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The NuA3 histone acetyltransferase complex is a multi-subunit protein complex primarily studied in budding yeast (Saccharomyces cerevisiae). It functions as an enzyme that specifically acetylates lysine 14 on histone H3 (H3K14), an epigenetic modification crucial for regulating various biological processes, including gene transcription, cell cycle control, and DNA repair. The complex is composed of several subunits, such as the catalytic subunit Sas3 and the non-catalytic subunit Nto1, which cooperatively form a histone tail-binding cleft. NuA3's targeting and activity are influenced by its interactions with other histone modifications, including binding to H3K4me3 via its Yng1 subunit and H3K36me3 via its Pdp3 subunit. Furthermore, NuA3 antagonizes the activity of histone deacetylases like Rpd3S and Rpd3L, contributing to the dynamic regulation of histone acetylation and gene expression.
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