In Vitro Assays to Measure Histone Methyltransferase Activity Using Different Chromatin Substrates

Yannick Jacob; Philipp Voigt

doi:10.1007/978-1-4939-7318-7_20

In Vitro Assays to Measure Histone Methyltransferase Activity Using Different Chromatin Substrates

Yannick Jacob, Philipp Voigt

School of Biological Sciences

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

In vitro histone modification (HM) assays are used to characterize the activity of chromatin-modifying enzymes. These assays provide information regarding the modification sites on histones, the product specificity, and the impact of other histone or nucleotide modifications on enzyme activity. In particular, histone methyltransferase (HMT) assays have been instrumental in elucidating the activity and site specificity of many plant HMT enzymes. In this chapter, we describe a general protocol that can be used to perform HMT assays using different chromatin substrates, detection methods, and enzymes directly purified from plant material or heterologous sources.

Original language	English
Title of host publication	Plant Chromatin Dynamics
Editors	Marian Bemer, Célia Baroux
Publisher	HUMANA PRESS INC
Pages	345-360
Number of pages	16
Volume	1675
Edition	1st ed. 2018 edition
ISBN (Print)	1493973177, 9781493973170
DOIs	https://doi.org/10.1007/978-1-4939-7318-7_20
Publication status	Published - 20 Oct 2017

Publication series

Name	Methods in Molecular Biology
Publisher	Humana Press
Volume	1675
ISSN (Print)	1064-3745
ISSN (Electronic)	1940-6029

Keywords

Histone modifications
histone variants
histone lysine methylation
histone peptides
histone octamers
nucleosomes

Access to Document

10.1007/978-1-4939-7318-7_20

In vitro assays AAM Jacob_Voigt_Final_incl_figuresAccepted author manuscript, 396 KB

Roles of symmetric and asymmetric histone H3 lysine 27 trimethylation in gene repression and epigenetic inheritance
Voigt, P. & Finnegan, D.
UK-based charities
1/11/14 → 31/12/21
Project: Research
Core funding renewal for the Wellcome Trust Centre for Cell Biology
Tollervey, D. & Earnshaw, B.
UK-based charities
1/10/11 → 30/04/17
Project: Research

Philipp Voigt
Person

Cite this

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abstract = "In vitro histone modification (HM) assays are used to characterize the activity of chromatin-modifying enzymes. These assays provide information regarding the modification sites on histones, the product specificity, and the impact of other histone or nucleotide modifications on enzyme activity. In particular, histone methyltransferase (HMT) assays have been instrumental in elucidating the activity and site specificity of many plant HMT enzymes. In this chapter, we describe a general protocol that can be used to perform HMT assays using different chromatin substrates, detection methods, and enzymes directly purified from plant material or heterologous sources.",

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volume = "1675",

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In Vitro Assays to Measure Histone Methyltransferase Activity Using Different Chromatin Substrates. / Jacob, Yannick; Voigt, Philipp.

Plant Chromatin Dynamics. ed. / Marian Bemer; Célia Baroux. Vol. 1675 1st ed. 2018 edition. ed. HUMANA PRESS INC, 2017. p. 345-360 (Methods in Molecular Biology; Vol. 1675).

Research output: Chapter in Book/Report/Conference proceeding › Chapter

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AU - Voigt, Philipp

N1 - This has been created by Philipp Voigt - I have been told by David Tollervey that the publisher doesn't consider this as book chapter (I have the email from Wellcome and this has been indexed in Pub/Med as Journal - In Scopus this is considered a Book Chapter - Hence Methods and Protocols has been classed in PURE as Chapter in Book > Chapter contribution 02/04/2018 EN - I have requested the acceptance for publication email, grant reference numbers and Open Access option taken to Philipp 30/03/2018 EN

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KW - Histone modifications

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KW - histone octamers

KW - nucleosomes

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SN - 9781493973170

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A2 - Bemer, Marian

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PB - HUMANA PRESS INC

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In Vitro Assays to Measure Histone Methyltransferase Activity Using Different Chromatin Substrates

Abstract

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Keywords

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Projects

Roles of symmetric and asymmetric histone H3 lysine 27 trimethylation in gene repression and epigenetic inheritance

Core funding renewal for the Wellcome Trust Centre for Cell Biology

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Philipp Voigt

Cite this