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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Autores principales:	Francesca Munari, Nasrollah Rezaei-Ghaleh, Shengqi Xiang, Wolfgang Fischle, Markus Zweckstetter
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/94f925db5f664815a27736b73ce193fd
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spelling	oai:doaj.org-article:94f925db5f664815a27736b73ce193fd2021-11-18T07:50:04ZStructural plasticity in human heterochromatin protein 1β.1932-620310.1371/journal.pone.0060887https://doaj.org/article/94f925db5f664815a27736b73ce193fd2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23585859/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203As 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.Francesca MunariNasrollah Rezaei-GhalehShengqi XiangWolfgang FischleMarkus ZweckstetterPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 4, p e60887 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Francesca Munari Nasrollah Rezaei-Ghaleh Shengqi Xiang Wolfgang Fischle Markus Zweckstetter Structural plasticity in human heterochromatin protein 1β.
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.
format	article
author	Francesca Munari Nasrollah Rezaei-Ghaleh Shengqi Xiang Wolfgang Fischle Markus Zweckstetter
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)
publishDate	2013
url	https://doaj.org/article/94f925db5f664815a27736b73ce193fd
work_keys_str_mv	AT francescamunari structuralplasticityinhumanheterochromatinprotein1b AT nasrollahrezaeighaleh structuralplasticityinhumanheterochromatinprotein1b AT shengqixiang structuralplasticityinhumanheterochromatinprotein1b AT wolfgangfischle structuralplasticityinhumanheterochromatinprotein1b AT markuszweckstetter structuralplasticityinhumanheterochromatinprotein1b
_version_	1718422925664583680

Structural plasticity in human heterochromatin protein 1β.

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