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PMID: 3038851 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Heat shock and hydrogen peroxide responses of Escherichia coli are not changed by dinucleoside tetraphosphate hydrolase overproduction.

Journal of bacteriology ·Vol. 169 ·No. 8 ·1987-08-00 ·Pages 3817-20

Plateau P, Fromant M, Blanquet S

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
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
Chemicals
Adenine Nucleotides Dinucleoside Phosphates Heat-Shock Proteins diadenosine tetraphosphate Hydrogen Peroxide Phosphoric Monoester Hydrolases Acid Anhydride Hydrolases bis(5'-nucleosyl)tetraphosphatase (asymmetrical)
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Plateau P
Fromant M
Blanquet S
References (24)
24 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.169.8.3817-3820.1987
Published
1987-08-00
Pages
3817-20
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC212472
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.169.8.3817-3820.1987 PMC Full Text View journal details
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