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Gene Review

mutM  -  formamidopyrimidine/5-formyluracil/ 5...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3625, JW3610, fpg
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Disease relevance of mutM


High impact information on mutM

  • After subcloning a 1.4-kb fragment which contained the Fapy-DNA glycosylase gene (fpg+) was inserted in the plasmids pUC18 and pUC19 yielding pFPG50 and pFPG60 respectively [5].
  • The nucleotide sequence of the fpg gene is composed of 809 base pairs and codes for a protein of 269 amino acids with a calculated mol. wt of 30.2 kd [5].
  • E. coli (fpg mutY) was transformed by a yeast DNA library, and clones that showed a reduced spontaneous mutagenesis were selected [6].
  • Cell-free extracts of E. coli (fpg mutY) harboring pYSB10 possess an enzymatic activity that cleaves a 34-mer oligonucleotide containing a single 8-oxoG opposite a cytosine (8-OxoG/C) [6].
  • The 2,6-diamino-4-hydroxy-5N-formamidopyrimidine (Fapy)-DNA glycosylase of Escherichia coli, which is coded for by the fpg gene, excises purine bases with ring-opened imidazoles [7].

Chemical compound and disease context of mutM


Biological context of mutM


Anatomical context of mutM

  • Furthermore CHO cells expressing the fpg gene had the same resistance to the lethal effect of hydrogen peroxide as control cells [17].

Associations of mutM with chemical compounds


Regulatory relationships of mutM


Other interactions of mutM

  • The locus, mutM, mapped near the cysE locus, which is at 81 min on the genetic map [1].
  • The frequencies of targeted G-->T transversions increased markedly in mutY strains, while this mutagenic event was not affected in mutM or mutS strains [22].
  • This strongly supports a role for NER in the repair of oxidative base damage in yeast, and differs from similar experiments carried out in E. coli, where transformation efficiency is only reduced in mutants defective in both fpg and uvrA [23].
  • To evaluate the relative importance of Fpg (Fapy) glycosylase (an enzyme known to remove oxidized bases) and the DNA damage-inducible UvrABC excinuclease in recovery from near-UV-induced stress, we have constructed fpg- and uvrA- derivatives of Escherichia coli and tested the response (survival) of these strains to both UVA and far-UV radiation [24].
  • The end of an open reading frame present upstream of the recA gene shows strong homology with formamidopyrimidine-DNA-glycosylase, a protein involved in DNA repair [25].

Analytical, diagnostic and therapeutic context of mutM


  1. mutM, a second mutator locus in Escherichia coli that generates G.C----T.A transversions. Cabrera, M., Nghiem, Y., Miller, J.H. J. Bacteriol. (1988) [Pubmed]
  2. Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein. Duwat, P., de Oliveira, R., Ehrlich, S.D., Boiteux, S. Microbiology (Reading, Engl.) (1995) [Pubmed]
  3. Mutagenic specificity of imidazole ring-opened 7-methylpurines in M13mp18 phage DNA. Tudek, B., Graziewicz, M., Kazanova, O., Zastawny, T.H., Obtułowicz, T., Laval, J. Acta Biochim. Pol. (1999) [Pubmed]
  4. Reduction of the toxicity and mutagenicity of aziridine in mammalian cells harboring the Escherichia coli fpg gene. Cussac, C., Laval, F. Nucleic Acids Res. (1996) [Pubmed]
  5. Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein. Boiteux, S., O'Connor, T.R., Laval, J. EMBO J. (1987) [Pubmed]
  6. Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine. van der Kemp, P.A., Thomas, D., Barbey, R., de Oliveira, R., Boiteux, S. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  7. Physical association of the 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase of Escherichia coli and an activity nicking DNA at apurinic/apyrimidinic sites. O'Connor, T.R., Laval, J. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  8. Deficiency of 8-hydroxyguanine DNA endonuclease activity and accumulation of the 8-hydroxyguanine in mutator mutant (mutM) of Escherichia coli. Bessho, T., Tano, K., Kasai, H., Nishimura, S. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  9. Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA. Gilboa, R., Zharkov, D.O., Golan, G., Fernandes, A.S., Gerchman, S.E., Matz, E., Kycia, J.H., Grollman, A.P., Shoham, G. J. Biol. Chem. (2002) [Pubmed]
  10. Escherichia coli Fpg protein and UvrABC endonuclease repair DNA damage induced by methylene blue plus visible light in vivo and in vitro. Czeczot, H., Tudek, B., Lambert, B., Laval, J., Boiteux, S. J. Bacteriol. (1991) [Pubmed]
  11. Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface. Buchko, G.W., McAteer, K., Wallace, S.S., Kennedy, M.A. DNA Repair (Amst.) (2005) [Pubmed]
  12. Cytotoxicity and mutagenesis induced by singlet oxygen in wild type and DNA repair deficient Escherichia coli strains. Cavalcante, A.K., Martinez, G.R., Di Mascio, P., Menck, C.F., Agnez-Lima, L.F. DNA Repair (Amst.) (2002) [Pubmed]
  13. Impact of reactive oxygen species on spontaneous mutagenesis in Escherichia coli. Sakai, A., Nakanishi, M., Yoshiyama, K., Maki, H. Genes Cells (2006) [Pubmed]
  14. Induction of the SOS response and mutations by reactive oxygen-generating compounds in various Escherichia coli mutants defective in the mutM, mutY or soxRS loci. Kato, T., Watanabe, M., Ohta, T. Mutagenesis (1994) [Pubmed]
  15. MutM, a protein that prevents G.C----T.A transversions, is formamidopyrimidine-DNA glycosylase. Michaels, M.L., Pham, L., Cruz, C., Miller, J.H. Nucleic Acids Res. (1991) [Pubmed]
  16. The genes encoding formamidopyrimidine and MutY DNA glycosylases in Escherichia coli are transcribed as part of complex operons. Gifford, C.M., Wallace, S.S. J. Bacteriol. (1999) [Pubmed]
  17. Expression of the E. coli fpg gene in mammalian cells reduces the mutagenicity of gamma-rays. Laval, F. Nucleic Acids Res. (1994) [Pubmed]
  18. Substrate discrimination by formamidopyrimidine-DNA glycosylase: a mutational analysis. Zaika, E.I., Perlow, R.A., Matz, E., Broyde, S., Gilboa, R., Grollman, A.P., Zharkov, D.O. J. Biol. Chem. (2004) [Pubmed]
  19. Hepsulfam induced DNA adducts and its excision repair by bacterial and mammalian 3-methyladenine DNA glycosylases. Je, K.H., Son, J.K., O'Connor, T.R., Lee, C.S. Mol. Cells (1998) [Pubmed]
  20. High Resolution Characterization of Formamidopyrimidine-DNA Glycosylase Interaction with Its Substrate by Chemical Cross-linking and Mass Spectrometry Using Substrate Analogs. Rogacheva, M., Ishchenko, A., Saparbaev, M., Kuznetsova, S., Ogryzko, V. J. Biol. Chem. (2006) [Pubmed]
  21. The influence of formamidopyrimidine-DNA glycosylase on the spontaneous and gamma-radiation-induced mutation spectrum of the lacZ alpha gene. Kuipers, G.K., Poldervaart, H.A., Slotman, B.J., Lafleur, M.V. Mutat. Res. (1999) [Pubmed]
  22. Mutations in the mutY gene of Escherichia coli enhance the frequency of targeted G:C-->T:a transversions induced by a single 8-oxoguanine residue in single-stranded DNA. Moriya, M., Grollman, A.P. Mol. Gen. Genet. (1993) [Pubmed]
  23. Spontaneous mutation, oxidative DNA damage, and the roles of base and nucleotide excision repair in the yeast Saccharomyces cerevisiae. Scott, A.D., Neishabury, M., Jones, D.H., Reed, S.H., Boiteux, S., Waters, R. Yeast (1999) [Pubmed]
  24. Role of Fapy glycosylase and UvrABC excinuclease in the repair of UVA (320-400 nm)-mediated DNA damage in Escherichia coli. Shennan, M.G., Palmer, C.M., Schellhorn, H.E. Photochem. Photobiol. (1996) [Pubmed]
  25. Use of degenerate primers for polymerase chain reaction cloning and sequencing of the Lactococcus lactis subsp. lactis recA gene. Duwat, P., Ehrlich, S.D., Gruss, A. Appl. Environ. Microbiol. (1992) [Pubmed]
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