecular β-sheet with methylated histone H3. The structural plasticity of hHP1β supports its ability to bind and connect a wide variety of binding partners in epigenetic processes.
url https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23585859/pdf/?tool=EBI
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