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Mechanistic and structural studies of KDM-catalysed demethylation of histone 1 isotype 4 at lysine 26

Lookup NU author(s): Dr Joanna BonniciORCiD, Professor Akane KawamuraORCiD

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Abstract

© 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.

Publication metadata

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

Year: 2018

Volume: 592

Issue: 19

Pages: 3264-3273

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

Publisher: Wiley-Blackwell

URL: https://doi.org/10.1002/1873-3468.13231

DOI: 10.1002/1873-3468.13231

PubMed id: 30156264

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