PMID:10097071: Difference between revisions

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<span style = 'font-size: large'> '''Liochev, SI, Hausladen, A and Fridovich, I'''  (1999) Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli.''Proc. Natl. Acad. Sci. U.S.A.'' '''96''':3537-9</span>
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'''Liochev, SI, Hausladen, A and Fridovich, I'''  (1999) Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli. ''Proc. Natl. Acad. Sci. U.S.A.'' '''96''':3537-9
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!align=left  |Abstract
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Nitroreductase A catalyzes the divalent reduction of nitro compounds, quinones, and dyes by NADPH. In this paper, nitroreductase A is induced in Escherichia coli by exposure to paraquat in a manner that depends on the expression of soxR. Nitroreductase activity was only slightly induced by paraquat in a strain bearing a mutational defect in the gene encoding nitroreductase A, but it was approximately 3-fold induced in the parental strain. Nitroreductase A thus appears to be a member of the soxRS regulon and probably contributes to the defenses against oxidative stress by minimizing the redox cycling attendant upon the univalent reduction of nitro compounds, quinones, and dyes.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10097071 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC22328 PMC22328]


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|{{TableHeadingColor}} |'''Abstract''' || Nitroreductase A catalyzes the divalent reduction of nitro compounds, quinones, and dyes by NADPH. In this paper, nitroreductase A is induced in Escherichia coli by exposure to paraquat in a manner that depends on the expression of soxR. Nitroreductase activity was only slightly induced by paraquat in a strain bearing a mutational defect in the gene encoding nitroreductase A, but it was approximately 3-fold induced in the parental strain. Nitroreductase A thus appears to be a member of the soxRS regulon and probably contributes to the defenses against oxidative stress by minimizing the redox cycling attendant upon the univalent reduction of nitro compounds, quinones, and dyes.
!align=left  |Keywords
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Drug Resistance, Neoplasm; Enzyme Induction; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Gene Expression Regulation, Bacterial/drug effects; Gene Expression Regulation, Enzymologic/drug effects; Mutagenesis; NAD/metabolism; Nitroreductases/biosynthesis; Nitroreductases/genetics; Paraquat/pharmacology; Regulon
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10097071 PubMed]
 
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Latest revision as of 04:09, 15 September 2013

Citation

Liochev, SI, Hausladen, A and Fridovich, I (1999) Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 96:3537-9

Abstract

Nitroreductase A catalyzes the divalent reduction of nitro compounds, quinones, and dyes by NADPH. In this paper, nitroreductase A is induced in Escherichia coli by exposure to paraquat in a manner that depends on the expression of soxR. Nitroreductase activity was only slightly induced by paraquat in a strain bearing a mutational defect in the gene encoding nitroreductase A, but it was approximately 3-fold induced in the parental strain. Nitroreductase A thus appears to be a member of the soxRS regulon and probably contributes to the defenses against oxidative stress by minimizing the redox cycling attendant upon the univalent reduction of nitro compounds, quinones, and dyes.

Links

PubMed PMC22328

Keywords

Drug Resistance, Neoplasm; Enzyme Induction; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Gene Expression Regulation, Bacterial/drug effects; Gene Expression Regulation, Enzymologic/drug effects; Mutagenesis; NAD/metabolism; Nitroreductases/biosynthesis; Nitroreductases/genetics; Paraquat/pharmacology; Regulon

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