The JmjN domain as a dimerization interface and a targeted inhibitor of KDM4 demethylase activity.

ABSTRACT: Histone methylation is regulated to shape the epigenome by modulating DNA compaction, thus playing central roles in fundamental chromatin-based processes including transcriptional regulation, DNA repair and cell proliferation. Histone methylation is erased by demethylases including the well-established KDM4 subfamily members, however, little is known about their dimerization capacity and its impact on their demethylase activity. Using the powerful bimolecular fluorescence complementation technique, we herein show the in situ formation of human KDM4A and KDM4C homodimers and heterodimers in nuclei of live transfectant cells and evaluate their H3K9me3 demethylation activity. Using size exclusion HPLC as well as Western blot analysis, we show that endogenous KDM4C undergoes dimerizatio

SUBMITTER: Levin M 

PROVIDER: S-EPMC5908291 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature