Deciphering the molecular mechanisms of BPTF interactions with nucleosomes via molecular simulations.

ABSTRACT: Many transcription factors regulate DNA accessibility and gene expression by recognizing post-translational modifications on histone tails within nucleosomes. These interactions are often studied in vitro using short peptide mimics of histone tails, which may overlook conformational changes that occur in the full nucleosomal context. Here, we employ molecular dynamics simulations to investigate the binding dynamics of the plant homeodomain (PHD) finger and bromodomain of bromodomain PHD-finger transcription factor (BPTF), both in solution and bound to either a histone H3 peptide or a full nucleosome. Our results show that BPTF adopts distinct conformational states depending on its binding context, with nucleosome engagement inducing compaction of the multidomain structure. PHD-finger bindi

SUBMITTER: Hebert R 

PROVIDER: S-EPMC12414703 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature