Histone chaperone exploits intrinsic disorder to switch acetylation specificity

Histone chaperones have been shown to control the activity and specificity of histone-modifying enzymes. Here the authors establish a structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4, finding that Vps75 promotes K9-acetylation by engaging th...

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Autores principales:	Nataliya Danilenko, Lukas Lercher, John Kirkpatrick, Frank Gabel, Luca Codutti, Teresa Carlomagno
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0b7982cadac74428b575ac9e21c9f021
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spelling	oai:doaj.org-article:0b7982cadac74428b575ac9e21c9f0212021-12-02T15:35:58ZHistone chaperone exploits intrinsic disorder to switch acetylation specificity10.1038/s41467-019-11410-72041-1723https://doaj.org/article/0b7982cadac74428b575ac9e21c9f0212019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11410-7https://doaj.org/toc/2041-1723Histone chaperones have been shown to control the activity and specificity of histone-modifying enzymes. Here the authors establish a structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4, finding that Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain.Nataliya DanilenkoLukas LercherJohn KirkpatrickFrank GabelLuca CoduttiTeresa CarlomagnoNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Nataliya Danilenko Lukas Lercher John Kirkpatrick Frank Gabel Luca Codutti Teresa Carlomagno Histone chaperone exploits intrinsic disorder to switch acetylation specificity
description	Histone chaperones have been shown to control the activity and specificity of histone-modifying enzymes. Here the authors establish a structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4, finding that Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain.
format	article
author	Nataliya Danilenko Lukas Lercher John Kirkpatrick Frank Gabel Luca Codutti Teresa Carlomagno
author_facet	Nataliya Danilenko Lukas Lercher John Kirkpatrick Frank Gabel Luca Codutti Teresa Carlomagno
author_sort	Nataliya Danilenko
title	Histone chaperone exploits intrinsic disorder to switch acetylation specificity
title_short	Histone chaperone exploits intrinsic disorder to switch acetylation specificity
title_full	Histone chaperone exploits intrinsic disorder to switch acetylation specificity
title_fullStr	Histone chaperone exploits intrinsic disorder to switch acetylation specificity
title_full_unstemmed	Histone chaperone exploits intrinsic disorder to switch acetylation specificity
title_sort	histone chaperone exploits intrinsic disorder to switch acetylation specificity
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/0b7982cadac74428b575ac9e21c9f021
work_keys_str_mv	AT nataliyadanilenko histonechaperoneexploitsintrinsicdisordertoswitchacetylationspecificity AT lukaslercher histonechaperoneexploitsintrinsicdisordertoswitchacetylationspecificity AT johnkirkpatrick histonechaperoneexploitsintrinsicdisordertoswitchacetylationspecificity AT frankgabel histonechaperoneexploitsintrinsicdisordertoswitchacetylationspecificity AT lucacodutti histonechaperoneexploitsintrinsicdisordertoswitchacetylationspecificity AT teresacarlomagno histonechaperoneexploitsintrinsicdisordertoswitchacetylationspecificity
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Histone chaperone exploits intrinsic disorder to switch acetylation specificity

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