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Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif

Lookup NU author(s): Dr Olivier Binda

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Licence

This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

© 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.


Publication metadata

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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Funding

Funder referenceFunder name
105617/Z/14/ZWellcome Trust (closed comp)

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