title: Heat shock and hydrogen peroxide responses of Escherichia coli are not changed by dinucleoside tetraphosphate hydrolase overproduction.
abstract: 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.
mesh_terms: 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*
chemical_list: 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)