1887

Abstract

(Sacc.) Nirenberg (teleomorph Wineland) is one of the key pathogens of maize stalk rot disease. However, a clear understanding of stalk rot pathogenesis is still lacking. Previously, we identified the gene, which plays a key role in fungal virulence and sexual mating. The predicted Fsr1 protein contains multiple protein-binding domains, namely a caveolin-binding domain, a coiled-coil structure, and a calmodulin-binding motif at the N terminus and a WD40 repeat domain at the C terminus. Fsr1 shares significant similarity to a family of striatin proteins that play a critical role in cellular mechanisms that regulate a variety of developmental processes. Significantly, function is conserved in , where it also plays a direct role in pathogenesis. In this study, our goal was to determine the motif(s) in Fsr1 that are directly associated with fungal virulence. We complemented the knockout (Δ) strain with mutated versions of the gene, and determined that the Fsr1 C-terminal WD40 repeat domain is dispensable for vegetative growth and maize stalk rot virulence. We also examined the potential link between -mediated virulence and cell wall-degrading enzyme (-amylase, pectinase and cellulase) activities. Further characterization of the N-terminal region revealed that the coiled-coil structure is essential for virulence in . The coiled-coil domain is involved in a variety of protein–protein interactions in eukaryotic systems, and thus we hypothesize that the interaction between Fsr1 and the putative Fsr1-binding protein triggers downstream gene signalling that is associated with virulence.

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2008-06-01
2024-04-26
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