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Lookup NU author(s): Dr Olivier Binda
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2019, © 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.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.
Author(s): Binda O
Publication type: Article
Publication status: Published
Journal: Epigenetics
Year: 2020
Volume: 15
Issue: 1-2
Pages: 26-31
Online publication date: 01/08/2019
Acceptance date: 22/07/2019
Date deposited: 29/11/2019
ISSN (print): 1559-2294
ISSN (electronic): 1559-2308
Publisher: Taylor and Francis Inc.
URL: https://doi.org/10.1080/15592294.2019.1649529
DOI: 10.1080/15592294.2019.1649529
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