The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation.
The demethylation of N<sup>ε</sup> -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<sup>ω</sup> -methylarginine residue demethylase (RDM) activity. Here, we describe bi...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
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Wiley
2023
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| _version_ | 1826310618702938112 |
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| author | Bonnici, J Oueini, R Salah, E Johansson, C Schofield, CJ Kawamura, A |
| author_facet | Bonnici, J Oueini, R Salah, E Johansson, C Schofield, CJ Kawamura, A |
| author_sort | Bonnici, J |
| collection | OXFORD |
| description | The demethylation of N<sup>ε</sup> -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<sup>ω</sup> -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<sup>ε</sup> -methyllysine demethylation. Although our study is limited to peptide fragments, the results should help guide biological studies investigating JmjC functions. |
| first_indexed | 2024-03-07T07:56:05Z |
| format | Journal article |
| id | oxford-uuid:7bca36e4-dea1-42ef-bb97-1adaba91145b |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T07:56:05Z |
| publishDate | 2023 |
| publisher | Wiley |
| record_format | dspace |
| spelling | oxford-uuid:7bca36e4-dea1-42ef-bb97-1adaba91145b2023-08-15T10:44:44ZThe catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation.Journal articlehttp://purl.org/coar/resource_type/c_545buuid:7bca36e4-dea1-42ef-bb97-1adaba91145bEnglishSymplectic ElementsWiley2023Bonnici, JOueini, RSalah, EJohansson, CSchofield, CJKawamura, AThe demethylation of N<sup>ε</sup> -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<sup>ω</sup> -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<sup>ε</sup> -methyllysine demethylation. Although our study is limited to peptide fragments, the results should help guide biological studies investigating JmjC functions. |
| spellingShingle | Bonnici, J Oueini, R Salah, E Johansson, C Schofield, CJ Kawamura, A The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation. |
| title | The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation. |
| title_full | The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation. |
| title_fullStr | The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation. |
| title_full_unstemmed | The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation. |
| title_short | The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation. |
| title_sort | catalytic domains of all human kdm5 jmjc demethylases catalyse n methyl arginine demethylation |
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