MesA, a novel fungal protein required for the stabilization of polarity axes in Aspergillus nidulans.

ABSTRACT: The Aspergillus nidulans proteome possesses a single formin, SepA, which is required for actin ring formation at septation sites and also plays a role in polarized morphogenesis. Previous observations imply that complex regulatory mechanisms control the function of SepA and ensure its correct localization within hyphal tip cells. To characterize these mechanisms, we undertook a screen for mutations that enhance sepA defects. Of the mutants recovered, mesA1 causes the most dramatic defect in polarity establishment when SepA function is compromised. In a wild-type background, mesA1 mutants undergo aberrant hyphal morphogenesis, whereas septum formation remains unaffected. Molecular characterization revealed that MesA is a novel fungal protein that contains predicted transmembrane domains and

SUBMITTER: Pearson CL 

PROVIDER: S-EPMC491826 | biostudies-literature | 2004 Aug

REPOSITORIES: biostudies-literature