Post-translational modification directs nuclear and hyphal tip localization of Candida albicans mRNA-binding protein Slr1.

ABSTRACT: The morphological transition of the opportunistic fungal pathogen Candida albicans from budding to hyphal growth has been implicated in its ability to cause disease in animal models. Absence of SR-like RNA-binding protein Slr1 slows hyphal formation and decreases virulence in a systemic candidiasis model, suggesting a role for post-transcriptional regulation in these processes. SR (serine-arginine)-rich proteins influence multiple steps in mRNA metabolism and their localization and function are frequently controlled by modification. We now demonstrate that Slr1 binds to polyadenylated RNA and that its intracellular localization is modulated by phosphorylation and methylation. Wildtype Slr1-GFP is predominantly nuclear, but also co-fractionates with translating ribosomes. The non-phosphoryl

SUBMITTER: Ariyachet C 

PROVIDER: S-EPMC5405739 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature