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.
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Authors | P Plateau, M Fromant, S Blanquet |
Journal | Journal of bacteriology
(J Bacteriol)
Vol. 169
Issue 8
Pg. 3817-20
(Aug 1987)
ISSN: 0021-9193 [Print] United States |
PMID | 3038851
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Adenine Nucleotides
- Dinucleoside Phosphates
- Heat-Shock Proteins
- diadenosine tetraphosphate
- Hydrogen Peroxide
- Phosphoric Monoester Hydrolases
- Acid Anhydride Hydrolases
- bis(5'-nucleosyl)tetraphosphatase (asymmetrical)
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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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