High impact information on EAF3

• Chromatin immunoprecipitation and biochemical experiments indicate that the chromodomain of Eaf3 recruits Rpd3C(S) to nucleosomes methylated by Set2 on histone H3 lysine 36, leading to deacetylation of transcribed regions [1].
• Set2 functioned upstream of Rpd3S and the Eaf3 methyl-histone binding chromodomain was important for recruitment of Rpd3S and for deacetylation within the STE11 ORF [2].
• Rco1 and Eaf3 were subunits specific to Rpd3S [2].
• Eaf3, a component of the NuA4 histone acetylase and Rpd3 histone deacetylase complexes, is important for the global pattern of histone acetylation in Saccharomyces cerevisiae [3].
• Lastly, Eaf3 inhibits internal initiation within mRNA coding regions in a manner similar to FACT and Spt6 [3].

Biological context of EAF3

• However, the Eaf3 chromodomain and H3-K36 methylation do not significantly affect acetylation at promoters, suggesting that Eaf3 has a distinct function, presumably in the NuA4 complex [3].
• Preferential deacetylation of coding regions requires the Eaf3 chromodomain and H3-K36 methylation by Set2 [3].
• Specifically, the loss of Eaf3 causes increases in H3 and H4 acetylation at coding sequences and decreases at promoters, such that histone acetylation levels become evenly distributed across the genome [4].
• Eaf3 does not affect the overall level of H4 acetylation, the recruitment of the NuA4 catalytic subunit Esa1 to target promoters, or the level of transcription of the genes analyzed for histone acetylation [4].

References