Abstract
Pyruvate dehydrogenase kinase (PDK) is a mitochondrial enzyme in a variety of eukaryotes, including the plant pathogen Fusarium graminearum. This enzyme can reduce the oxidation of glucose to acetyl-coA by phosphorylation and selectively inhibits the activity of pyruvate dehydrogenase (PDH), which is a kind of pyruvate dehydrogenase complex (PDC). In this study, we investigated the F. graminearum pyruvate dehydrogenase kinase encoded by FgPDK2, which is a homologue of Neurospora crassa PDK2. The disruption of the FgPDK2 gene led to several phenotypic defects including effects on mycelial growth, conidiation, pigmentation, and pathogenicity. The mutants also showed decreased resistance to osmotic stress and cell membrane/wall-damaging agents. The FgPDK2 deletion mutant exhibited reduced virulence. All of these defects were restored by genetic complementation of the mutant with the complete FgPDK2 gene. Overall, the results demonstrated that FgPDK2 is crucial for the growth of F. graminearum and can be exploited as a potential molecular target for novel fungicides to control Fusarium head blight caused by F. graminearum.Graphical abstract
Highlights
Fusarium head blight (FHB) caused by Fusarium species is an economically devastating disease of wheat and other small grain cereal crops around the world (Mcmullen et al 1997)
Statistical analysis At least three replicated measurements were used to calculate the mean standard deviation (SD) and data are Identification of the FgPDK2 gene in F. graminearum The full sequence of FgPDK2 gene (FGSG_07381.3) was obtained from the F. graminearum genome sequence which was deposited in the FungiDB Institute Database
It was found that FgPDK2 is important in the growth of F. graminearum
Summary
Fusarium head blight (FHB) caused by Fusarium species is an economically devastating disease of wheat and other small grain cereal crops around the world (Mcmullen et al 1997). Pyruvate dehydrogenase kinase (PDK) is a kind of mitochondrial enzyme that can reduce the oxidation of glucose to acetyl-coA by phosphorylation and selectively inhibits the activity of PDH. There are two PDHKs (Pkp1p and Pkp2p) in S. cerevisiae and deletion of them results in defects during growth in the presence of acetate and ethanol as carbon sources (Steensma et al 2008). This phenomenon indicates that the PDHKs in S. cerevisiae may cause a predicted aborted carbon utilization cycle (Steensmays 1996). The PDHK in A. nidulans, PkpC (AN6207) was shown to be important for the secretion of cellulose and cellulose in the process of growth (Ries et al 2018)
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