| Author |
Sun, F; Cao, XQ; Yu, DZ; Hu, DQ; Yan, Z; Fan, YY; Wang, C; Wu, AB |
| Abstract |
Taking tenuazonic acid (TeA) synthetase 1 (TAS1) in Pyricularia oryzae as a reference, the homolog AaTAS1 was first anchored in Alternaria alternata via de novo sequencing. Subsequently, AaMFS1, as a major facilitator superfamily (MFS) protein-encoding gene in the adjacent upstream region, was followed with interest. As hypothesized, AaTAS1 is required for TeA biosynthesis, while AaMFS1 is an efflux pump for the transmembrane transport of TeA. Comparatively, the TeA yield of Delta AaTAS1 and Delta AaMFS1 dropped significantly compared with that of the wild-type strain. Specifically, the A domain of AaTAS1 catalyzed the start of TeA biosynthesis in vitro. Simultaneously, the pathogenicity of Delta AaTAS1 was also significantly decreased. Transcriptome analysis confirmed the abovementioned consistency between the TeA-producing phenotypes and related gene expression. Moreover, the proteins AaTAS1 and AaMFS1 were found present in the cytoplasm, plasma membrane, and intracellular membrane system, respectively, by fluorescence localization. Namely, AaTAS1 was responsible for the biosynthesis of TeA, and AaMFS1 was responsible for the efflux transport of TeA. Certainly, AaTAS1 indirectly regulated the expression of AaMFS1 through the level of synthetic TeA. Overall, data on the novel AaTAS1 and AaMFS1 genes mainly contribute to theoretical advances in mycotoxin biosynthesis and the pathogenicity of phytopathogens to agricultural foods. |
