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

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Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms. / Ferreira, Helder; Flaus, Andrew; Owen-Hughes, Tom.

In: Journal of Molecular Biology, Vol. 374, No. 3, 30.11.2007, p. 563-579.

Research output: Contribution to journalArticlepeer-review

Harvard

Ferreira, H, Flaus, A & Owen-Hughes, T 2007, 'Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms', Journal of Molecular Biology, vol. 374, no. 3, pp. 563-579. https://doi.org/10.1016/j.jmb.2007.09.059

APA

Ferreira, H., Flaus, A., & Owen-Hughes, T. (2007). Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms. Journal of Molecular Biology, 374(3), 563-579. https://doi.org/10.1016/j.jmb.2007.09.059

Vancouver

Ferreira H, Flaus A, Owen-Hughes T. Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms. Journal of Molecular Biology. 2007 Nov 30;374(3):563-579. https://doi.org/10.1016/j.jmb.2007.09.059

Author

Ferreira, Helder ; Flaus, Andrew ; Owen-Hughes, Tom. / Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms. In: Journal of Molecular Biology. 2007 ; Vol. 374, No. 3. pp. 563-579.

Bibtex - Download

@article{5ef732e9d1a74f34beb0d630e36ffb86,
title = "Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms",
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.",
keywords = "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",
author = "Helder Ferreira and Andrew Flaus and Tom Owen-Hughes",
year = "2007",
month = nov,
day = "30",
doi = "10.1016/j.jmb.2007.09.059",
language = "English",
volume = "374",
pages = "563--579",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD",
number = "3",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms

AU - Ferreira, Helder

AU - Flaus, Andrew

AU - Owen-Hughes, Tom

PY - 2007/11/30

Y1 - 2007/11/30

N2 - 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.

AB - 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.

KW - histone

KW - acetylation

KW - Snf2

KW - nucleosome

KW - chromatin

KW - NATIVE CHEMICAL LIGATION

KW - YEAST PHO5 PROMOTER

KW - RNA-POLYMERASE-II

KW - SACCHAROMYCES-CEREVISIAE

KW - NUCLEOSOMAL DNA

KW - IN-VIVO

KW - GENE-EXPRESSION

KW - H3 ACETYLATION

KW - H4 ACETYLATION

KW - CHROMATIN

U2 - 10.1016/j.jmb.2007.09.059

DO - 10.1016/j.jmb.2007.09.059

M3 - Article

VL - 374

SP - 563

EP - 579

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -

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