Ontology highlight
ABSTRACT:
SUBMITTER: Walport LJ
PROVIDER: S-EPMC6220849 | biostudies-literature | 2018 Oct
REPOSITORIES: biostudies-literature
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]