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MeSH Review

SOS Response (Genetics)

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Disease relevance of SOS Response (Genetics)

  • Induction of SOS functions: regulation of proteolytic activity of E. coli RecA protein by interaction with DNA and nucleoside triphosphate [1].
  • From our results we conclude that antipain inhibits lambda prophage induction by blocking proteolytic inactivation of lambda repressor and that it inhibits the induction or expression of SOS repair and filamentous growth [2].
  • Inactivation of transfecting molecules showed that one lethal hit corresponded to 1.5 to 2.1 thymine glycols per phage DNA in normal cells, whereas conditions of W-reactivation (SOS induction) reversed 60 to 80% of inactivating events [3].
  • Induction of SOS response in Salmonella typhimurium TA4107/pSK1002 by peroxynitrite-generating agent, N-morpholino sydnonimine [4].
  • Two lines of evidence suggest that a gene analogous to the recA gene of Escherichia coli exists in Vibrio cholerae and that its product serves a proteolytic function in the SOS response [5].

High impact information on SOS Response (Genetics)

  • RecA is also a multifunctional protein, serving in different biochemical roles for recombinational processes, SOS induction, and mutagenic lesion bypass [6].
  • Genetic analyses have shown that SOS induction in response to double-stranded DNA (dsDNA) breaks requires LexA repressor, and the RecA and RecBCD enzymes--proteins best known for their role as initiators of dsDNA break repair and homologous recombination [7].
  • Chi is dispensable when cells are induced for the SOS response or contain a recD mutation. recBC sbcA mutant cells are also capable of RDR induction [8].
  • During the SOS response, LexA repressor is inactivated by specific cleavage [9].
  • RecA protein modified by tif mutations allows expression of SOS functions in the absence of inducing treatments [1].

Chemical compound and disease context of SOS Response (Genetics)


Biological context of SOS Response (Genetics)

  • Minichromosomes (oriC plasmids) pOC23 and pOC81 were induced to replicate in the absence of DnaA protein and transcription after SOS induction [15].
  • In this work, induction of the SOS response by the addition of mitomycin C was found to be prevented by overexpression of the dinI gene. dinI is an SOS gene which maps at 24.6 min of the E.coli chromosome and encodes a small protein of 81 amino acids [16].
  • The induction by methylating agents of the SOS function sfiA was measured by means of a sfiA::lac operon fusion in Escherichia coli mutants defective in alkylation repair [17].
  • The bacterial RecA protein plays a central role in the repair of stalled replication forks, double-strand break repair, general recombination, induction of the SOS response, and SOS mutagenesis [18].
  • It is a colorimetric assay based on the induction by these agents of the SOS function sfiA, whose level of expression is monitored by means of a sfiA::lacZ operon fusion [19].

Anatomical context of SOS Response (Genetics)


Associations of SOS Response (Genetics) with chemical compounds

  • 2-Keto-4-hydroxyglutarate aldolase also plays a role in respiratory metabolic pathways, which suggests a mechanism for respiration resumption during the termination of the SOS response [12].
  • Induction of the SOS response causes an increase in TLS events through the AAF adduct (approximately 13%) [22].
  • To test this hypothesis, we investigated the effect of a protease inhibitor, antipain [(1-carboxy-2-phenylethyl)carbamoyl-L-arginyl-L-valylargininal], on SOS induction [2].
  • This high concentration of beta 2 may be responsible for the observation that very little (if any) bypass of pyrimidine photodimers occurred in vivo when the SOS system was not induced [23].
  • When host cells were ultraviolet-irradiated to induce the SOS response, a slight increase (about 2-fold) in survival of transfecting f1-K12 DNA containing beta-ureidoisobutyric acid was observed [24].

Gene context of SOS Response (Genetics)

  • It was not observed in lexA and recA mutants which abolish the induction of the SOS response [25].
  • We found that a recA mutant that is defective in recombination but proficient in SOS induction could not elicit iSDR [26].
  • We reported earlier that the SOS box of the neighbouring uvrA gene also controls the transcription of the ssb gene [27].
  • These results indicate that the uvrD gene is induced during the SOS response, and that the expression of the gene may also be regulated by transcription attenuation [28].
  • Moreover, despite the fact that both dinB and umuDC loci are controlled by the SOS response, their constitutive and induced levels of expression are dramatically different [29].

Analytical, diagnostic and therapeutic context of SOS Response (Genetics)


  1. Induction of SOS functions: regulation of proteolytic activity of E. coli RecA protein by interaction with DNA and nucleoside triphosphate. Phizicky, E.M., Roberts, J.W. Cell (1981) [Pubmed]
  2. A protease inhibitor blocks SOS functions in Escherichia coli: antipain prevents lambda repressor inactivation, ultraviolet mutagenesis, and filamentous growth. Meyn, M.S., Rossman, T., Troll, W. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  3. Oxidative damage in DNA. Lack of mutagenicity by thymine glycol lesions. Hayes, R.C., Petrullo, L.A., Huang, H.M., Wallace, S.S., LeClerc, J.E. J. Mol. Biol. (1988) [Pubmed]
  4. Induction of SOS response in Salmonella typhimurium TA4107/pSK1002 by peroxynitrite-generating agent, N-morpholino sydnonimine. Motohashi, N., Saito, Y. Mutat. Res. (2002) [Pubmed]
  5. Evidence that a system similar to the recA system of Escherichia coli exists in Vibrio cholerae. Ghosh, R.K., Siddiqui, K.A., Mukhopadhyay, G., Ghosh, A. Mol. Gen. Genet. (1985) [Pubmed]
  6. The bacterial RecA protein and the recombinational DNA repair of stalled replication forks. Lusetti, S.L., Cox, M.M. Annu. Rev. Biochem. (2002) [Pubmed]
  7. Reconstitution of an SOS response pathway: derepression of transcription in response to DNA breaks. Anderson, D.G., Kowalczykowski, S.C. Cell (1998) [Pubmed]
  8. DNA replication triggered by double-stranded breaks in E. coli: dependence on homologous recombination functions. Asai, T., Bates, D.B., Kogoma, T. Cell (1994) [Pubmed]
  9. LexA and lambda Cl repressors as enzymes: specific cleavage in an intermolecular reaction. Kim, B., Little, J.W. Cell (1993) [Pubmed]
  10. Inducible repair of near-UV radiation lethal damage in E. coli. Peters, J., Jagger, J. Nature (1981) [Pubmed]
  11. Self-cleaving proteases. Blair, W.S., Semler, B.L. Curr. Opin. Cell Biol. (1991) [Pubmed]
  12. Recovery of respiration following the SOS response of Escherichia coli requires RecA-mediated induction of 2-keto-4-hydroxyglutarate aldolase. Cayrol, C., Petit, C., Raynaud, B., Capdevielle, J., Guillemot, J.C., Defais, M. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  13. Structural and functional organization of the colicin E1 operon. Waleh, N.S., Johnson, P.H. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  14. Changes in DNA base sequence induced by gamma-ray mutagenesis of lambda phage and prophage. Tindall, K.R., Stein, J., Hutchinson, F. Genetics (1988) [Pubmed]
  15. DNA damage-inducible origins of DNA replication in Escherichia coli. Magee, T.R., Asai, T., Malka, D., Kogoma, T. EMBO J. (1992) [Pubmed]
  16. Inhibition of Escherichia coli RecA coprotease activities by DinI. Yasuda, T., Morimatsu, K., Horii, T., Nagata, T., Ohmori, H. EMBO J. (1998) [Pubmed]
  17. 3-Methyladenine residues in DNA induce the SOS function sfiA in Escherichia coli. Boiteux, S., Huisman, O., Laval, J. EMBO J. (1984) [Pubmed]
  18. The bacterial RecA protein as a motor protein. Cox, M.M. Annu. Rev. Microbiol. (2003) [Pubmed]
  19. SOS chromotest, a direct assay of induction of an SOS function in Escherichia coli K-12 to measure genotoxicity. Quillardet, P., Huisman, O., D'Ari, R., Hofnung, M. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  20. Antioxidant effects of hydroxybenzalacetones on peroxynitrite-induced lipid peroxidation in red blood cell membrane ghost and SOS response in Salmonella typhimurium TA4107/pSK1002. Motohashi, N., Takahashi, A., Yamagami, C., Saito, Y. Chem. Pharm. Bull. (2005) [Pubmed]
  21. Identification of yebG as a DNA damage-inducible Escherichia coli gene. Lomba, M.R., Vasconcelos, A.T., Pacheco, A.B., de Almeida, D.F. FEMS Microbiol. Lett. (1997) [Pubmed]
  22. Cellular strategies for accommodating replication-hindering adducts in DNA: control by the SOS response in Escherichia coli. Koffel-Schwartz, N., Coin, F., Veaute, X., Fuchs, R.P. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  23. The beta subunit modulates bypass and termination at UV lesions during in vitro replication with DNA polymerase III holoenzyme of Escherichia coli. Shavitt, O., Livneh, Z. J. Biol. Chem. (1989) [Pubmed]
  24. Processing of DNA base damage by DNA polymerases. Dihydrothymine and beta-ureidoisobutyric acid as models for instructive and noninstructive lesions. Ide, H., Petrullo, L.A., Hatahet, Z., Wallace, S.S. J. Biol. Chem. (1991) [Pubmed]
  25. Induction of dnaN and dnaQ gene expression in Escherichia coli by alkylation damage to DNA. Quiñones, A., Kaasch, J., Kaasch, M., Messer, W. EMBO J. (1989) [Pubmed]
  26. Homologous recombination-dependent initiation of DNA replication from DNA damage-inducible origins in Escherichia coli. Asai, T., Sommer, S., Bailone, A., Kogoma, T. EMBO J. (1993) [Pubmed]
  27. Analysis of the regulatory region of the ssb gene of Escherichia coli. Brandsma, J.A., Bosch, D., de Ruÿter, M., van de Putte, P. Nucleic Acids Res. (1985) [Pubmed]
  28. Transcription of the uvrD gene of Escherichia coli is controlled by the lexA repressor and by attenuation. Easton, A.M., Kushner, S.R. Nucleic Acids Res. (1983) [Pubmed]
  29. Properties and functions of Escherichia coli: Pol IV and Pol V. Fuchs, R.P., Fujii, S., Wagner, J. Adv. Protein Chem. (2004) [Pubmed]
  30. Nucleotide sequence of the regulatory region of the uvrD gene of Escherichia coli. Finch, P., Emmerson, P.T. Gene (1983) [Pubmed]
  31. Production and crystallization of a selenomethionyl variant of UmuD', an Escherichia coli SOS response protein. Peat, T.S., Frank, E.G., Woodgate, R., Hendrickson, W.A. Proteins (1996) [Pubmed]
  32. The use of radiation-induced bacterial promoters in anaerobic conditions: a means to control gene expression in clostridium-mediated therapy for cancer. Nuyts, S., Van Mellaert, L., Theys, J., Landuyt, W., Lambin, P., Anné, J. Radiat. Res. (2001) [Pubmed]
  33. Cloning and sequence comparison of AvaI and BsoBI restriction-modification systems. Ruan, H., Lunnen, K.D., Scott, M.E., Moran, L.S., Slatko, B.E., Pelletier, J.J., Hess, E.J., Benner, J., Wilson, G.G., Xu, S.Y. Mol. Gen. Genet. (1996) [Pubmed]
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