The NuA4 histone acetyltransferase complex and the SWR1 chromatin remodeling complex are two distinct complexes and incorporate with each other to alter the chromatin structure in Saccharomyces cerevisiae.In higher eukaryotes,like human,these two complexes seem to merge together to form a large complex TIP60.In this study,we observed a dynamic interplay between NuA4 and SWR1 complexes during reversible morphological transition in Candida albicans.In yeast growth state,the two complexes merge together like TIP60 in human;in hyphal differentiation state,the two complexes separate each other;and during dedifferentiation from hyphae to yeast,the two separated complexes re-merge together.We proved that Yaf9 is a stable subunit of SWR1 complex and mediates the integration and separation of NuA4 and SWR1 complexes via interaction with Eaf1,a platform protein in the NuA4 complex.By in vivo and in vitro analyses,we verified that acetylation of Eaf1 at Lysine 173 but not Lysine 489 regulates its association with Yaf9,and Yaf9 recognizes acetylated Eaf1 through its YEATS domain.The acetylation and de-acetylation of Eaf1 is regulated in an Esa1-and Hda1-dependent manner.Our biochemical and morphological data demonstrates that separation of NuA4 from SWR1 is necessary for hyphal development.On the other hand,integration of NuA4 and SWR1 promotes hyphae dedifferentiation as well as yeast cell proliferation.The dynamic association and dissociation of NuA4 and SWR1 provide an evidence to support the evolution of two chromatin modifying complexes NuA4 and SWR1 into a large merger TIP60 from yeast to human and add a new layer of regulation in cell fate control in eukaryotes.