AUTHOR=Yang Qianqian , Song Limin , Miao Zhengang , Su Meiling , Liang Wenxing , He Yawen 

TITLE=Acetylation of BcHpt Lysine 161 Regulates Botrytis cinerea Sensitivity to Fungicides, Multistress Adaptation and Virulence

JOURNAL=Frontiers in Microbiology

VOLUME=10

YEAR=2020

URL=https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2019.02965

DOI=10.3389/fmicb.2019.02965

ISSN=1664-302X

ABSTRACT=<p>BcHpt is a core element of the high-osmolarity glycerol (HOG) transduction pathway in <italic>Botrytis cinerea</italic>. 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 <italic>B. cinerea</italic>, BcHpt (Histidine-containing phosphotransfer) is essential but uncharacterized in <italic>B. cinerea</italic>. 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<sup>K161Q</sup>-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 <italic>B. cinerea</italic>. Constitutive acetylation of BcHpt Ly161 apparently inhibits hyphal growth, the multistress response, and sensitivity to fungicides in <italic>B. cinerea.</italic> Moreover, the lysine acetylation site affected phosphorylation of the MAPK BcSak1.</p>