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Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms

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Author(s)

Helder Ferreira, Andrew Flaus, Tom Owen-Hughes

School/Research organisations

Abstract

Alteration of chromatin structure by chromatin modifying and remodelling activities is a key stage in the regulation of many nuclear processes. These activities are frequently interlinked, and many chromatin remodelling enzymes contain motifs that recognise modified histones. Here we adopt a peptide ligation strategy to generate specifically modified chromatin templates and used these to study the interaction of the Chd1, Isw2 and RSC remodelling complexes with differentially acetylated nucleosomes. Specific patterns of histone acetylation are found to alter the rate of chromatin remodelling in different ways. For example, histone H3 lysine 14 acetylation acts to increase recruitment of the RSC complex to nucleosomes. However, histone H4 tetra-acetylation alters the spectrum of remodelled products generated by increasing octamer transfer in trans. In contrast, histone H4 tetra-acetylation was also found to reduce the activity of the Chd1 and Isw2 remodelling enzymes by reducing catalytic turnover without affecting recruitment. These observations illustrate a range of different means by which modifications to histones can influence the action of remodelling enzymes. (c) 2007 Elsevier Ltd. All rights reserved.

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Details

Original languageEnglish
Pages (from-to)563-579
Number of pages17
JournalJournal of Molecular Biology
Volume374
Issue number3
DOIs
Publication statusPublished - 30 Nov 2007

    Research areas

  • histone, acetylation, Snf2, nucleosome, chromatin, NATIVE CHEMICAL LIGATION, YEAST PHO5 PROMOTER, RNA-POLYMERASE-II, SACCHAROMYCES-CEREVISIAE, NUCLEOSOMAL DNA, IN-VIVO, GENE-EXPRESSION, H3 ACETYLATION, H4 ACETYLATION, CHROMATIN

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