Toxoplasma gondii histone H4 is a core chromatin component whose post-translational modification state partitions the genome into active and silent domains (PMID:29101771, PMID:19120792). The MYST-family acetyltransferase TgMYST-A acetylates H4 in vitro preferentially at lysines 5, 8, 12, and 16 (PMID:16339723), and genome-wide, acetylated H4 (H4ac) marks the promoters of actively transcribed genes alongside H3K4me3 and H3K9ac (PMID:19120792). A distinct modification within the globular domain, H4K31, is bifunctionally regulated: H4K31 acetylation at promoters correlates with gene expression, whereas H4K31 monomethylation accumulates in the bodies of active genes yet inversely correlates with transcription (PMID:29101771). Silencing is imposed by methylation of H4K20: a Set8-related methyltransferase catalyzes mono-, di-, and trimethylation of H4K20 and is focally enriched at pericentric and telomeric heterochromatin (PMID:17562855), and H4K20me1 together with the histone variant H2A.X marks subtelomeric-like silenced heterochromatin (PMID:24417889). Global H4 acetylation levels are functionally coupled to the cell cycle, as HDAC inhibition raises nuclear H4 acetylation and impairs endodyogeny and daughter-cell budding (PMID:33360687). Beyond its chromatin role, recombinant TgH4 applied exogenously binds murine macrophages and modulates their inflammatory responses in vitro (PMID:29722109).