1887

Abstract

Fur (ferric uptake regulator) is an iron-responsive transcriptional regulator in many bacterial species, and the mutant of ATCC 17616 exhibits pleiotropic phenotypes, such as an inability to efficiently use several carbon sources, as well as high sensitivity to hydrogen peroxide (HO), paraquat (a superoxide-producing compound) and nitric oxide (NO). To gain more insight into the pleiotropic role of the Fur protein of ATCC 17616, spontaneous suppressor mutants of the ATCC 17616 mutant that restored tolerance to NO were isolated and characterized in this study. The microarray-based comparative genomic analysis and subsequent sequencing analysis indicated that such suppressor mutants had a 2 bp deletion in the gene, whose orthologues encode HO-responsive transcriptional regulators in other bacterial species. The suppressor mutants and the reconstructed double-deletion mutant showed indistinguishable phenotypes in that they were all (i) more resistant than the mutant to HO, superoxide, NO and streptonigrin (an iron-activated antibiotic) and (ii) able to use carbon sources that cannot efficiently support the growth of the mutant. These results clearly indicate that the mutation suppressed the pleiotropic effect of the mutant. The double mutants were found to overexpress the KatG (catalase/peroxidase) and AhpC1 and AhpD (alkyl hydroperoxide reductase subunits C and D) proteins, and their enzymic activities to remove reactive oxygen and nitrogen species were suggested to be responsible for the suppression of phenotypes caused by the mutation.

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2012-05-01
2024-03-28
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