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- W2889508766 abstract "N-Methylation of lysyl residues is widely observed on histone proteins. Using isolated enzymes, we report mechanistic and structural studies on histone lysine demethylase (KDM)-catalysed demethylation of Nε -methylated lysine 26 on histone 1 isotype 4 (H1.4). The results reveal that methylated H1.4K26 is a substrate for all members of the KDM4 subfamily and that KDM4A-catalysed demethylation of H1.4K26me3 peptide is similarly efficient to that of H3K9me3. Crystallographic studies of an H1.4K26me3:KDM4A complex reveal a conserved binding geometry to that of H3K9me3. In the light of the high activity of the KDM4s on this mark, our results suggest JmjC KDM-catalysed demethylation of H1.4K26 may be as prevalent as demethylation on the H3 tail and warrants further investigation in cells." @default.
- W2889508766 created "2018-09-07" @default.
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- W2889508766 date "2018-09-14" @default.
- W2889508766 modified "2023-10-15" @default.
- W2889508766 title "Mechanistic and structural studies of <scp>KDM</scp> ‐catalysed demethylation of histone 1 isotype 4 at lysine 26" @default.
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- W2889508766 doi "https://doi.org/10.1002/1873-3468.13231" @default.
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