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

Qianqian Yang; Limin Song; Zhengang Miao; Meiling Su; Wenxing Liang; Yawen He

doi:10.3389/fmicb.2019.02965

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

Front Microbiol. 2020 Jan 8:10:2965. doi: 10.3389/fmicb.2019.02965. eCollection 2019.

Authors

Qianqian Yang¹, Limin Song¹, Zhengang Miao¹, Meiling Su¹, Wenxing Liang^{1

2}, Yawen He³

Affiliations

¹ Key Lab of Integrated Crop Pest Management of Shandong, College of Plant Health and Medicine, Qingdao Agricultural University, Qingdao, China.
² Shandong Province Key Laboratory of Applied Mycology, Qingdao Agricultural University, Qingdao, China.
³ State Key Laboratory of Microbial Metabolism, Shanghai Jiao Tong University, Shanghai, China.

Abstract

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

Keywords: Botrytis cinerea; dicarboximides and demethylation inhibitor sensitivity; histidine phosphotransfer protein; lysine acetylation; osmotic and oxidative stress; virulence.