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Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases

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  • Louise J. Walport

    (Chemistry Research Laboratory, University of Oxford)

  • Richard J. Hopkinson

    (Chemistry Research Laboratory, University of Oxford)

  • Rasheduzzaman Chowdhury

    (Chemistry Research Laboratory, University of Oxford)

  • Rachel Schiller

    (Chemistry Research Laboratory, University of Oxford)

  • Wei Ge

    (Chemistry Research Laboratory, University of Oxford)

  • Akane Kawamura

    (Chemistry Research Laboratory, University of Oxford
    Wellcome Trust Centre for Human Genetics)

  • Christopher J. Schofield

    (Chemistry Research Laboratory, University of Oxford)

Abstract

While the oxygen-dependent reversal of lysine Nɛ-methylation is well established, the existence of bona fide Nω-methylarginine demethylases (RDMs) is controversial. Lysine demethylation, as catalysed by two families of lysine demethylases (the flavin-dependent KDM1 enzymes and the 2-oxoglutarate- and oxygen-dependent JmjC KDMs, respectively), proceeds via oxidation of the N-methyl group, resulting in the release of formaldehyde. Here we report detailed biochemical studies clearly demonstrating that, in purified form, a subset of JmjC KDMs can also act as RDMs, both on histone and non-histone fragments, resulting in formaldehyde release. RDM catalysis is studied using peptides of wild-type sequences known to be arginine-methylated and sequences in which the KDM’s methylated target lysine is substituted for a methylated arginine. Notably, the preferred sequence requirements for KDM and RDM activity vary even with the same JmjC enzymes. The demonstration of RDM activity by isolated JmjC enzymes will stimulate efforts to detect biologically relevant RDM activity.

Suggested Citation

  • Louise J. Walport & Richard J. Hopkinson & Rasheduzzaman Chowdhury & Rachel Schiller & Wei Ge & Akane Kawamura & Christopher J. Schofield, 2016. "Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases," Nature Communications, Nature, vol. 7(1), pages 1-12, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11974
    DOI: 10.1038/ncomms11974
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    Cited by:

    1. Lixiao Zhou & Xingsen Zhao & Jie Sun & Kun Zou & Xiaoli Huang & Liyang Yu & Mingxuan Wu & Yong Wang & Xuekun Li & Wen Yi, 2024. "Mina53 demethylates histone H4 arginine 3 asymmetric dimethylation to regulate neural stem/progenitor cell identity," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Jingyi Li & Tao Zhang & Tao Ren & Xiaoyu Liao & Yilong Hao & Je Sun Lim & Jong-Ho Lee & Mi Li & Jichun Shao & Rui Liu, 2022. "Oxygen-sensitive methylation of ULK1 is required for hypoxia-induced autophagy," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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