title: pryB mutations as suppressors of arginine auxotrophy in Salmonella typhimurium.
abstract: Salmonella typhimurium strains which produce high constitutive levels of aspartate transcarbamoylase due to the pyrH700 mutation were found to grow more slowly in minimal medium than pyrH+ controls. The addition of arginine or citrulline but not ornithine restored normal growth rates. This requirement for arginine was completely suppressed by pyrB mutations and partially suppressed by pyrC and pyrD mutations. No suppression was observed with mutants at the pyrF locus. Introduction of leaky mutation argI2002 resulted in a more extreme arginine requirement and accentuated suppression by pyrB mutations. Suppression by the pyrC and pyrD mutations was reduced as a result of the incorporation of the leaky argI2002 allele. These results indicate that in pyrH700 strains carbamoyl phosphate is preferentially directed toward the formation of intermediates in the pyrimidine biosynthetic pathway. Arginine auxotrophy results from the reduced availability of carbamoyl phosphate for the biosynthesis of arginine. Suppression of this arginine dependence for growth is used as a convenient positive selection technique for pyrB mutations.
mesh_terms: D001120:Arginine / Q000494:pharmacology*; D001221:Aspartate Carbamoyltransferase / Q000235:genetics*; D002221:Carbamyl Phosphate / Q000378:metabolism; D002956:Citrulline / Q000494:pharmacology; D005796:Genes; D009154:Mutation; D009952:Ornithine / Q000494:pharmacology; D012486:Salmonella typhimurium / Q000235:genetics* / Q000378:metabolism; D013489:Suppression, Genetic
chemical_list: D002956:Citrulline; D002221:Carbamyl Phosphate; D001120:Arginine; D009952:Ornithine; D001221:Aspartate Carbamoyltransferase