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Gene Review

soxS  -  superoxide response regulon...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4054, JW4023
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Disease relevance of soxS


High impact information on soxS

  • The hmp promoter is more sensitive to SNP and S-nitroso-N-penicillamine (SNAP) than is the soxS promoter, consistent with the role of Hmp in protection from reactive nitrogen species [6].
  • Genomics of the marA/soxS/rob regulon of Escherichia coli: identification of directly activated promoters by application of molecular genetics and informatics to microarray data [7].
  • Purified SoxR protein is a homodimer containing a pair of [2Fe-2S] centers essential for soxS transcription in vitro . The [2Fe-2S] centers are thought to be anchored by a C-terminal cluster of four cysteine residues in SoxR [8].
  • To facilitate purification and characterization of SoxS, we constructed a fusion of soxS to malE, which encodes maltose-binding protein, and demonstrated that the in vivo expression of the MalE-SoxS fusion protein can provide SoxS function to a soxRS deletion mutant [9].
  • These genes, named soxR and soxS, are arranged divergently with their 5' ends separated by only 85 bp [10].

Chemical compound and disease context of soxS


Biological context of soxS


Anatomical context of soxS

  • After incubation with murine macrophages, soxS expression was induced in the phagocytosed bacteria up to approximately 30-fold after an 8-h exposure [16].

Associations of soxS with chemical compounds

  • Multicopy expression of mar, soxS, or robA induced cyclohexane tolerance in strains with a deleted or inactivated chromosomal mar, soxRS, or robA locus; thus, each transcriptional activator acts independently of the others [13].
  • In contrast, growth inhibition of the mutant by paraquat was relieved, and soxS was no longer induced by exogenous putrescine (1 mmol/L) [3].
  • Putrescine and spermidine downregulate the expression of soxS induced by paraquat in a concentration-dependent manner [3].
  • Several other superoxide-generating agents also trigger soxR(+)-dependent soxS expression, and the inductions by paraquat and phenazine methosulfate were dependent on the presence of oxygen [17].
  • We report here that overexpression of the multidrug efflux pump locus acrAB, or of marA or soxS, both encoding positive regulators of acrAB, decreased susceptibility to triclosan 2-fold [11].

Other interactions of soxS

  • It has been shown that mutations giving rise to increased expression of the transcriptional activators marA and soxS affect the expression of a variety of different genes, including ompF and acrAB [18].
  • This increase could be explained by transcription of soxS gene in a rpoS-dependent pathway [14].


  1. Overexpression of the marA or soxS regulatory gene in clinical topoisomerase mutants of Escherichia coli. Oethinger, M., Podglajen, I., Kern, W.V., Levy, S.B. Antimicrob. Agents Chemother. (1998) [Pubmed]
  2. Regulation of superoxide stress in Pseudomonas putida KT2440 is different from the SoxR paradigm in Escherichia coli. Park, W., Peña-Llopis, S., Lee, Y., Demple, B. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  3. Polyamines reduce paraquat-induced soxS and its regulon expression in Escherichia coli. Jung, I.L., Kim, I.G. Cell Biol. Toxicol. (2003) [Pubmed]
  4. Intracellular generation of superoxide as a by-product of Vibrio harveyi luciferase expressed in Escherichia coli. González-Flecha, B., Demple, B. J. Bacteriol. (1994) [Pubmed]
  5. MarA, SoxS and Rob function as virulence factors in an Escherichia coli murine model of ascending pyelonephritis. Casaz, P., Garrity-Ryan, L.K., McKenney, D., Jackson, C., Levy, S.B., Tanaka, S.K., Alekshun, M.N. Microbiology (Reading, Engl.) (2006) [Pubmed]
  6. The flavohemoglobin of Escherichia coli confers resistance to a nitrosating agent, a "Nitric oxide Releaser," and paraquat and is essential for transcriptional responses to oxidative stress. Membrillo-Hernández, J., Coopamah, M.D., Anjum, M.F., Stevanin, T.M., Kelly, A., Hughes, M.N., Poole, R.K. J. Biol. Chem. (1999) [Pubmed]
  7. Genomics of the marA/soxS/rob regulon of Escherichia coli: identification of directly activated promoters by application of molecular genetics and informatics to microarray data. Martin, R.G., Rosner, J.L. Mol. Microbiol. (2002) [Pubmed]
  8. Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and the role of the [2Fe-2S] centers in transcriptional activation. Bradley, T.M., Hidalgo, E., Leautaud, V., Ding, H., Demple, B. Nucleic Acids Res. (1997) [Pubmed]
  9. Purification of a MalE-SoxS fusion protein and identification of the control sites of Escherichia coli superoxide-inducible genes. Fawcett, W.P., Wolf, R.E. Mol. Microbiol. (1994) [Pubmed]
  10. Molecular characterization of the soxRS genes of Escherichia coli: two genes control a superoxide stress regulon. Amábile-Cuevas, C.F., Demple, B. Nucleic Acids Res. (1991) [Pubmed]
  11. Overexpression of marA, soxS, or acrAB produces resistance to triclosan in laboratory and clinical strains of Escherichia coli. McMurry, L.M., Oethinger, M., Levy, S.B. FEMS Microbiol. Lett. (1998) [Pubmed]
  12. Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli. Wu, J., Weiss, B. J. Bacteriol. (1991) [Pubmed]
  13. Role of the acrAB locus in organic solvent tolerance mediated by expression of marA, soxS, or robA in Escherichia coli. White, D.G., Goldman, J.D., Demple, B., Levy, S.B. J. Bacteriol. (1997) [Pubmed]
  14. Does UVB radiation induce SoxS gene expression in Escherichia coli cells? Gomes, A.A., Asad, L.M., Felzenszwalb, I., Leitão, A.C., Silva, A.B., Guillobel, H.C., Asad, N.R. Radiation and environmental biophysics. (2004) [Pubmed]
  15. Transcriptional regulation via redox-sensitive iron-sulphur centres in an oxidative stress response. Demple, B., Hidalgo, E., Ding, H. Biochem. Soc. Symp. (1999) [Pubmed]
  16. Roles of nitric oxide in inducible resistance of Escherichia coli to activated murine macrophages. Nunoshiba, T., DeRojas-Walker, T., Tannenbaum, S.R., Demple, B. Infect. Immun. (1995) [Pubmed]
  17. Two-stage control of an oxidative stress regulon: the Escherichia coli SoxR protein triggers redox-inducible expression of the soxS regulatory gene. Nunoshiba, T., Hidalgo, E., Amábile Cuevas, C.F., Demple, B. J. Bacteriol. (1992) [Pubmed]
  18. Mechanisms of fluoroquinolone resistance: an update 1994-1998. Piddock, L.J. Drugs (1999) [Pubmed]
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