KDM2A integrates DNA and histone modification signals through a CXXC/PHD module and direct interaction with HP1.

ABSTRACT: Functional genomic elements are marked by characteristic DNA and histone modification signatures. How combinatorial chromatin modification states are recognized by epigenetic reader proteins and how this is linked to their biological function is largely unknown. Here we provide a detailed molecular analysis of chromatin recognition by the lysine demethylase KDM2A. Using biochemical approaches we identify a nucleosome interaction module within KDM2A consisting of a CXXC type zinc finger, a PHD domain and a newly identified Heterochromatin Protein 1 (HP1) interaction motif that mediates direct binding between KDM2A and HP1. This nucleosome interaction module enables KDM2A to decode nucleosomal H3K9me3 modification in addition to CpG methylation signals. The multivalent engagement with DNA an

SUBMITTER: Borgel J 

PROVIDER: S-EPMC5388433 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature