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PMID: 10097071 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 96 ·No. 7 ·1999-03-30 ·Pages 3537-9

Liochev SI, Hausladen A, Fridovich I

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.

MeSH Terms
Drug Resistance, Neoplasm Enzyme Induction Escherichia coli/enzymology,genetics Escherichia coli Proteins Gene Expression Regulation, Bacterial/drug effects Gene Expression Regulation, Enzymologic/drug effects Mutagenesis NAD/metabolism Nitroreductases/biosynthesis,genetics Paraquat/pharmacology Regulon
Chemicals
Escherichia coli Proteins NAD NfsA protein, E coli Nitroreductases Paraquat
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Liochev S I
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Hausladen A
Fridovich I
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.96.7.3537
Published
1999-03-30
Pages
3537-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC22328
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.96.7.3537 PMC Full Text View journal details
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