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Gene Review

sodA  -  superoxide dismutase, Mn

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3901, JW3879
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Disease relevance of sodA


High impact information on sodA


Chemical compound and disease context of sodA

  • The precise location of the rhaT gene, encoding rhamnose permease, has been established between sodA and rhaC at 3605-3607 kb of Kohara's physical map, which corresponds to 88.4 min on the Escherichia coli chromosomal map [8].
  • Strains of E. coli with an inactivating insertion in the sodA gene do not induce inactive, reconstitutable MnSOD in response to NO3- plus PQ2+ and lack the immunoreactive MnSOD band [9].
  • Moreover, using fusions of sodA promoter to lacZ, we showed that sodA transcription was diminished in flavin reductase-deficient E. coli and that the induction of MnSOD by flavin reductase was SoxRS-independent [10].
  • We report the unexpected result that Escherichia coli isolates containing a multicopy plasmid (pDT1.5) carrying the manganese-superoxide dismutase gene sodA were more sensitive than the wild type to paraquat-mediated growth inhibition [11].

Biological context of sodA

  • The action of these effectors on the sodA promoter was investigated by using chromosomal sodA-lacZ operon fusions with intact or deleted promoters, different environmental conditions, and strains carrying different combinations of null mutations in the effector genes [12].
  • In aerobiosis, activation of sodA transcription by SoxRS was compatible with CfxB activation or Fur repression, whereas cfxB and fur controls were mutually exclusive [12].
  • Also, a second putative Fnr-binding site that straddles the ribosomal binding-site was identified in the sodA gene [13].
  • The sequence of the sodA-rhaC interval displayed a single ORF corresponding to rhaT, which is transcribed counterclockwise on the E. coli chromosome [8].
  • A strain of E. coli bearing a multicopy plasmid carrying the MnSOD gene (sodA) overproduces inactive MnSOD 19-fold compared to the parent strain under anaerobic conditions [9].

Associations of sodA with chemical compounds

  • Protein and operon fusions between the manganese superoxide dismutase (MnSOD) gene, sodA, and genes of the lactose operon were constructed in an attempt to explore the effects of various factors on MnSOD expression and the level at which they operate [14].
  • In sodA mutant cells lacking manganese superoxide dismutase activity but expressing the cloned gor gene (QC772:pJIK1) increased cellular glutathione reductase activity did not provide protection against methylviologen [15].
  • Paraquat-mediated selection for mutations in the manganese-superoxide dismutase gene sodA [11].
  • To our best knowledge, this is the first report of a sodA from S. thermophilus being expressed in other lactic acid bacteria [3].
  • Transcriptional analysis revealed that the sodA gene of S. agalactiae NEM318 was transcribed monocistronically from a promoter, the activity of which is neither regulated by pH, O2, nor CO2 concentrations of the culture medium [16].

Other interactions of sodA

  • In a soxR mutant, the expression of sodA, unlike that of nfo, was also regulated independently by oxygen tension [17].
  • Nucleotide sequence of the rhaR-sodA interval specifying rhaT in Escherichia coli [8].
  • In vivo, sodA-lacZ fusion activity was increased 3-fold by introducing plasmid pPL341, containing the hmp gene, or by growth with paraquat [18].
  • A total of six recombinant Escherichia coli strains with the promoters from three oxidative-stress responsive genes, i.e. the katG, sodA and pqi-5 genes, fused to either the lux genes from Vibrio fischeri or X. luminescens were characterized and their responses to different chemicals compared [19].
  • The sodF gene strongly complemented an Escherichia coli triple mutant (sodA sodB recA), restoring aerobic growth when the gene was expressed from the synthetic tac promoter but when expressed from its own promoter showed only slight rescue, suggesting that it was poorly recognized by the E. coli RNA polymerase [20].

Analytical, diagnostic and therapeutic context of sodA

  • A 1.2-kb PCR product containing the sodA gene was cloned into the shuttle vector pTRK563, to yield pSodA, which was functionally expressed and complemented an Escherichia coli strain deficient in Mn and FeSODs [3].
  • Gel retardation assays demonstrate high-affinity binding of pure, Mn2(+)-Fur protein to DNA fragments containing the sodA promoter [21].
  • Analysis by high resolution agarose gel electrophoresis of the AluI DNA polymorphism of the sodA locus in wild-type strains of S. agalactiae belonging to serogroups I, II, or III revealed no detectable difference [16].


  1. Use of site-directed mutagenesis to identify an upstream regulatory sequence of sodA gene of Escherichia coli K-12. Naik, S.M., Hassan, H.M. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  2. The sodA gene of Haemophilus ducreyi encodes a hydrogen peroxide-inhibitable superoxide dismutase. San Mateo, L.R., Toffer, K.L., Kawula, T.H. Gene (1998) [Pubmed]
  3. Expression of a heterologous manganese superoxide dismutase gene in intestinal lactobacilli provides protection against hydrogen peroxide toxicity. Bruno-Bárcena, J.M., Andrus, J.M., Libby, S.L., Klaenhammer, T.R., Hassan, H.M. Appl. Environ. Microbiol. (2004) [Pubmed]
  4. Essential role of superoxide dismutase on the pathogenicity of Erwinia chrysanthemi strain 3937. Santos, R., Franza, T., Laporte, M.L., Sauvage, C., Touati, D., Expert, D. Mol. Plant Microbe Interact. (2001) [Pubmed]
  5. Transcriptional regulation by iron of genes encoding iron- and manganese-superoxide dismutases from Pseudomonas putida. Kim, Y.C., Miller, C.D., Anderson, A.J. Gene (1999) [Pubmed]
  6. Induction of manganese-containing superoxide dismutase in anaerobic Escherichia coli by diamide and 1,10-phenanthroline: sites of transcriptional regulation. Privalle, C.T., Kong, S.E., Fridovich, I. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  7. Roles of manganese and iron in the regulation of the biosynthesis of manganese-superoxide dismutase in Escherichia coli. Hassan, H.M., Schrum, L.W. FEMS Microbiol. Rev. (1994) [Pubmed]
  8. Nucleotide sequence of the rhaR-sodA interval specifying rhaT in Escherichia coli. Garcia-Martin, C., Baldomà, L., Badía, J., Aguilar, J. J. Gen. Microbiol. (1992) [Pubmed]
  9. Anaerobic induction of ProMn-superoxide dismutase in Escherichia coli. Privalle, C.T., Beyer, W.F., Fridovich, I. J. Biol. Chem. (1989) [Pubmed]
  10. The NAD(P)H:flavin oxidoreductase from Escherichia coli as a source of superoxide radicals. Gaudu, P., Touati, D., Nivière, V., Fontecave, M. J. Biol. Chem. (1994) [Pubmed]
  11. Paraquat-mediated selection for mutations in the manganese-superoxide dismutase gene sodA. Bloch, C.A., Ausubel, F.M. J. Bacteriol. (1986) [Pubmed]
  12. Interaction of six global transcription regulators in expression of manganese superoxide dismutase in Escherichia coli K-12. Compan, I., Touati, D. J. Bacteriol. (1993) [Pubmed]
  13. Characterization of regulatory mutations causing anaerobic derepression of the sodA gene in Escherichia coli K12: cooperation between cis- and trans-acting regulatory loci. Beaumont, M.D., Hassan, H.M. J. Gen. Microbiol. (1993) [Pubmed]
  14. Transcriptional and posttranscriptional regulation of manganese superoxide dismutase biosynthesis in Escherichia coli, studied with operon and protein fusions. Touati, D. J. Bacteriol. (1988) [Pubmed]
  15. Variations in the activity of glutathione reductase and the cellular glutathione content in relation to sensitivity to methylviologen in Escherichia coli. Kunert, K.J., Cresswell, C.F., Schmidt, A., Mullineaux, P.M., Foyer, C.H. Arch. Biochem. Biophys. (1990) [Pubmed]
  16. Molecular characterization and expression analysis of the superoxide dismutase gene from Streptococcus agalactiae. Gaillot, O., Poyart, C., Berche, P., Trieu-Cuot, P. Gene (1997) [Pubmed]
  17. soxR, a locus governing a superoxide response regulon in Escherichia coli K-12. Tsaneva, I.R., Weiss, B. J. Bacteriol. (1990) [Pubmed]
  18. The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in vitro and causes oxidative stress in vivo. Membrillo-Hernández, J., Ioannidis, N., Poole, R.K. FEBS Lett. (1996) [Pubmed]
  19. Enhancement of the multi-channel continuous monitoring system through the use of Xenorhabdus luminescens lux fusions. Lee, J.H., Mitchell, R.J., Gu, M.B. Biosensors & bioelectronics. (2004) [Pubmed]
  20. Characterization of the sodF gene region of Frankia sp. strain ACN14a and complementation of Escherichia coli sod mutant. Maréchal, J., Santos, R., Hammad, Y., Alloisio, N., Domenach, A.M., Normand, P. Can. J. Microbiol. (2003) [Pubmed]
  21. Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus. Niederhoffer, E.C., Naranjo, C.M., Bradley, K.L., Fee, J.A. J. Bacteriol. (1990) [Pubmed]
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