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Mechanistic and structural studies of KDM-catalysed demethylation of histone 1 isotype 4 at lysine 26.


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 N? -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.

SUBMITTER: Walport LJ 

PROVIDER: S-EPMC6220849 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Mechanistic and structural studies of KDM-catalysed demethylation of histone 1 isotype 4 at lysine 26.

Walport Louise J LJ   Hopkinson Richard J RJ   Chowdhury Rasheduzzaman R   Zhang Yijia Y   Bonnici Joanna J   Schiller Rachel R   Kawamura Akane A   Schofield Christopher J CJ  

FEBS letters 20180914 19


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 N<sup>ε</sup> -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 a  ...[more]

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