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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.
AuthorsP Plateau, M Fromant, S Blanquet
JournalJournal of bacteriology (J Bacteriol) Vol. 169 Issue 8 Pg. 3817-20 (Aug 1987) ISSN: 0021-9193 [Print] United States
PMID3038851 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Adenine Nucleotides
  • Dinucleoside Phosphates
  • Heat-Shock Proteins
  • diadenosine tetraphosphate
  • Hydrogen Peroxide
  • Phosphoric Monoester Hydrolases
  • Acid Anhydride Hydrolases
  • bis(5'-nucleosyl)tetraphosphatase (asymmetrical)
Topics
  • Acid Anhydride Hydrolases
  • Adenine Nucleotides (metabolism)
  • Dinucleoside Phosphates
  • Escherichia coli (enzymology, metabolism)
  • Heat-Shock Proteins (biosynthesis)
  • Hot Temperature
  • Hydrogen Peroxide (pharmacology)
  • Phosphoric Monoester Hydrolases (metabolism)

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