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 + BcHptK161Q-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.
Highlights
Mitogen-activated protein kinase (MAPK) signaling pathways play important roles in the response of fungal pathogens to various extracellular stresses, including osmotic and oxidative stress (Kruppa and Calderone, 2006)
The Lys161 acetylation site in BcHpt is conserved in 4 of the 11 fungal species analyzed
BcHpt is a core element of the high-osmolarity glycerol (HOG) pathway, which can be activated by various stresses, including oxidative and osmotic stresses, fungicides and hormones; the sensitivity of the mutants to these stresses was investigated
Summary
Mitogen-activated protein kinase (MAPK) signaling pathways play important roles in the response of fungal pathogens to various extracellular stresses, including osmotic and oxidative stress (Kruppa and Calderone, 2006). In S. cerevisiae, the HOG pathway contains two branches (Sln and Sho1), which converge on the MAPKK Pbs (Hohmann, 2002). Sln can sense extracellular osmotic conditions and transfer different signals to downstream MAPK by sequential phosphorylation (Posas et al, 1996; Krantz et al, 2006). The Sho branch consists of Sho, Cdc, Ste, Ste, Ste, and Pbs (Posas and Saito, 1997; O’Rourke and Herskowitz, 1998)
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