论文信息：Functional Characterization of the M36 Metalloprotease FgFly1 in Fusarium graminearum . Xintong Wang, Miaomiao He, Huanhuan Liu, Huiyi Ding, Kouhan Liu, Ying Li, Peng Cheng, Qiang Li*, Baotong Wang*. Journal of Fungi, 2022, 8:726.
JCR分区Q1，中科院大类二区，IF: 5.724
论文摘要：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 Fusarium graminearum has not been reported. In this study, we explored the biological functions of FgFly1, a fungalysin metallopeptidase (M36) of F. graminearum . We found that DFgFly1 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 F. graminearum 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 Arabidopsis thaliana, the morbidity level of DAtCAMTA was increased after infection with F. graminearum , and the expression level of NPR1 was significantly reduced. Based on the above results, we concluded that FgFly1 regulated F. graminearum pathogenicity by interacting with host cell CAMTA protein.
原文链接：https://doi.org/10.3390/jof8070726
