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Journal of Bacteriology, April 2000, p. 1788-1793, Vol. 182, No. 7
Department of Pathology and Laboratory
Medicine, Emory University School of Medicine, Atlanta, Georgia 30322
Received 28 October 1999/Accepted 4 January 2000
The flavodoxins are flavin mononucleotide-containing electron
transferases. Flavodoxin I has been presumed to be the only flavodoxin
of Escherichia coli, and its gene, fldA, is
known to belong to the soxRS (superoxide response)
oxidative stress regulon. An insertion mutation of fldA was
constructed and was lethal under both aerobic and anaerobic conditions;
only cells that also had an intact (fldA+)
allele could carry it. A second flavodoxin, flavodoxin II, was postulated, based on the sequence of its gene, fldB. Unlike
the fldA mutant, an fldB insertion mutant is a
viable prototroph in the presence or absence of oxygen. A
high-copy-number fldB+ plasmid did not
complement the fldA mutation. Therefore, there must be a
vital function for which FldB cannot substitute for flavodoxin I. An
fldB-lacZ fusion was not induced by
H2O2 and is therefore not a member of the
oxyR regulon. However, it displayed a
soxS-dependent induction by paraquat (methyl viologen), and the fldB gene is preceded by two overlapping regions that
resemble known soxS binding sites. The fldB
insertion mutant did not have an increased sensitivity to the effects
of paraquat on either cellular viability or the expression of a
soxS-lacZ fusion. Therefore, fldB is a new
member of the soxRS (superoxide response) regulon, a group
of genes that is induced primarily by univalent oxidants and redox
cycling compounds. However, the reactions in which flavodoxin II
participates and its role during oxidative stress are unknown.
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Copyright © 2000, American Society for Microbiology. All rights reserved.
Flavodoxin Mutants of Escherichia
coli K-12
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Corresponding author. Mailing address: Glenn Memorial
Building, 69 Butler St., S.E., Atlanta, GA 30303. Phone: (404)
616-0602. Fax: (404) 616-7455. E-mail: bweiss2{at}emory.edu.
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