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Lookup NU author(s): Professor Akane Kawamura
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2018 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. N-Methylation of lysyl residues is widely observed on histone proteins. Using isolated enzymes, we report mechanistic and structural studies on histone lysine demethylase (KDM)-catalysed demethylation of Nε-methylated lysine 26 on histone 1 isotype 4 (H1.4). The results reveal that methylated H1.4K26 is a substrate for all members of the KDM4 subfamily and that KDM4A-catalysed demethylation of H1.4K26me3 peptide is similarly efficient to that of H3K9me3. Crystallographic studies of an H1.4K26me3:KDM4A complex reveal a conserved binding geometry to that of H3K9me3. In the light of the high activity of the KDM4s on this mark, our results suggest JmjC KDM-catalysed demethylation of H1.4K26 may be as prevalent as demethylation on the H3 tail and warrants further investigation in cells.
Author(s): Walport LJ, Hopkinson RJ, Chowdhury R, Zhang Y, Bonnici J, Schiller R, Kawamura A, Schofield CJ
Publication type: Article
Publication status: Published
Journal: FEBS Letters
Print publication date: 01/10/2018
Online publication date: 14/09/2018
Acceptance date: 24/08/2018
Date deposited: 14/10/2019
ISSN (print): 0014-5793
ISSN (electronic): 1873-3468
PubMed id: 30156264
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