In response to infection, plants can induce the production of reactive oxygen species (ROS) to restrict pathogen invasion. In turn, adapted pathogens have evolved a counteracting mechanism of enzymatic ROS detoxification, but how it is activated remains elusive. Here, we show that in the tomato vascular wilt pathogen Fusarium oxysporum f. sp. lycopersici ( Fol ) this process is initiated by deacetylation of the FolSrpk1 kinase. Upon ROS exposure, Fol decreases FolSrpk1 acetylation on the K304 residue by altering the expression of the acetylation‐controlling enzymes. Deacetylated FolSrpk1 disassociates from the cytoplasmic FolAha1 protein, thus enabling its nuclear translocation. Increased accumulation of FolSrpk1 in the nucleus allows for hyperphosphorylation of its phosphorylation target FolSr1 that subsequently enhances transcription of different types of antioxidant enzymes. Secretion of these enzymes removes plant‐produced H 2 O 2 , and enables successful Fol invasion. Deacetylation of FolSrpk1 homologs has a similar function in Botrytis cinerea and likely other fungal pathogens. These findings reveal a conserved mechanism for initiation of ROS detoxification upon plant fungal infection.

Botrytis cinerea is one of the top 10 plant pathogens in the world, affecting 586 genera and more than 1000 species (Dean et al., 2012; Elad et al., 2016a). B. cinerea is a model aggressive necrotrophic plant pathogen that can not only infect leaves, stems, flowers, and other parts during plant growth, but also cause considerable losses in the postharvest stage (Elad et al., 2016b). With the long-term use of fungicides at high doses, B. cinerea has evolved multidrug resistance to a variety of fungicides, leading to weaker control effects of fungicides

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