Site-specific ubiquitylation acts as a regulator of linker histone H1

While the role of specific posttranslational modifications (PTMs) is increasingly well understood for core histones, this is not the case for linker histone H1. Here the authors show that site-specific ubiquitylation of H1 results in distinct interactomes, regulates phase separation, and modulates a...

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Autores principales:	Eva Höllmüller, Simon Geigges, Marie L. Niedermeier, Kai-Michael Kammer, Simon M. Kienle, Daniel Rösner, Martin Scheffner, Andreas Marx, Florian Stengel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/17bd88aa7fda430bbade73ff65e2a471
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spelling	oai:doaj.org-article:17bd88aa7fda430bbade73ff65e2a4712021-12-02T17:34:34ZSite-specific ubiquitylation acts as a regulator of linker histone H110.1038/s41467-021-23636-52041-1723https://doaj.org/article/17bd88aa7fda430bbade73ff65e2a4712021-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23636-5https://doaj.org/toc/2041-1723While the role of specific posttranslational modifications (PTMs) is increasingly well understood for core histones, this is not the case for linker histone H1. Here the authors show that site-specific ubiquitylation of H1 results in distinct interactomes, regulates phase separation, and modulates assembly of chromatosomes.Eva HöllmüllerSimon GeiggesMarie L. NiedermeierKai-Michael KammerSimon M. KienleDaniel RösnerMartin ScheffnerAndreas MarxFlorian StengelNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Eva Höllmüller Simon Geigges Marie L. Niedermeier Kai-Michael Kammer Simon M. Kienle Daniel Rösner Martin Scheffner Andreas Marx Florian Stengel Site-specific ubiquitylation acts as a regulator of linker histone H1
description	While the role of specific posttranslational modifications (PTMs) is increasingly well understood for core histones, this is not the case for linker histone H1. Here the authors show that site-specific ubiquitylation of H1 results in distinct interactomes, regulates phase separation, and modulates assembly of chromatosomes.
format	article
author	Eva Höllmüller Simon Geigges Marie L. Niedermeier Kai-Michael Kammer Simon M. Kienle Daniel Rösner Martin Scheffner Andreas Marx Florian Stengel
author_facet	Eva Höllmüller Simon Geigges Marie L. Niedermeier Kai-Michael Kammer Simon M. Kienle Daniel Rösner Martin Scheffner Andreas Marx Florian Stengel
author_sort	Eva Höllmüller
title	Site-specific ubiquitylation acts as a regulator of linker histone H1
title_short	Site-specific ubiquitylation acts as a regulator of linker histone H1
title_full	Site-specific ubiquitylation acts as a regulator of linker histone H1
title_fullStr	Site-specific ubiquitylation acts as a regulator of linker histone H1
title_full_unstemmed	Site-specific ubiquitylation acts as a regulator of linker histone H1
title_sort	site-specific ubiquitylation acts as a regulator of linker histone h1
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/17bd88aa7fda430bbade73ff65e2a471
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Site-specific ubiquitylation acts as a regulator of linker histone H1

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