Recognition of Histone H3 Methylation States by the PHD1 Domain of Histone Demethylase KDM5A.

ABSTRACT: PHD reader domains are chromatin binding modules often responsible for the recruitment of large protein complexes that contain histone modifying enzymes, chromatin remodelers, and DNA repair machinery. A majority of PHD domains recognize N-terminal residues of histone H3 and are sensitive to the methylation state of Lys4 in histone H3 (H3K4). Histone demethylase KDM5A, an epigenetic eraser enzyme that contains three PHD domains, is often overexpressed in various cancers, and its demethylation activity is allosterically enhanced when its PHD1 domain is bound to the H3 tail. The allosteric regulatory function of PHD1 expands roles of reader domains, suggesting unique features of this chromatin interacting module. Our previous studies determined the H3 binding site of PHD1, although it remain

SUBMITTER: Longbotham JE 

PROVIDER: S-EPMC8380758 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature