Heat shock and hydrogen peroxide responses of Escherichia coli are not changed by dinucleoside tetraphosphate hydrolase overproduction.
In Escherichia coli strains overproducing dinucleoside tetraphosphate hydrolase, the accumulation of dinucleoside tetraphosphates (AppppN, with N = A, C, G, or U) during heat shock or H2O2 treatment was reduced about 10-fold as compared with a control strain. This accumulation neither modified the pattern of the proteins induced by a temperature shift or H2O2 nor reduced the protection against oxidative damage induced by moderate H2O2 levels.
D017766:Acid Anhydride Hydrolases; D000227:Adenine Nucleotides / Q000378:metabolism; D015226:Dinucleoside Phosphates; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*
D000227:Adenine Nucleotides; D015226:Dinucleoside Phosphates; D006360:Heat-Shock Proteins; C020733:diadenosine tetraphosphate; D006861:Hydrogen Peroxide; D010744:Phosphoric Monoester Hydrolases; D017766:Acid Anhydride Hydrolases; C020023:bis(5'-nucleosyl)tetraphosphatase (asymmetrical)