title: Pleiotropic mutants of Aspergillus nidulans altered in carbon metabolism.
abstract: Mutants altered in carbon catabolite regulation have been isolated by selecting for mutants of the areA217 strain capable of using acetamide as the sole nitrogen source in the presence of sucrose. In addition to creA mutants described previously be Arst and Cove, strains with mutations in two new genes, creB and cre C, have been found. The creB and creC mutants grow poorly on some sole carbon sources and have low levels of some enzymes of carbon catabolism e.g. beta-galactosidase and D-quinate dehydrogenase. The creB and creC mutants are hypersensitive to fluoroacetate, fluoroacetamide and allyl alcohol in the presence of glucose or sucrose but not glycerol; and the enzymes, acetamidase and alcohol dehydrogenase, are less sensitive to carbon catabolite repression than the wild-type strain. Extracellular protease and alpha-glucosidase enzyme activities are elevated in creB and creC mutants, while L-proline and L-glutamate uptake capacities are lower in both the presence and absence of glucose. Interactions between creA, B and C mutations have been investigated in double mutants, and the dominance properties of creB and creC mutants determined. The results indicate that the creB and creC genes may have a regulatory role in the control of carbon catabolism.
mesh_terms: D000081:Acetamides / Q000378:metabolism; D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000581:Amidohydrolases / Q000378:metabolism; D001233:Aspergillus nidulans / Q000201:enzymology / Q000378:metabolism*; D002244:Carbon / Q000378:metabolism*; D005696:Galactosidases / Q000378:metabolism; D005809:Genes, Regulator; D005959:Glucosidases / Q000378:metabolism; D005969:Glutamate Dehydrogenase / Q000378:metabolism; D009154:Mutation; D013395:Sucrose / Q000378:metabolism
chemical_list: D000081:Acetamides; D013395:Sucrose; D002244:Carbon; D000429:Alcohol Oxidoreductases; D005969:Glutamate Dehydrogenase; D005696:Galactosidases; D005959:Glucosidases; D000581:Amidohydrolases