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sodA  -  superoxide dismutase

Escherichia coli UTI89

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Disease relevance of sodA

  • Escherichia coli double mutants (sodA sodB) completely lacking superoxide dismutase (SOD) have greatly enhanced mutation rates during aerobic growth [1].
  • A SOD mimic protected the sodA sodB strain against the toxicity of erythrose as did the carbonyl-blocking reagents hydrazine and aminoguanidine [2].
  • The gene sodA, encoding manganese-containing SOD ([Mn]-SOD), has been cloned from a virulent strain of Haemophilus influenzae type b using degenerate oligonucleotides encoding regions of the gene conserved across different bacterial species [3].
  • The S. typhimurium sodA mutant was not significantly attenuated in mice, however, which suggests that resistance to early oxygen-dependent microbicidal mechanisms in vivo may play only a minor role in Salmonella pathogenesis [4].
  • One detectable cytoplasmic SOD was identified in the human mucosal pathogen Moraxella catarrhalis, and the gene responsible for the SOD activity, sodA, was isolated from a recent pediatric clinical isolate (strain 7169) [5].

Psychiatry related information on sodA

  • The concentrations of immunoreactive Mn SOD and Cu/Zn SOD in the cerebral cortex were not different among the patients with Alzheimer's disease, and the age matched and young patients without neurological disorders [6].

High impact information on sodA


Chemical compound and disease context of sodA


Biological context of sodA

  • However, the enhanced mutagenesis in aerobically grown sodA sodB mutants is largely dependent on functional exonuclease III, suggesting that the increased flux of superoxide radicals results in DNA lesions that can be acted on by this enzyme, leading to mutations [1].
  • Fusion of a 120-base pair fragment, containing 90 base pairs of DNA upstream of the sodA transcription initiation site, to a promoterless galactokinase gene (galK) conferred redox-sensitivity to GalK synthesis [9].
  • Erythrose inhibited the growth of a sodA sodB strain of Escherichia coli under aerobiosis; but did not inhibit anaerobic growth of the sodA sodB strain, or the aerobic growth of the superoxide dismutase (SOD)-competent parental strain [2].
  • Growth of bacteria under iron-limiting conditions, inactivation of the Fur repressor, or expression of sodA from a plasmid resulted in increased resistance to early killing by J774 cells, which was abolished in the sodA mutant [4].
  • The important role of sodA for the pathogenicity of Y. enterocolitica could also be due to detoxification of endogenous, metabolically produced oxygen radicals which are encountered by extracellular enteric pathogens during the invasion of the host [13].

Anatomical context of sodA

  • In contrast, inactivation of sodA had only minor effects on survival and multiplication in the gut and Peyer's patches, as could be demonstrated in the orogastric infection model [13].
  • A S. typhimurium sodA mutant was created by allelic exchange and tested for the ability to survive in the murine macrophage-like cell line J774 [4].
  • Therefore, it appeared likely that the induction of the sodA gene was a response to an increase in superoxide radical production mediated by these membrane-binding drugs in E. coli cells, possibly by disruption of the electron transport systems in the cell membranes [14].
  • After allowing for this serum sensitivity difference, the delta sodA delta sodB strain also showed increased susceptibility to phagocytic killing by human neutrophils [15].
  • Role of Salmonella typhimurium Mn-superoxide dismutase (SodA) in protection against early killing by J774 macrophages [4].

Associations of sodA with chemical compounds

  • A redox buffer containing various ratios of oxidized and reduced glutathione also modulated transcription of sodA thus demonstrating the existence of a redox-sensitive mechanism controlling sodA transcription [9].
  • We now report that NADPH, but not NADH, selectively decreases transcription of sodA in vitro and that an NADPH generating system utilizing glucose 6-phosphate and the corresponding dehydrogenase markedly augments this suppressive effect [9].
  • Since SOD activity could not be detected in dilute extracts, of the RBO-overexpressing sodA sodB strain, we propose that RBO catalyzes the reduction of O-2 at the expense of cellular reductants such as NAD(P)H [16].
  • Maxicell analysis and two-dimensional O'Farrell polyacrylamide gel electrophoresis demonstrated that the structural gene, sodA, of manganese superoxide dismutase was cloned [17].
  • The sodA gene was inactivated by insertion of an integrative vector carrying a kanamycin resistance gene [18].

Regulatory relationships of sodA


Other interactions of sodA

  • Northern blot analysis revealed a transcript that included fumC, orfX, and sodA, the amount of which was increased in response to iron deprivation [20].
  • Results on weak oxidative stress promoters (for sodA and acnA genes) were striking in that significant induction was observed when they were under a superoxide stress in plates [21].
  • In a comparison with an existing oxidative stress responsive strain, DPD2511 (katG::luxCDABE), which is sensitive to H(2)O(2), the mechanism of chemicals that cause oxidative damage was elucidated via the key transcriptional factors involved in induction of the sodA and katG promoters, i.e. SoxRS and OxyR, respectively [22].

Analytical, diagnostic and therapeutic context of sodA


  1. Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase. Farr, S.B., D'Ari, R., Touati, D. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  2. Superoxide dependence of the toxicity of short chain sugars. Benov, L., Fridovich, I. J. Biol. Chem. (1998) [Pubmed]
  3. Molecular and genetic characterization of superoxide dismutase in Haemophilus influenzae type b. Kroll, J.S., Langford, P.R., Saah, J.R., Loynds, B.M. Mol. Microbiol. (1993) [Pubmed]
  4. Role of Salmonella typhimurium Mn-superoxide dismutase (SodA) in protection against early killing by J774 macrophages. Tsolis, R.M., Bäumler, A.J., Heffron, F. Infect. Immun. (1995) [Pubmed]
  5. Inactivation of the Moraxella catarrhalis superoxide dismutase SodA induces constitutive expression of iron-repressible outer membrane proteins. Luke, N.R., Karalus, R.J., Campagnari, A.A. Infect. Immun. (2002) [Pubmed]
  6. Sensitive enzyme immunoassay for human Mn superoxide dismutase. Kurobe, N., Inagaki, T., Kato, K. Clin. Chim. Acta (1990) [Pubmed]
  7. Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli. Hassan, H.M., Sun, H.C. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  8. Cloned manganese superoxide dismutase reduces oxidative stress in Escherichia coli and Anacystis nidulans. Gruber, M.Y., Glick, B.R., Thompson, J.E. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  9. NADPH inhibits transcription of the Escherichia coli manganese superoxide dismutase gene (sodA) in vitro. Gardner, P.R., Fridovich, I. J. Biol. Chem. (1993) [Pubmed]
  10. Transcriptional regulation of Mn-superoxide dismutase gene (sodA) of Escherichia coli is stimulated by DNA gyrase inhibitors. Schrum, L.W., Hassan, H.M. Arch. Biochem. Biophys. (1992) [Pubmed]
  11. Cloning, nucleotide sequence and characterization of a gene encoding superoxide dismutase from Campylobacter jejuni and Campylobacter coli. Purdy, D., Park, S.F. Microbiology (Reading, Engl.) (1994) [Pubmed]
  12. Transcriptional activation of Mn-superoxide dismutase gene (sodA) of Escherichia coli by MnCl2. Schrum, L.W., Hassan, H.M. Biochim. Biophys. Acta (1993) [Pubmed]
  13. Contribution of the Mn-cofactored superoxide dismutase (SodA) to the virulence of Yersinia enterocolitica serotype O8. Roggenkamp, A., Bittner, T., Leitritz, L., Sing, A., Heesemann, J. Infect. Immun. (1997) [Pubmed]
  14. Induction of manganese-superoxide dismutase by membrane-binding drugs in Escherichia coli. Zhang, Q.M., Yonei, S. J. Bacteriol. (1991) [Pubmed]
  15. Superoxide dismutase protects Escherichia coli against killing by human serum. McManus, D.C., Josephy, P.D. Arch. Biochem. Biophys. (1995) [Pubmed]
  16. A mechanism for complementation of the sodA sodB defect in Escherichia coli by overproduction of the rbo gene product (desulfoferrodoxin) from Desulfoarculus baarsii. Liochev, S.I., Fridovich, I. J. Biol. Chem. (1997) [Pubmed]
  17. Cloning and mapping of the manganese superoxide dismutase gene (sodA) of Escherichia coli K-12. Touati, D. J. Bacteriol. (1983) [Pubmed]
  18. Cloning of the sodA gene from Corynebacterium melassecola and role of superoxide dismutase in cellular viability. Merkamm, M., Guyonvarch, A. J. Bacteriol. (2001) [Pubmed]
  19. Regulation of the manganese-containing superoxide dismutase is independent of the inducible DNA repair system in Escherichia coli. Hancock, L.C., Hassan, H.M. J. Biol. Chem. (1985) [Pubmed]
  20. Fumarase C activity is elevated in response to iron deprivation and in mucoid, alginate-producing Pseudomonas aeruginosa: cloning and characterization of fumC and purification of native fumC. Hassett, D.J., Howell, M.L., Sokol, P.A., Vasil, M.L., Dean, G.E. J. Bacteriol. (1997) [Pubmed]
  21. A high-throughput approach to promoter study using green fluorescent protein. Lu, C., Bentley, W.E., Rao, G. Biotechnol. Prog. (2004) [Pubmed]
  22. Construction of a sodA::luxCDABE fusion Escherichia coli: comparison with a katG fusion strain through their responses to oxidative stresses. Lee, H.J., Gu, M.B. Appl. Microbiol. Biotechnol. (2003) [Pubmed]
  23. Molecular cloning and nucleotide sequence of the superoxide dismutase gene and characterization of its product from Bacillus subtilis. Inaoka, T., Matsumura, Y., Tsuchido, T. J. Bacteriol. (1998) [Pubmed]
  24. Cloning and characterization of an Mn-containing superoxide dismutase (SodA) of Bordetella pertussis. Graeff-Wohlleben, H., Killat, S., Banemann, A., Guiso, N., Gross, R. J. Bacteriol. (1997) [Pubmed]
  25. Binding of integration host factor (IHF) to the Escherichia coli sodA gene and its role in the regulation of a sodA-lacZ fusion gene. Presutti, D.G., Hassan, H.M. Mol. Gen. Genet. (1995) [Pubmed]
  26. Controls on the biosynthesis of the manganese-containing superoxide dismutase of Escherichia coli. Effects of thiols. Gardner, P.R., Fridovich, I. J. Biol. Chem. (1987) [Pubmed]
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