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

DOI: 10.1002/feb2.2018.592.issue-19 DOI Help

Authors: Louise Walport (University of Oxford) , Richard J. Hopkinson (University of Oxford) , Rasheduzzaman Chowdhury (University of Oxford) , Yijia Zhang (University of Oxford) , Joanna Bonnici (University of Oxford) , Rachel Schiller (University of Oxford) , Akane Kawamura (University of Oxford; The Wellcome Trust Centre for Human Genetics) , Christopher J. Schofield (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters , VOL 592 , PAGES 3264 - 3273

State: Published (Approved)
Published: October 2018
Diamond Proposal Number(s): 18069

Open Access Open Access

Abstract: 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.

Journal Keywords: 2‐oxoglutarate oxygenases; demethylases; epigenetics; histones; JmjC demethylases; lysine N‐methylation

Subject Areas: Medicine, Chemistry, Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Documents:
Walport_et_al-2018-FEBS_Letters.pdf

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