Effect of netropsin on the derepression of enzymes during growth and sporulation of Bacillus subtilis.
Netropsin, a polypeptide antibiotic which binds specifically to adenylate-thymidylate-rich regions of deoxyribonucleic acid, inhibitis sporulation at about stage II, but does not inhibit growth of Bacillys subtilis. An analysis of the sporulation-associated enzymes aconitase, alkaline phosphatase, and glucose dehydrogenase revealed that their rates of expression were not affected by the presence of the antibiotic. The derepression of histidase, a vegetatively induced enzyme was stimulated by netropsin. Oxygen utilization by the cells during sporulation was not effected nor was spore germination prevented by the drug. Netropsin, however, did prevent the formation of dipicolinic acid. These and earlier results suggest that netropsin may be affecting the transcription of only select sporulation genes that are particularly rich in adenylate-thymidylate base pairs.
D000154:Aconitate Hydratase / Q000378:metabolism*; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000469:Alkaline Phosphatase / Q000378:metabolism*; D001412:Bacillus subtilis / Q000201:enzymology / Q000502:physiology*; D004790:Enzyme Induction / Q000187:drug effects; D006146:Guanidines / Q000494:pharmacology*; D006638:Histidine Ammonia-Lyase / Q000096:biosynthesis; D006836:Hydro-Lyases / Q000378:metabolism*; D009429:Netropsin / Q000494:pharmacology*; D010101:Oxygen Consumption / Q000187:drug effects; D010848:Picolinic Acids / Q000378:metabolism; D013171:Spores, Bacterial
D006146:Guanidines; D010848:Picolinic Acids; D009429:Netropsin; D000429:Alcohol Oxidoreductases; D000469:Alkaline Phosphatase; D006836:Hydro-Lyases; D000154:Aconitate Hydratase; D006638:Histidine Ammonia-Lyase