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Arsenite-resistance protein 2 (Ars2) is an important nuclear protein involved in various RNA metabolisms in animals and plants, but no Ars2 ortholog has been studied in filamentous fungi. Although it is an essential gene in most model eukaryotes,  FgARS2  null mutants were viable in the plant pathogenic fungus  Fusarium graminearum . The deletion of  FgARS2  resulted in pleiotropic defects in various fungal developmental processes.  Fgars2  mutants were irregular in nuclear division, and conidial germination was significantly retarded, causing the fungus to manifest its hypersensitive phenotypes under DNA damage stress. While  FgARS2  deletion caused abnormal morphologies of ascospores and defective ascospore discharge, our data revealed that  FgARS2  was not closely involved in small-non-coding RNA production in  F. graminearum . The dominant nuclear localization of  Fg Ars2-green fluorescent proteins (GFP) and abnormal nuclear division in  FgARS2  deletion mutant implicated that  Fg Ars2 functions in the nucleus. Intriguingly, we found that  Fg Ars2 established a robust physical interaction with the cap binding complex (CBC) to form a tertiary complex CBC-Ars2 (CBCA), and disruption of any CBCA complex subunit drastically attenuated the virulence of  F. graminearum . The results of the study indicate that Ars2 regulates fungal development, stress response, and pathogenesis via interaction with CBC in  F. graminearum  and provide a novel insight into understanding of the biological functions of Ars2 in filamentous fungi.

ARS2 Plays Diverse Roles in DNA Damage Response, Fungal Development, and Pathogenesis in the Plant Pathogenic Fungus Fusarium graminearum