The MYST Family Histone Acetyltransferase SasC Governs Diverse Biological Processes in .

The conserved MYST proteins form the largest family of histone acetyltransferases (HATs) that acetylate lysines within the N-terminal tails of histone, enabling active gene transcription. Here, we have investigated the biological and regulatory functions of the MYST family HAT SasC in the opportunistic human pathogenic fungus using a series of genetic, biochemical, pathogenic, and transcriptomic analyses. The deletion (Δ) of results in a drastically reduced colony growth, asexual development, spore germination, response to stresses, and the fungal virulence. Genome-wide expression analyses have revealed that the Δ mutant showed 2402 significant differentially expressed genes: 1147 upregulated and 1255 downregulated. The representative upregulated gene resulting from Δ is , predicted to encode a bZIP transcription factor, whereas the UV-endonuclease UVE-1 was significantly downregulated by Δ. Furthermore, our Western blot analyses suggest that SasC likely catalyzes the acetylation of H3K9, K3K14, and H3K29 in . . In conclusion, SasC is associated with diverse biological processes and can be a potential target for controlling pathogenic fungi.