ePrints

The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation

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

Downloads

• Published version [.pdf]

Licence

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

Abstract

The demethylation of N^ε-methyllysine residues on histones by Jumonji-C lysine demethylases (JmjC-KDMs) has been established. A subset of JmjC-KDMs has also been reported to have N^ω-methylarginine residue demethylase (RDM) activity. Here, we describe biochemical screening studies, showing that the catalytic domains of all human KDM5s (KDM5A-KDM5D), KDM4E and, to a lesser extent, KDM4A/D, have both KDM and RDM activities with histone peptides. Ras GTPase-activating protein-binding protein 1 peptides were shown to be RDM substrates for KDM5C/D. No RDM activity was observed with KDM1A and the other JmjC-KDMs tested. The results highlight the potential of JmjC-KDMs to catalyse reactions other than N^ε-methyllysine demethylation. Although our study is limited to peptide fragments, the results should help guide biological studies investigating JmjC functions.

Publication metadata

Author(s): Bonnici J, Oueini R, Salah E, Johansson C, Schofield CJ, Kawamura A

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 2023

Volume: 597

Issue: 7

Pages: 933-946

Print publication date: 01/04/2023

Online publication date: 26/01/2023

Acceptance date: 28/12/2022

Date deposited: 01/03/2023

ISSN (print): 0014-5793

ISSN (electronic): 1873-3468

Publisher: John Wiley & Sons Ltd.

URL: https://doi.org/10.1002/1873-3468.14586

DOI: 10.1002/1873-3468.14586

PubMed id: 36700827

Altmetrics

Funding

Share