Investigating the N-terminal linker histone H1 subtypes as substrates for JmjC lysine demethylases.

ABSTRACT: Members of the Jumonji C (JmjC) subfamily of non-heme Fe(ii) and 2-oxoglutarate (2OG) dependent N ^ε-lysine demethylases have established roles in catalysing demethylation of N ^ε-methylated lysine residues in core histones; their roles in accepting linker H1 histones as substrates have been less well explored. We report studies on the H1 substrate specificity of human JmjC lysine demethylases (KDMs), specifically KDM3A-C, KDM4A, KDM4D, KDM4E, KDM5D, and KDM6B, for mono-, di- and trimethylated N ^ε-lysine residues in peptide fragments of the N-terminal tail of human linker histone H1 isoforms (H1.2, H1.3, H1.4 and H1.5). The KDM4s, but not the other tested JmjC KDMs, catalysed demethylation of tri- and dimethylated H1 peptide isoforms with

SUBMITTER: Turkmen VA 

PROVIDER: S-EPMC12363342 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature