Phosphorylation of H3.3 at Serine 31 acts as a switch of nucleosome dynamics for transcription.

ABSTRACT: The incorporation of histone variant H3.3 into the genome plays a critical role in regulating gene transcription, genomic stability, and mitosis progression. However, the precise mechanisms underlying the influence of H3.3 on nucleosome stability and dynamics remain poorly understood. In this study, we demonstrate that while the incorporation of H3.3 into nucleosomes does not significantly alter their stability, it enhances the maintenance of nucleosome integrity. Notably, H3.3 recruits the FACT complexes more efficiently than the canonical H3, counteracting FACT's destabilizing effect on nucleosomes. The binding of FACT to H3.3-nucleosome further stabilizes the nucleosome structure, which can be reversed by phosphorylation at Serine 31 (H3.3S31ph). Through genome-wide analyses, we show th

SUBMITTER: Ma J 

PROVIDER: S-EPMC12445699 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature