Protein degradation, meiosis and sporulation in proteinase-deficient mutants of Saccharomyces cerevisiae.
During the process of sporulation, a/alpha diploids degrade about 50% of their vegetative proteins. This degradation is not sporulation specific, for asporogenous diploids of a/a mating type degrade their vegetative proteins in a fashion similar to that of their a/alpha counterparts. Diploids lacking carboxypeptidase Y activity, prc1/prc1, show about 80% of wild-type levels of protein degradation, but are unimpaired in the production of normal asci. Diploids lacking proteinase B activity, prb1/prb1, show about 50% of wild-type levels of protein degradation. The effect on degradation of the proteinase B deficiency is epistatic to the degradation deficit attributable to the carboxypeptidase Y deficiency. The prb1 homozygotes undergo meiosis and produce spores, but the asci and, possibly, the spores are abnormal. Diploids homozygous for the pleiotropic pep4-3 mutation show only 30% of the wild-type levels of degradation when exposed to a sporulation regimen, and do not undergo meiosis or sporulation. Neither proteinase B nor carboxypeptidase Y is necessary for germination of spores. Approximately half of the colonies arising from a/a or alpha/alpha diploids exposed to the sporulation regimen that express an initially heterozygous drug-resistance marker (can1) appear to arise from mating-type switches followed by meiosis and sporulation.
D002268:Carboxypeptidases / Q000172:deficiency; D005656:Fungal Proteins / Q000378:metabolism*; D008540:Meiosis; D009154:Mutation; D010447:Peptide Hydrolases / Q000172:deficiency / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000502:physiology*; D013172:Spores, Fungal / Q000502:physiology
D005656:Fungal Proteins; D002268:Carboxypeptidases; D010447:Peptide Hydrolases