Proteins driving liquid-liquid phase separation and histone modifications cooperatively associate with chromatin looping and transcriptional regulation.

ABSTRACT:

Background

Although liquid-liquid phase separation (LLPS) proteins are known to participate in genome organization and transcriptional regulation through the formation of biomolecular condensates, their functional interplay with other regulatory proteins and histone modifications in chromatin loop formation remains poorly characterized. By combining Hi-C chromatin interaction data with ChIP-seq profiles of 12, 27, and 24 LLPS proteins in GM12878, K562, and HepG2 cell lines, respectively, we identified chromatin loops associated with LLPS proteins and systematically analysed patterns of cooperative protein binding and histone modification enrichment within these loop-associated peaks.

Results

We identified 162, 313, and 431 chromatin loops associated with LLPS proteins in GM1

SUBMITTER: Ji X 

PROVIDER: S-EPMC12512537 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature