Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif

Although central to regulating the access to genetic information, most lysine methyltransferases remain poorly characterised relative to other family of enzymes. Herein, I report new substrates for the lysine methyltransferase SETD6. Based on the SETD6-catalysed site on the histone variant H2AZ, I i...

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Detalles Bibliográficos
Autor principal: Binda, Olivier
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2019
Materias:
Brief Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6961689/
https://www.ncbi.nlm.nih.gov/pubmed/31370726
http://dx.doi.org/10.1080/15592294.2019.1649529
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author Binda, Olivier
author_facet Binda, Olivier
author_sort Binda, Olivier
collection PubMed
description Although central to regulating the access to genetic information, most lysine methyltransferases remain poorly characterised relative to other family of enzymes. Herein, I report new substrates for the lysine methyltransferase SETD6. Based on the SETD6-catalysed site on the histone variant H2AZ, I identified similar sequences in the canonical histones H2A, H3, and H4 that are modified by SETD6 in vitro, and putative non-histone substrates. I herein expend the repertoire of substrates for methylation by SETD6.
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spelling pubmed-69616892020-01-28 Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif Binda, Olivier Epigenetics Brief Report Although central to regulating the access to genetic information, most lysine methyltransferases remain poorly characterised relative to other family of enzymes. Herein, I report new substrates for the lysine methyltransferase SETD6. Based on the SETD6-catalysed site on the histone variant H2AZ, I identified similar sequences in the canonical histones H2A, H3, and H4 that are modified by SETD6 in vitro, and putative non-histone substrates. I herein expend the repertoire of substrates for methylation by SETD6. Taylor & Francis 2019-08-01 /pmc/articles/PMC6961689/ /pubmed/31370726 http://dx.doi.org/10.1080/15592294.2019.1649529 Text en © 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Brief Report
Binda, Olivier
Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif
title Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif
title_full Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif
title_fullStr Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif
title_full_unstemmed Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif
title_short Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif
title_sort lysine methyltransferase setd6 modifies histones on a glycine-lysine motif
topic Brief Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6961689/
https://www.ncbi.nlm.nih.gov/pubmed/31370726
http://dx.doi.org/10.1080/15592294.2019.1649529
work_keys_str_mv AT bindaolivier lysinemethyltransferasesetd6modifieshistonesonaglycinelysinemotif

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