A constitutive mutation in a posttranscriptional regulator gene for a phenoloxidase and proteases in Podospora anserina.
A recessive mutation in the gene mod-2 results in the synthesis at low temperatures of a phenoloxidase and an arrest of growth, reversible by beta-phenyl-pyruvic acid, a protease inhibitor. Phenoloxidase synthesis is 5-fluorouracil resistant and cycloheximade sensitive. Suppression of both cold sensitivity and phenoloxidase synthesis by common factors (higher NH4+ concentrations or mutations) suggests that the protease, suspected to be responsible for cold sensitivity, also arises from preexisting mRNA molecules. Instead of being recessive and constitutive, the mod-2 mutations is suppressive and dominant when cold sensitivity and phenoloxidases synthesis are induced as the consequence of the nonallelic gene interactions C/D, C/E, or R/V responsible for protoplasmic incompatibility. Combinations of nonallelic incompatibility systems and several mod-2 mutations lead us to hypothesize that the translational control of the above proteins depends on conformational relationships between incompatibility gene products and mod-2.
D000641:Ammonia / Q000494:pharmacology; D001203:Ascomycota / Q000201:enzymology*; D004156:Catechol Oxidase / Q000378:metabolism*; D003080:Cold Temperature; D003513:Cycloheximide / Q000494:pharmacology; D005467:Floxuridine / Q000494:pharmacology; D005799:Genes, Dominant; D005808:Genes, Recessive; D005809:Genes, Regulator; D005838:Genotype; D006899:Mixed Function Oxygenases / Q000096:biosynthesis; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D009154:Mutation; D010447:Peptide Hydrolases / Q000378:metabolism*; D010667:Phenylpyruvic Acids / Q000494:pharmacology; D014176:Protein Biosynthesis / Q000187:drug effects; D013489:Suppression, Genetic
D010667:Phenylpyruvic Acids; D005467:Floxuridine; D000641:Ammonia; D003513:Cycloheximide; D006899:Mixed Function Oxygenases; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase; D010447:Peptide Hydrolases