Fig. 8: Model for dynamic merge and separation of NuA4 and SWR1 complexes.

a Model for dynamic merge and separation of NuA4 and SWR1 complexes during reversible yeast–hypha transition of C. albicans. In yeast growth state, NuA4 and SWR1 merge together via the Eaf1–Yaf9 interaction. During hyphal development, NuA4–SWR1 is un-separated at the early stage, but separates into two distinct complexes during hyphal elongation. When hyphae convert to yeast, the two complexes remerge into one complex. The reversible acetylation and deacetylation of Eaf1 at K173 by the NuA4 core enzyme Esa1 and the histone deacetylase Hda1 control the merge and separation of NuA4 and SWR1, and this regulation is triggered by Brg1 recruitment of Hda1 to chromatin in response to nutritional signals that sustain hyphal elongation and hypha-gene expression. Red arrows represent acetylation is activated and green lines represent acetylation is inhibited. The expression of hypha-specific genes (HSGs) is activated in hyphae state, but repressed in yeast state. b Predicted orthologues of Eaf1, p400 and Swr1 in eukaryotes. Protein domains HSA, ATPase, and SANT form three different domain architectures, which occur in various combinations across eukaryotes. In fungi, each genome contains an Eaf1 ortholog and a Swr1 ortholog, but no p400-like proteins. In protista, Eaf1 and Swr1 orthologs are found in some genomes of protophyta or protozoa, p400-like proteins, as well in protozoa. The p400-like proteins are broadly found in higher eukaryotes of both animalia and plantae. In addition of a p400-like protein, a Swr1-like protein is found in genome of metazoa, and an Eaf1-like protein in plants. The orthologs of Eaf1, p400, and Swr1 are analyzed in each sequenced genome (http://blast.ncbi.nlm.nih.gov/Blast.cgi)