Journal of General Microbiology · 1972 · 110 citations · 0 references
Life SciencesGeneticsMolecular GeneticsEnzymologyMicrobial GeneticsMicrobial MetabolismFungal BiochemistryFungal GeneticsFungal MetabolismNitrogen AssimilationNitrogen MetabolismProteolytic EnzymesAmmonium AssimilationEnzyme Expression In FungiExtracellular ProteasesFungal Nitrogen MetabolismMicrobial ProteasesNitrate Reductase ActivityNitrogen Source UtilizationProtease Production
Summary Extracellular protease of Aspergillus nidulans is repressible by ammonium. A mutant (xprDI) selected for derepression of protease in the presence of ammonium is also derepressed for nitrate reductase, xanthine dehydrogenase and glutamate uptake; it retains the ability to use ammonium as sole nitrogen source. The mutant is partially dominant in heterozygous diploids. The mutation does not confer methylamine resistance, nor are methylamine-resistant(meaA) strains derepressed for protease.