Cryo-EM of nucleosome core particle interactions in trans

Abstract Nucleosomes, the basic unit of chromatin, are repetitively spaced along DNA and regulate genome expression and maintenance. The long linear chromatin molecule is extensively condensed to fit DNA inside the nucleus. How distant nucleosomes interact to build tertiary chromatin structure remai...

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Autores principales:	Silvija Bilokapic, Mike Strauss, Mario Halic
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f602bcecdea24fc09731f8793c1cc913
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spelling	oai:doaj.org-article:f602bcecdea24fc09731f8793c1cc9132021-12-02T12:32:21ZCryo-EM of nucleosome core particle interactions in trans10.1038/s41598-018-25429-12045-2322https://doaj.org/article/f602bcecdea24fc09731f8793c1cc9132018-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-25429-1https://doaj.org/toc/2045-2322Abstract Nucleosomes, the basic unit of chromatin, are repetitively spaced along DNA and regulate genome expression and maintenance. The long linear chromatin molecule is extensively condensed to fit DNA inside the nucleus. How distant nucleosomes interact to build tertiary chromatin structure remains elusive. In this study, we used cryo-EM to structurally characterize different states of long range nucleosome core particle (NCP) interactions. Our structures show that NCP pairs can adopt multiple conformations, but, commonly, two NCPs are oriented with the histone octamers facing each other. In this conformation, the dyad of both nucleosome core particles is facing the same direction, however, the NCPs are laterally shifted and tilted. The histone octamer surface and histone tails in trans NCP pairs remain accessible to regulatory proteins. The overall conformational flexibility of the NCP pair suggests that chromatin tertiary structure is dynamic and allows access of various chromatin modifying machineries to nucleosomes.Silvija BilokapicMike StraussMario HalicNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-8 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Silvija Bilokapic Mike Strauss Mario Halic Cryo-EM of nucleosome core particle interactions in trans
description	Abstract Nucleosomes, the basic unit of chromatin, are repetitively spaced along DNA and regulate genome expression and maintenance. The long linear chromatin molecule is extensively condensed to fit DNA inside the nucleus. How distant nucleosomes interact to build tertiary chromatin structure remains elusive. In this study, we used cryo-EM to structurally characterize different states of long range nucleosome core particle (NCP) interactions. Our structures show that NCP pairs can adopt multiple conformations, but, commonly, two NCPs are oriented with the histone octamers facing each other. In this conformation, the dyad of both nucleosome core particles is facing the same direction, however, the NCPs are laterally shifted and tilted. The histone octamer surface and histone tails in trans NCP pairs remain accessible to regulatory proteins. The overall conformational flexibility of the NCP pair suggests that chromatin tertiary structure is dynamic and allows access of various chromatin modifying machineries to nucleosomes.
format	article
author	Silvija Bilokapic Mike Strauss Mario Halic
author_facet	Silvija Bilokapic Mike Strauss Mario Halic
author_sort	Silvija Bilokapic
title	Cryo-EM of nucleosome core particle interactions in trans
title_short	Cryo-EM of nucleosome core particle interactions in trans
title_full	Cryo-EM of nucleosome core particle interactions in trans
title_fullStr	Cryo-EM of nucleosome core particle interactions in trans
title_full_unstemmed	Cryo-EM of nucleosome core particle interactions in trans
title_sort	cryo-em of nucleosome core particle interactions in trans
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/f602bcecdea24fc09731f8793c1cc913
work_keys_str_mv	AT silvijabilokapic cryoemofnucleosomecoreparticleinteractionsintrans AT mikestrauss cryoemofnucleosomecoreparticleinteractionsintrans AT mariohalic cryoemofnucleosomecoreparticleinteractionsintrans
_version_	1718394132324417536

Cryo-EM of nucleosome core particle interactions in trans

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