title: Intracellular serine proteinase behaves as a heat-stress protein in nongrowing but as a cold-stress protein in growing populations of Bacillus megaterium.
abstract: A temperature increase from 35 degrees to 40-42 degrees C enhances the rise of cytoplasmic serine proteinase (ISP1) activity in Bacillus megaterium incubated in a sporulation medium. A temperature shift from 27 degrees C in the growth medium to 35 degrees C in the sporulation medium has the same effect. Elevated temperature stimulates the increase of ISP1 level when applied immediately after the transfer of cells from the growth to the sporulation medium (at T0) or at T3, when sporulation becomes irreversible. The cytoplasmic PMSF-resistant activity or the proteolytic activity associated with the membrane fraction is stimulated only slightly or not at all. A temperature increase to 45-47 degrees C suppresses the rise of proteolytic activities in all cell fractions. In addition to the elevation of the ISP1 activity by an upward temperature shift, the rise of this enzyme in nongrowing cells is also stimulated by osmotic stress. In growing populations, in contrast to the rise of the ISP1 activity caused by elevated temperature in nongrowing cells, this proteinase is induced by low temperatures (24-27 degrees C). The ISP1 activity roughly correlates with the enzyme protein concentration determined by immunoblotting.
authors.affiliation: Department of Molecular and Cell Microbiology, Institute of Microbiology, Czech Academy of Sciences, Prague.
authors.forename: H
authors.initials: H
authors.lastname: Kucerová
authors.forename: J
authors.initials: J
authors.lastname: Chaloupka
mesh_terms: D001410:Bacillus megaterium / Q000201:enzymology* / Q000502:physiology; D003080:Cold Temperature; D003470:Culture Media; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D012697:Serine Endopeptidases / Q000378:metabolism*; D013171:Spores, Bacterial
chemical_list: D003470:Culture Media; D006360:Heat-Shock Proteins; D012697:Serine Endopeptidases