ASPA — Fusarium graminearum PH-1

Summary

FgASPA (ASPA, SPN7, CDC11) on chromosome 4 of Fusarium graminearum PH-1 encodes a septin family protein with a G_SEPTIN domain and P-loop NTPase domain. The product exhibits GTP binding, lipid binding including phosphatidylinositol-5-phosphate binding, and acts as a structural constituent of the cytoskeleton. FgASPA is associated with septin ring assembly and disassembly, cytokinesis, contractile ring assembly, cell polarity maintenance, chitin localization, ER polarization, growth of unicellular organism as a thread of attached cells, chlamydospore formation, and adhesion of symbiont to host. The protein localizes to the septin cytoskeleton, cellular bud neck septin structure, hyphal septin ring, and mitotic and meiotic septin complexes. Associations with cell cycle progression, including G2/M phase transition and metaphase-anaphase transition, as well as with telomere length, chromosome segregation, and thermotolerance have been noted. Studies of related genes in other species link the family to reduced virulence and fusarium head blight.