title: Neurospora crassa mutant impaired in glutamine regulation.
abstract: The final products of the catabolism of arginine that can be utilized as nitrogen sources by Neurospora crassa are ammonium, glutamic acid, and glutamine. Of these compounds, only glutamine represses arginase and glutamine synthetase. We report here the isolation and characterization of a mutant of N. crassa whose arginase, glutamine synthetase, and amino acid accumulations are resistant to glutamine repression (glnI). This mutant has a greater capacity than the wild type (glns) to accumulate most of the arginine and some of the glutamine in osmotically sensitive compartments while growing exponentially. Nonetheless, the major part of the glutamine remains soluble and metabolically available for repression. We propose that the lower repression of glutamine synthetase by glutamine in this mutant could be a necessary condition for sustaining the higher flow of nitrogen for the accumulation of amino acids observed in ammonium excess and that, if glutamine is the nitrogen signal that regulates the arginine accumulation of the vesicle, the glnr mutant has also escaped this control. Finally, in the glnr mutant, some glutamine resynthesis is necessary for arginine biosynthesis and accumulation.
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D001119:Arginase / Q000235:genetics; D004790:Enzyme Induction; D005970:Glutamate Synthase / Q000235:genetics; D005974:Glutamate-Ammonia Ligase / Q000235:genetics; D005973:Glutamine / Q000378:metabolism*; D007700:Kinetics; D009154:Mutation; D009491:Neurospora / Q000235:genetics*; D009492:Neurospora crassa / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D010641:Phenotype; D013045:Species Specificity
chemical_list: D000596:Amino Acids; D005973:Glutamine; D005970:Glutamate Synthase; D001119:Arginase; D005974:Glutamate-Ammonia Ligase