title: Control of the Production of orthophosphate repressible extracellular enzymes in Neurospora crassa.
abstract: The abilities of purine- and pyrimidine-requiring mutants to produce six orthophosphate repressible extracellular enzymes, alkaline phosphatase, 5'-nucleotidase, acid phosphatase, two nucleases and ribonuclease N1 were examined by culturing these mutants in low and high phosphate media containing nucleotide or nucleoside. All the purine requiring mutants produced significantly reduced amounts of alkaline phosphatase, 5'-nucleotidase, acid phosphatase, alkaline nuclease and acid nuclease ranging 0.5-4.2, 5.0-17.4, 25.0-100, 20.3-67.5 and 6.2-48.5%, respectively. Production of ribonuclease N1 was found to be rather stimulated (150-564%) in these mutants. Essentially the same results were obtained for pyrimidine requiring mutants. Among those mutants ad-2 and ad-9 showed relatively high enzyme producing activity. Especially the production of ribonuclease N1 in ad-2 and ad-9 ranged to 4.9- and 5.6-fold that in the wild type. Though nuc-1 mutant (A1) has no ability to produce all these six repressible enzymes, double mutants A1ad-2 and A1ad-9 produced a significant amount of ribonuclease N1 in low and high phosphate media and acid phosphatase in low phosphate media.
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000378:metabolism; D004794:Enzyme Repression; D005809:Genes, Regulator; D009154:Mutation; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000187:drug effects / Q000201:enzymology*; D009708:Nucleotidases / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011687:Purines / Q000378:metabolism; D011743:Pyrimidines / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism
chemical_list: D010710:Phosphates; D011687:Purines; D011743:Pyrimidines; D012260:Ribonucleases; D009708:Nucleotidases; D000469:Alkaline Phosphatase; D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases