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• W4318166582 abstract "The demethylation of Nε -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 Nω -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 Nε -methyllysine demethylation. Although our study is limited to peptide fragments, the results should help guide biological studies investigating JmjC functions." @default.
• W4318166582 created "2023-01-27" @default.
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• W4318166582 date "2023-02-07" @default.
• W4318166582 modified "2023-10-14" @default.
• W4318166582 title "The catalytic domains of all human <scp>KDM5 JmjC</scp> demethylases catalyse <i>N</i>‐methyl arginine demethylation" @default.
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• W4318166582 doi "https://doi.org/10.1002/1873-3468.14586" @default.
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