BPTF Target Engagement by Acetylated H2A.Z Photoaffinity Probes.

ABSTRACT: Histone variant H2A.Z has been increasingly associated with cancer progression, including cancers characterized by the dysregulated function of the epigenetic reader protein BPTF (bromodomain and PHD finger containing transcription factor). Despite this association, a direct interaction between acetylated H2A.Z and BPTF has not been validated in a physiological context, given the weak bromodomain-histone tail affinity. Here, we developed photoaffinity acetylated histone probes based on differentially acetylated H2A.Z isoforms I and II with an N-terminal diazirine and a C-terminal biotin tag for covalently capturing and enriching BPTF and new interactors. Photo-crosslinking experiments followed by SDS-PAGE revealed that recombinant BPTF bromodomain (BPTF BD) directly interacts with both iso

SUBMITTER: Peterson KE 

PROVIDER: S-EPMC12504027 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature