Journal article : Letter
The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation.
- Abstract:
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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 prote...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 1.6MB, Terms of use)
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- Publisher copy:
- 10.1002/1873-3468.14586
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Funding
Bibliographic Details
- Publisher:
- Wiley
- Journal:
- FEBS Letters More from this journal
- Volume:
- 597
- Issue:
- 7
- Pages:
- 933-946
- Publication date:
- 2023-02-07
- Acceptance date:
- 2022-12-28
- DOI:
- EISSN:
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1873-3468
- ISSN:
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0014-5793
- Pmid:
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36700827
Item Description
- Language:
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English
- Keywords:
- Subtype:
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Letter
- Pubs id:
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1326806
- Local pid:
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pubs:1326806
- Deposit date:
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2023-05-19
Terms of use
- Copyright holder:
- Bonnici et al.
- Copyright date:
- 2023
- Rights statement:
- © 2023 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Notes:
- This research was funded in whole or in part by European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme (Grant agreement No. 679479) (to AK). For the purpose of Open Access, the author has applied a CC BY public copyright licence to any Author Accepted Manuscript (AAM) version arising from this submission.
- Licence:
- CC Attribution (CC BY)
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