Induction of superoxide dismutase in Escherichia coli by heat shock.
Exposure of midlogarithmic-phase cultures of Escherichia coli B to 48 degrees C for 1 hr elicited an induction of the manganese-containing superoxide dismutase (MnSOD), which became more pronounced during 1 hr of recovery at 37 degrees C. This induction required protein biosynthesis, since it was suppressed by chloramphenicol. Induction of MnSOD appeared to be a response to a heat-mediated increase in O2- production because it was dioxygen-dependent and because heating to 48 degrees C doubled the cyanide-resistant fraction of the total respiration.
D004790:Enzyme Induction; D004926:Escherichia coli / Q000201:enzymology* / Q000254:growth & development; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D013482:Superoxide Dismutase / Q000235:genetics*
D006360:Heat-Shock Proteins; D013482:Superoxide Dismutase