Regulate its cellular metabolic activities to adapt to nutrient unavailability

Previous studies have proved the generation of acetyl-CoA via fatty acid b-oxidation is a prerequisite for appressorium-mediated plant infection, as acetylCoA is the substrate to synthesize glucans and chitin, which are required for cell wall biosynthesis. Given the decreased amount of peroxisomes during appressorial development, we investigated whether the mutant defects in appressorial function and invasive growth could be rescued by external carbon source, which can supply acetyl-CoA and other intermediates via the glycolytic pathway and citric acid cycle independent of peroxisomal fatty acid b-oxidation. As expected, pathogenic defects of all the mutants were partially complemented in the presence of exogenous glucose. In order to explore the exact reason, we monitored the changes in appressorial structure and function in detail. As a hemibiotrophic pathogen, M. Abiraterone Acetate oryzae has to regulate its cellular metabolic activities to adapt to nutrient unavailability during the early infection stage. In yeast, the SNF1 signaling pathway plays a central role in regulating energy status by its involvement in carbon catabolite derepression, a mechanism to ensure the utilization of unfavorable carbon sources when glucose is deprived. Previous studies on SNF1 function in phytopathogenic fungi have uncovered its great influences on the expression of cell wall degrading enzymes and the utilization of alternative sugars, both of which are subject to carbon catabolite repression. However, the protein was reported not to preserve such regulatory role. Recently, trehalose-6-phosphate synthase was recognized as a glucose-6-phosphate sensor, which cooperates with its downstream inhibitors SB415286 Nmr1-3 to mediate CCR regulatory system in M. oryzae. Besides, the expression pattern of CWDEs was found to be disturbed in MoTPS1 disruption mutant. These reports suggest the components of metabolic regulatory systems have changed greatly in M. oryzae, likely not involving MoSnf1. This study set out to investigate how MoSnf1 acts as a virulence determinant and delve into the function of SNF1 pathway in M. oryzae.

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