Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/104784
Title: ISWI remodelling of physiological chromatin fibres acetylated at Lysine 16 of Histone H4
Authors: Klinker, Henrike
Mueller-Planitz, Felix
Nordenskiöld, Lars
Yang, Renliang
Forné, Ignasi
Liu, Chuan-Fa
Becker, Peter B.
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2014
Source: Klinker, H., Mueller-Planitz, F., Yang, R., Forné, I., Liu, C.-F., Nordenskiöld, L., et al. (2014). ISWI Remodelling of Physiological Chromatin Fibres Acetylated at Lysine 16 of Histone H4. PLoS ONE, 9(2), e88411-.
Series/Report no.: PLoS ONE
Abstract: 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.
URI: https://hdl.handle.net/10356/104784
http://hdl.handle.net/10220/20283
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0088411
Rights: © 2014 Klinker et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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