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Histone H3, Histone H4, and Histone H2B are basic nuclear proteins fundamental to the organization of chromatin in eukaryotic cells. They interact with DNA to form the nucleosome, the repetitive structural unit of chromatin, which regulates DNA accessibility, gene expression, replication, and repair. Each histone can undergo extensive post-translational modifications (acetylation, methylation, etc.), which are central to the regulation of chromatin structure and are implicated in numerous diseases when misregulated. Histone H3 and H4 form a stable heterotetramer at the core of the nucleosome, flanked by two H2A-H2B heterodimers. All three are highly conserved across evolution and are critical for proper cellular function.
Most drugs act by altering the post-translational modification state of histones ("histone acetylation", "histone methylation", etc.), thus changing chromatin accessibility and gene expression. Some chaperone proteins help assemble/disassemble the nucleosome.
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