Pleiotropic effect of a rifampin-resistant mutation in Bacillus subtilis.
Rifampin-resistant (Rifr) mutants were isolated spontaneously from Bacillus subtilis strain 168. A fraction of the mutants did not grow on a minimal medium. A high concentration of one of the L-amino acids (glutamic acid, glutamine, arginine, proline, aspartic acid, or asparagine) was required to restore their growth on the medium. Further analysis of one of the mutants (strain RF 161) suggested that the mutant is unable to use ammonia as a nitrogen source and requires amino acids instead. Activity of glutamate synthase was not detected in the crude extract of the mutant. The Rifr mutation was closely located to cysA and the drug resistance was cotransformed with the property of amino acid requirement at 100% frequency. All revertants to prototrophy tested showed the rifampin-sensitive (Rifs) property. The activity of the DNA-dependent RNA polymerase of the mutant was resistant to rifampin. It is concluded that some alteration of RNA polymerase may cause absence of the activity of an enzyme involved in the nitrogen metabolism.
D000596:Amino Acids / Q000378:metabolism; D000641:Ammonia / Q000378:metabolism; D001412:Bacillus subtilis / Q000187:drug effects / Q000235:genetics*; D002874:Chromosome Mapping; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D004352:Drug Resistance, Microbial; D005796:Genes; D005970:Glutamate Synthase / Q000378:metabolism; D009154:Mutation; D012293:Rifampin / Q000494:pharmacology*
D000596:Amino Acids; D000641:Ammonia; D005970:Glutamate Synthase; D012321:DNA-Directed RNA Polymerases; D012293:Rifampin