title: Tunicamycin-resistant mutants of Bacillus amyloliquefaciens are deficient in amylase, protease and penicillinase synthesis and have altered sensitivity to antibiotics and autolysis.
abstract: Mutants of Bacillus amyloliquefaciens resistant to at least 10 micrograms/ml of tunicamycin were isolated and shown to be pleiotropic. The mutants were more resistant to streptomycin, chloramphenicol, kanamycin and neomycin than was the parent strain but less resistant to penicillin G and tetracycline. They were more autolytic, presumably due to an altered cell wall. The mutants produced reduced levels of amylase, penicillinase and both metal and serine protease besides having an enhanced sporulation frequency and being more motile.
mesh_terms: D000681:Amylases / Q000096:biosynthesis*; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001407:Bacillus / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D001433:Bacteriolysis; D002701:Chloramphenicol / Q000494:pharmacology; D007612:Kanamycin / Q000494:pharmacology; D009154:Mutation; D009355:Neomycin / Q000494:pharmacology; D010400:Penicillin G / Q000494:pharmacology; D010403:Penicillin Resistance; D010405:Penicillinase / Q000096:biosynthesis*; D010447:Peptide Hydrolases / Q000096:biosynthesis*; D013171:Spores, Bacterial; D013307:Streptomycin / Q000494:pharmacology; D013752:Tetracycline / Q000494:pharmacology; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D014415:Tunicamycin; D007612:Kanamycin; D002701:Chloramphenicol; D000681:Amylases; D010447:Peptide Hydrolases; D010405:Penicillinase; D013752:Tetracycline; D009355:Neomycin; D010400:Penicillin G; D013307:Streptomycin