High impact information on RIM13

• Rim101p-dependent genes were also dependent on Rim13p, a protease required for Rim101p processing [1].
• Pretreatment of mice with cyclophosphamide increased susceptibility to wild-type C. albicans and partially rescued the attenuated phenotype of the genetically deficient rim13(-/-) fungal mutant [2].
• Full attenuation of the fungal rim13(-/-) mutant is the first direct demonstration of a hyphal morphogenesis-related gene as a specific virulence factor for C. albicans during corneal infection [2].
• METHODS: Scarified corneas of immunocompetent or cyclophosphamide-treated BALB/c mice were topically inoculated with one of three human isolates of C. albicans, a homozygous mutant of the pH-dependent filamentation gene rim13 or a mutant reference strain control [2].
• We suggest that Rim20p may serve as part of a scaffold that places Rim101p and Rim13p in close proximity [3].

Biological context of RIM13

• This phenotype is complemented by the wild-type CPL1 gene, and its protease activity is essential for complementation [4].

Associations of RIM13 with chemical compounds

• Abstract Saccharomyces cerevisiae has only one putative gene (designated CPL1) for a cysteine protease with a protease domain similar to that of calpain [4].

Regulatory relationships of RIM13

• Disruption of CPL1 also causes reduced sporulation efficiency and promotes the degradation of the transcription factor Rim101p, which is involved in the sporulation pathway and has been shown to accumulate in a C-terminally truncated, active form under alkaline conditions [4].

Other interactions of RIM13

• Candida albicans Rim13p, a protease required for Rim101p processing at acidic and alkaline pHs [5].
• Mutations in RIM13, RIM101 and MDS3 delay normal chlamydospore formation [6].

References