ISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.

ISWI is the catalytic subunit of several ATP-dependent chromatin remodelling factors that catalyse the sliding of nucleosomes along DNA and thereby endow chromatin with structural flexibility. Full activity of ISWI requires residues of a basic patch of amino acids in the N-terminal 'tail'...

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Autores principales:	Henrike Klinker, Felix Mueller-Planitz, Renliang Yang, Ignasi Forné, Chuan-Fa Liu, Lars Nordenskiöld, Peter B Becker
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5a3705fa6d1a4035903bf9dbaeda5073
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spelling	oai:doaj.org-article:5a3705fa6d1a4035903bf9dbaeda50732021-11-18T08:33:23ZISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.1932-620310.1371/journal.pone.0088411https://doaj.org/article/5a3705fa6d1a4035903bf9dbaeda50732014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24516652/?tool=EBIhttps://doaj.org/toc/1932-6203ISWI is the catalytic subunit of several ATP-dependent chromatin remodelling factors that catalyse the sliding of nucleosomes along DNA and thereby endow chromatin with structural flexibility. Full activity of ISWI requires residues of a basic patch of amino acids in the N-terminal 'tail' of histone H4. Previous studies employing oligopeptides and mononucleosomes suggested that acetylation of the H4 tail at lysine 16 (H4K16) within the basic patch may inhibit the activity of ISWI. On the other hand, the acetylation of H4K16 is known to decompact chromatin fibres. Conceivably, decompaction may enhance the accessibility of nucleosomal DNA and the H4 tail for ISWI interactions. Such an effect can only be evaluated at the level of nucleosome arrays. We probed the influence of H4K16 acetylation on the ATPase and nucleosome sliding activity of Drosophila ISWI in the context of defined, in vitro reconstituted chromatin fibres with physiological nucleosome spacing and linker histone content. Contrary to widespread expectations, the acetylation did not inhibit ISWI activity, but rather stimulated ISWI remodelling under certain conditions. Therefore, the effect of H4K16 acetylation on ISWI remodelling depends on the precise nature of the substrate.Henrike KlinkerFelix Mueller-PlanitzRenliang YangIgnasi FornéChuan-Fa LiuLars NordenskiöldPeter B BeckerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 2, p e88411 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Henrike Klinker Felix Mueller-Planitz Renliang Yang Ignasi Forné Chuan-Fa Liu Lars Nordenskiöld Peter B Becker ISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.
description	ISWI is the catalytic subunit of several ATP-dependent chromatin remodelling factors that catalyse the sliding of nucleosomes along DNA and thereby endow chromatin with structural flexibility. Full activity of ISWI requires residues of a basic patch of amino acids in the N-terminal 'tail' of histone H4. Previous studies employing oligopeptides and mononucleosomes suggested that acetylation of the H4 tail at lysine 16 (H4K16) within the basic patch may inhibit the activity of ISWI. On the other hand, the acetylation of H4K16 is known to decompact chromatin fibres. Conceivably, decompaction may enhance the accessibility of nucleosomal DNA and the H4 tail for ISWI interactions. Such an effect can only be evaluated at the level of nucleosome arrays. We probed the influence of H4K16 acetylation on the ATPase and nucleosome sliding activity of Drosophila ISWI in the context of defined, in vitro reconstituted chromatin fibres with physiological nucleosome spacing and linker histone content. Contrary to widespread expectations, the acetylation did not inhibit ISWI activity, but rather stimulated ISWI remodelling under certain conditions. Therefore, the effect of H4K16 acetylation on ISWI remodelling depends on the precise nature of the substrate.
format	article
author	Henrike Klinker Felix Mueller-Planitz Renliang Yang Ignasi Forné Chuan-Fa Liu Lars Nordenskiöld Peter B Becker
author_facet	Henrike Klinker Felix Mueller-Planitz Renliang Yang Ignasi Forné Chuan-Fa Liu Lars Nordenskiöld Peter B Becker
author_sort	Henrike Klinker
title	ISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.
title_short	ISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.
title_full	ISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.
title_fullStr	ISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.
title_full_unstemmed	ISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.
title_sort	iswi remodelling of physiological chromatin fibres acetylated at lysine 16 of histone h4.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/5a3705fa6d1a4035903bf9dbaeda5073
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ISWI remodelling of physiological chromatin fibres acetylated at lysine 16 of histone H4.

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