Formation of extracellular neutral proteinase and the stringent response in Bacillus subtilis.
The kinetics of extracellular neutral proteinase synthesis by an isogenic stringent (IS58) and a relaxed (IS56) strain of B. subtilis were compared. The specific enzyme formation rate by the stringent strain was higher than that of the relaxed one. Norvaline addition (1 mg/mL) induced the formation of pppGpp and ppGpp, respectively, as well as the appearance of extracellular neutral proteinase activities in cultures of the stringent strain IS58 and a strain with high proteinase production (ZF-178) only. These correlations support the suggestion that (p)ppGpp are involved in the regulation processes responsible for production of extracellular neutral proteinases by B. subtilis.
D001412:Bacillus subtilis / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D010450:Endopeptidases / Q000096:biosynthesis*; D006158:Guanosine Pentaphosphate / Q000096:biosynthesis; D006159:Guanosine Tetraphosphate / Q000096:biosynthesis; D006160:Guanosine Triphosphate / Q000378:metabolism; D015260:Neprilysin
D006159:Guanosine Tetraphosphate; D006158:Guanosine Pentaphosphate; D006160:Guanosine Triphosphate; D010450:Endopeptidases; D015260:Neprilysin