Functional Characterization of the M36 Metalloprotease FgFly1 in .

Fungalysin metallopeptidase (M36), a hydrolase, catalyzes the hydrolysis of alanine, glycine, etc. Normally, it is considered to play an important role in the progress of fungal infection. However, the function of fungalysin metallopeptidase (M36) in has not been reported. In this study, we explored the biological functions of FgFly1, a fungalysin metallopeptidase (M36) of . We found that did not affect the ability to produce DON toxin, although it inhibited spore germination during asexual reproduction and reduction in pathogenicity compared with PH-1. Therefore, we speculated that FgFly1 affects the pathogenicity of by affecting pathways related to wheat disease resistance. Target protein TaCAMTA (calmodulin-binding transcription activator) was selected by a yeast two-hybrid (Y2H) system. Then, the interaction between FgFly1 and TaCAMTA was verified by bimolecular fluorescent complimentary (BiFC) and luciferase complementation assay (LCA). Furthermore, compared with wild-type , the morbidity level of was increased after infection with , and the expression level of was significantly reduced. Based on the above results, we concluded that FgFly1 regulated pathogenicity by interacting with host cell CAMTA protein.