Linker histone defines structure and self-association behaviour of the 177 bp human chromatosome

Abstract Linker histones play essential roles in the regulation and maintenance of the dynamic chromatin structure of higher eukaryotes. The influence of human histone H1.0 on the nucleosome structure and biophysical properties of the resulting chromatosome were investigated and compared with the 17...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Sai Wang, Vinod K. Vogirala, Aghil Soman, Nikolay V. Berezhnoy, Zhehui Barry Liu, Andrew S. W. Wong, Nikolay Korolev, Chun-Jen Su, Sara Sandin, Lars Nordenskiöld
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5d28fa7870a14582a5c7ed001b9fe0eb
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:5d28fa7870a14582a5c7ed001b9fe0eb
record_format	dspace
spelling	oai:doaj.org-article:5d28fa7870a14582a5c7ed001b9fe0eb2021-12-02T14:01:37ZLinker histone defines structure and self-association behaviour of the 177 bp human chromatosome10.1038/s41598-020-79654-82045-2322https://doaj.org/article/5d28fa7870a14582a5c7ed001b9fe0eb2021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-79654-8https://doaj.org/toc/2045-2322Abstract Linker histones play essential roles in the regulation and maintenance of the dynamic chromatin structure of higher eukaryotes. The influence of human histone H1.0 on the nucleosome structure and biophysical properties of the resulting chromatosome were investigated and compared with the 177-bp nucleosome using Cryo-EM and SAXS. The 4.5 Å Cryo-EM chromatosome structure showed that the linker histone binds at the nucleosome dyad interacting with both linker DNA arms but in a tilted manner leaning towards one of the linker sides. The chromatosome is laterally compacted and rigid in the dyad and linker DNA area, in comparison with the nucleosome where linker DNA region is more flexible and displays structural variability. In solution, the chromatosomes appear slightly larger than the nucleosomes, with the volume increase compared to the bound linker histone, according to solution SAXS measurements. SAXS X-ray diffraction characterisation of Mg-precipitated samples showed that the different shapes of the 177 chromatosome enabled the formation of a highly ordered lamello-columnar phase when precipitated by Mg2+, indicating the influence of linker histone on the nucleosome stacking. The biological significance of linker histone, therefore, may be affected by the change in the polyelectrolyte and DNA conformation properties of the chromatosomes, in comparison to nucleosomes.Sai WangVinod K. VogiralaAghil SomanNikolay V. BerezhnoyZhehui Barry LiuAndrew S. W. WongNikolay KorolevChun-Jen SuSara SandinLars NordenskiöldNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-16 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sai Wang Vinod K. Vogirala Aghil Soman Nikolay V. Berezhnoy Zhehui Barry Liu Andrew S. W. Wong Nikolay Korolev Chun-Jen Su Sara Sandin Lars Nordenskiöld Linker histone defines structure and self-association behaviour of the 177 bp human chromatosome
description	Abstract Linker histones play essential roles in the regulation and maintenance of the dynamic chromatin structure of higher eukaryotes. The influence of human histone H1.0 on the nucleosome structure and biophysical properties of the resulting chromatosome were investigated and compared with the 177-bp nucleosome using Cryo-EM and SAXS. The 4.5 Å Cryo-EM chromatosome structure showed that the linker histone binds at the nucleosome dyad interacting with both linker DNA arms but in a tilted manner leaning towards one of the linker sides. The chromatosome is laterally compacted and rigid in the dyad and linker DNA area, in comparison with the nucleosome where linker DNA region is more flexible and displays structural variability. In solution, the chromatosomes appear slightly larger than the nucleosomes, with the volume increase compared to the bound linker histone, according to solution SAXS measurements. SAXS X-ray diffraction characterisation of Mg-precipitated samples showed that the different shapes of the 177 chromatosome enabled the formation of a highly ordered lamello-columnar phase when precipitated by Mg2+, indicating the influence of linker histone on the nucleosome stacking. The biological significance of linker histone, therefore, may be affected by the change in the polyelectrolyte and DNA conformation properties of the chromatosomes, in comparison to nucleosomes.
format	article
author	Sai Wang Vinod K. Vogirala Aghil Soman Nikolay V. Berezhnoy Zhehui Barry Liu Andrew S. W. Wong Nikolay Korolev Chun-Jen Su Sara Sandin Lars Nordenskiöld
author_facet	Sai Wang Vinod K. Vogirala Aghil Soman Nikolay V. Berezhnoy Zhehui Barry Liu Andrew S. W. Wong Nikolay Korolev Chun-Jen Su Sara Sandin Lars Nordenskiöld
author_sort	Sai Wang
title	Linker histone defines structure and self-association behaviour of the 177 bp human chromatosome
title_short	Linker histone defines structure and self-association behaviour of the 177 bp human chromatosome
title_full	Linker histone defines structure and self-association behaviour of the 177 bp human chromatosome
title_fullStr	Linker histone defines structure and self-association behaviour of the 177 bp human chromatosome
title_full_unstemmed	Linker histone defines structure and self-association behaviour of the 177 bp human chromatosome
title_sort	linker histone defines structure and self-association behaviour of the 177 bp human chromatosome
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/5d28fa7870a14582a5c7ed001b9fe0eb
work_keys_str_mv	AT saiwang linkerhistonedefinesstructureandselfassociationbehaviourofthe177bphumanchromatosome AT vinodkvogirala linkerhistonedefinesstructureandselfassociationbehaviourofthe177bphumanchromatosome AT aghilsoman linkerhistonedefinesstructureandselfassociationbehaviourofthe177bphumanchromatosome AT nikolayvberezhnoy linkerhistonedefinesstructureandselfassociationbehaviourofthe177bphumanchromatosome AT zhehuibarryliu linkerhistonedefinesstructureandselfassociationbehaviourofthe177bphumanchromatosome AT andrewswwong linkerhistonedefinesstructureandselfassociationbehaviourofthe177bphumanchromatosome AT nikolaykorolev linkerhistonedefinesstructureandselfassociationbehaviourofthe177bphumanchromatosome AT chunjensu linkerhistonedefinesstructureandselfassociationbehaviourofthe177bphumanchromatosome AT sarasandin linkerhistonedefinesstructureandselfassociationbehaviourofthe177bphumanchromatosome AT larsnordenskiold linkerhistonedefinesstructureandselfassociationbehaviourofthe177bphumanchromatosome
_version_	1718392141609172992

Linker histone defines structure and self-association behaviour of the 177 bp human chromatosome

Ejemplares similares