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Chromatin, the complex of DNA and proteins within the nucleus, plays a central role in gene expression and cellular function. However, studying chromatin-bound proteins has been challenging due to their intricate interactions with DNA.

Nucleosome model

To address this, researchers at Shanghai Jiao Tong University and Heidelberg University developed an advanced chromatin isolation technique that preserves protein–DNA interactions. They then applied mass spectrometry and bioinformatics analysis to examine how signaling pathways alter the chromatin-bound proteome. They published their in Â鶹´«Ã½É«ÇéƬ & Cellular Proteomics.

The researchers found that different signaling cues, such as stress or growth factors, significantly alter chromatin composition by affecting transcription factors, chromatin remodelers and DNA repair proteins. These changes influence gene expression and cellular responses.

The findings emphasize how external signals regulate DNA-bound proteins, offering new insights into diseases driven by dysregulated signaling, such as cancer. This work opens new possibilities for developing therapies that target specific protein–DNA interactions.

This chromatin profiling technique offers a valuable tool for investigating gene regulation and has the potential to inform precision medicine strategies.