Chromatin-binding proteins regulate the effective solvent quality experienced by chromatin and impact global chromatin organization in the nucleus.

The Polycomb group protein SCML2 contributes to the assembly and gene silencing function of Polycomb Repressive Complex 1 (PRC1) and requires an RNA-binding region to reach chromatin targets.

CUT&RUN (Cleavage Under Targets & Release Using Nuclease) profiles antibody-targeted DNA-binding proteins in situ with high resolution and low background, providing a simple, robust and scalable alternative to chromatin immunoprecipitation.

RNA binding is a key input of an active chromatin complex and maintenance of stem cell fate.

In vivo single-molecule imaging demonstrates that Smc5/6 chromatin association depends on ATP hydrolysis and dsDNA binding, requires Nse6 and is modulated by Brc1 after DNA damage.

Transcription factor proteins play an important role in modulating base damage formation and excision repair at the binding sites in the genome.

The binding of transcription factors to mesoscale chromatin fibers leads to microdomains whose features are dependent on the linker DNA length, linker histone density, and tail acetylation levels.

In fusion-positive rhabdomyosarcoma, CHD4 positively regulates super-enhancer-mediated gene expression by allowing a chromatin architecture at these cis-regulatory regions, which is permissive to the binding of the transcription factor PAX3-FOXO1.

The PBAF chromatin-remodelling complex is essential for the proliferation of melanocytes and melanoma cells and is recruited to critical regulatory elements by physical and functional interactions with MITF, a transcription factor and master regulator of melanoma.

Heat shock induces relocalization of epigenetic modifiers to the nucleolus, which acts as a dedicated protein quality control center that is indispensable for recovery of epigenetic regulators and epigenetic modifications.