Effect of nitrate on the level of superoxide dismutase in anaerobically grown Escherichia coli.

Miyake, Kohichiro

doi:10.2323/jgam.32.527

J. Gen. Appl. Microbiol.

1986

DOI: 10.2323/jgam.32.527

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Effect of nitrate on the level of superoxide dismutase in anaerobically grown Escherichia coli.

Kohichiro Miyake

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Cited by 18 publications

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“…The expression of sodA in E. coli is regulated by several environmental stimuli including oxygen (3,4), compounds capable of increasing the intracellular flux of 0° (5,6), iron chelators (7)(8)(9), anaerobic respiration using nitrate as an electron acceptor (10)(11)(12), and strong oxidants capable of positively changing the redox potential of the cells (13). These and other results led us (8,10) to propose that expression of sodA in E. coli is negatively regulated by an iron-containing trans-acting repressor protein.…”

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confidence: 99%

Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli.

Hassan

Sun

1992

Proc. Natl. Acad. Sci. U.S.A.

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Transcriptional regulation of the sodA gene, encoding the manganese superoxide dismutase (superoxide: superoxide oxidoreductase, EC 1.15.1.1) of Escherchia coli, was studied by monitoring expression of sodA-lacZ in different genetic backgrounds and under different growth conditions. Mutations in the fnr gene were found to affect aerobic and anaerobic expression of sodA-wacZ. Potential Fnr-binding sites were identified in the promoter region of sodA. Strains harboring simultaneous mutations in arcAiB and fur expressed sodA-lacZ under anaerobic growth conditions but were still inducible by iron chelators. However, in the triple mutants (fnr fur arcAiB) sodA-lacZ was fully expressed under anaerobiosis and was not further induced by the presence of 2,2'-dipyridyl, nitrate, or oxidants. On the other hand, aerobic expression of sodA-lacZ from a Fur-strain was -3.8-fold higher than that from the wild-type strain but was diminished by introducing mutations in fnr or arcAiB. In conclusion, Fnr, Arc, and Fur act as anaerobic repressors of sodA. Furthermore, the regulation of sodA by Fur (ferric uptake regulation protein), Arc (aerobic respiratory control), and Fnr (fumarate nitrate reduction/regulator of anaerobic respiration) is independent of the superoxide response regulon SoxRS.

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confidence: 99%

Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli.

Hassan

Sun

1992

Proc. Natl. Acad. Sci. U.S.A.

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“…Thus, sodA expression, as measured by MnSOD activity, occurs during respiratory growth when dioxygen, nitrate, trimethylamine-N-oxide, dimethyl sulfoxide, or ferricyanide is used as a terminal electron acceptor (31,37,45,47,51); it is noteworthy that during either aerobic or anaerobic respiration, MnSOD is induced on the addition of methyl viologen (pQ2+) to the culture (45). MnSOD activity also appears to depend on the nutritional status of the cell in a manner suggesting that involvement of the catabolite activation system (30).…”

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Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus

et al. 1990

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The ferric uptake regulation (fur) gene Mn2+-Fur had a significantly higher affinity for the promoter fragment of sodB compared with that of random DNA sequences but significantly lower than for the promoter fragment of sodA. These observations suggest that the apparent positive regulation of sodB does not result exclusively from a direct interaction of holo (metallated) Fur itself with the sodB promoter. Nevertheless, the sodB gene also appears to be part of the iron uptake regulon but not in the classical manner of Fe-dependent repression.

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“…The regulation of SodA biosynthesis in E. coli has been extensively studied both in vivo and in vitro (9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21). Thus, the enzyme is induced by: oxygen (5,10), redox-active compounds capable of generating superoxide radical in the presence of oxygen (11,12), ferrous iron chelators under aerobiosis or anaerobiosis (13,14), nitrate under anaerobiosis (9,15,16), and several strong oxidants capable of positively changing the redox potential of the cells (17).…”

mentioning

confidence: 99%

“…Thus, the enzyme is induced by: oxygen (5,10), redox-active compounds capable of generating superoxide radical in the presence of oxygen (11,12), ferrous iron chelators under aerobiosis or anaerobiosis (13,14), nitrate under anaerobiosis (9,15,16), and several strong oxidants capable of positively changing the redox potential of the cells (17). These findings led us to propose that the synthesis of SodA in E. coli is negatively regulated by an iron-containing trans-acting repressor protein (RPFe) (9,13).…”

mentioning

confidence: 99%

Use of site-directed mutagenesis to identify an upstream regulatory sequence of sodA gene of Escherichia coli K-12.

Naik

Hassan²

1990

Proc. Natl. Acad. Sci. U.S.A.

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Mn-containing superoxide dismutase (SodA; superoxide:superoxide oxidoreductase, EC 1.15.1.1) biosynthesis in Escherichia coli is regulated by several environmental stimuli. The DNA sequence of sodA shows the presence of a potential binding site for a regulatory protein(s) at the -35 region. To explore the possible role of this region in the regulation of sodA, we used oligonucleotide-directed sitespecific mutagenesis to change the sequence of nucleotides -48 through -44 from 5'-GGCAT-3' to 5'-TTACG-3'. We studied the effect ofthis altered sequence on the expression ofsodA. The data showed that the altered sequence resulted in the constitutive expression of the gene. Thus, E. coli harboring a plasmid containing the mutated sodA gene (pSNM6) were uninducible by paraquat in aerobiosis or by 2,2'-dipyridyl in aerobiosis or anaerobiosis. Furthermore, a multicopy plasmid containing the mutated sodA failed to titrate the repressor molecules present in an E. coli strain carrying the sodA-lacZ fusion. In contrast, multicopy plasmids containing the wild-type sodA gene were able to titrate the repressor protein and to cause the anaerobic induction of P-galactosidase in this sodA-acZ fusion strain. These results indicate that the region within and around the mutated sequence probably plays an important role in sod4 regulation and that the mutation disrupts a sequence that interacts with the repressor.

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Effect of nitrate on the level of superoxide dismutase in anaerobically grown Escherichia coli.

Cited by 18 publications

References 0 publications

Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli.

Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli.

Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus

Use of site-directed mutagenesis to identify an upstream regulatory sequence of sodA gene of Escherichia coli K-12.

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