Heat and osmotic stress enhance the development of cytoplasmic serine proteinase activity in sporulating Bacillus megaterium
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
8061621
Knihovny.cz E-resources
- MeSH
- Enzyme Activation MeSH
- Bacillus megaterium enzymology physiology MeSH
- Cytoplasm enzymology MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Immunoblotting MeSH
- Osmotic Pressure MeSH
- Heat-Shock Proteins biosynthesis metabolism MeSH
- Serine Endopeptidases biosynthesis metabolism MeSH
- Spores, Bacterial enzymology physiology MeSH
- Temperature MeSH
- Hot Temperature * MeSH
- Chromatography, High Pressure Liquid MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Heat-Shock Proteins MeSH
- Serine Endopeptidases MeSH
The intracellular Ca(2+)-dependent serine proteinase (ISP1) activity in the cytoplasm of nongrowing Bacillus megaterium incubated in a sporulation medium was determined at 35 degrees C and at temperatures decreasing the sporulation frequency (42 degrees C) or suppressing sporulation (43.5 degrees C). The enzyme in the crude cytoplasmic fraction was partially inhibited by a loosely bound inhibitor(s) because the ISP1 activity rose after protein fractionation by HPLC. Temperature shift-up or osmotic stress applied at 35 degrees C increased the development of the ISP1 activity several times. The increase was caused at least partially by the synthesis of the enzyme protein, as proved by SDS-PAGE and immunoblotting of the cytoplasm. This enzyme thus probably belongs among heat-shock proteins.
General and molecular microbiology and microbial genetics in the IM CAS
