Differences in the Regulation of the Intracellular Ca2+-Dependent Serine Proteinase Activity Between Bacillus subtilis and B. megaterium

Kučerová, Helena; Hlaváček, Otakar; Váchová, Libuče; Mlíchová, Štěpánka; Chaloupka, Jiří
March 2001
Current Microbiology;Mar2001, Vol. 42 Issue 3, p178
Academic Journal
A rise of the intracellular serine proteinase activity (ISP) during postexponential growth of Bacillus subtilis was decreased by a temperature upshift from 35° to 42°C. However, the amount of both molecular forms of the major intracellular serine proteinase ISP1 determined by immunoblotting was similar at both temperatures or even slightly increased at 42°C. The evolution of the ISP activity in B. megaterium showed an opposite temperature dependence, being faster during growth at 42°C. The amount of immunologically detected ISP1 again did not correlate well with the enzyme activity. Moreover, most of the ISP1 molecules in cell-free extracts from B. megaterium were inactive and were activated by increasing the CaCl2 concentration up to 30 mm—unlike B. subtilis, where the enzymic activity was unaffected by Ca2+ concentration. These data suggest that the ISP1 activity in the two bacillar species during postexponential growth is regulated posttranscriptionally, but that the regulatory mechanisms differ.


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