Acetylation of BcHpt Lysine 161 Regulates Sensitivity to Fungicides, Multistress Adaptation and Virulence.

BcHpt is a core element of the high-osmolarity glycerol (HOG) transduction pathway in . In contrast to other elements of the pathway, which have been characterized and proven to play important roles in vegetative differentiation, fungicide resistance, the multistress response, and virulence in , BcHpt (Histidine-containing phosphotransfer) is essential but uncharacterized in . Our previous study reported the first lysine acetylation site (Lys161) in BcHpt. In this study, the functions of this lysine acetylation site in BcHpt were characterized using site-directed mutagenesis. To mimic Lys161 acetylation, we generated the mutant strain ΔBcHPt + BcHpt-GFP, which exhibited a slower growth rate; lower pathogenicity; higher sensitivity to multiple stresses, including osmotic and oxidative stresses, dicarboximides, and demethylation inhibitors (DMIs); and lower BcSak1 phosphorylation levels than wild-type . Constitutive acetylation of BcHpt Ly161 apparently inhibits hyphal growth, the multistress response, and sensitivity to fungicides in Moreover, the lysine acetylation site affected phosphorylation of the MAPK BcSak1.