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Gene Review

mutY  -  adenine DNA glycosylase

Escherichia coli str. K-12 substr. MG1655

 
 
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Disease relevance of mutY

  • Strains of Escherichia coli carrying the mutY mutation lack a mismatch correction glycosylase that removes adenines from various mismatch situations [1].
  • The mutT, mutM, and mutY genes of the GO system of the Pseudomonas aeruginosa PAO1 strain have been characterized by cloning, sequencing, and complementation analysis [2].
  • Antimutator role of the DNA glycosylase mutY gene in Helicobacter pylori [3].
 

High impact information on mutY

  • We now show that when trpA23 mutY bacteria are held under tryptophan starvation conditions the tryptophan-independent mutants that arise include small in-frame deletions in addition to transversions [1].
  • Extracts prepared from mutY/mutM E. coli expressing mOgg1 contain an activity that excises 8-oxoguanine from DNA and a beta-lyase activity that nicks DNA 3' to the lesion [4].
  • In addition, we have isolated a strain with a chromosomal mutation that suppresses the mutY phenotype and found that this suppressor also overexpresses MutM [5].
  • We find that the mutator phenotype of a mutY strain can be fully complemented by overexpressing MutM protein (Fpg protein) from a plasmid clone [5].
  • The Escherichia coli adenine DNA glycosylase, MutY, plays an important role in the maintenance of genomic stability by catalyzing the removal of adenine opposite 8-oxo-7,8-dihydroguanine or guanine in duplex DNA [6].
 

Chemical compound and disease context of mutY

 

Biological context of mutY

  • Here, we demonstrate that the mutant MutY(Delta26-134), which lacks the six-helix barrel domain, cannot complement the mutator phenotype of a mutY mutant in vivo [9].
  • In contrast, the ung and mutY mutants did not show higher frequencies of intergenomic recombination or greater sensitivity to UV-induced DNA damage than the wild type [3].
  • The H. pylori mutY open reading frame contains an eight-adenine homonucleotide tract; we provide evidence that this is subject to slipped-strand mispairing, leading to frameshifts that eliminate gene function [3].
  • In strains IC3894 (mutY) and IC3981 (mutY mutM), lacking mutagenesis proteins, SOS-independent revertants arose almost exclusively via G:C-T:A transversions probably derived from oxidatively damaged 8-oxoguanine/adenine mispairs [10].
  • The DNA sequence of a 2.3-kb fragment containing the micA gene has been determined [11].
 

Associations of mutY with chemical compounds

 

Other interactions of mutY

  • Spontaneous mutation frequencies of JP26 mutY mutants, assessed by rifampin resistance, were consistently higher (26-fold) than that of the wild type, whereas the ung and xthA mutants showed smaller increases [3].
  • Repair of heteroduplex DNA containing an A/G mismatch in a mutL background requires the Escherichia coli mutY gene function [16].
 

Analytical, diagnostic and therapeutic context of mutY

  • The observation that oG specificity derives almost exclusively from the C-terminal domain of MutY adds credence to the sequence analyses and suggests that specificity for oG.A mismatches was acquired by fusion of a MutT-like protein onto the core catalytic domain of an adenine-DNA glycosylase [15].

References

  1. Mutation in Escherichia coli under starvation conditions: a new pathway leading to small deletions in strains defective in mismatch correction. Bridges, B.A., Timms, A.R. EMBO J. (1997) [Pubmed]
  2. Characterization of the GO system of Pseudomonas aeruginosa. Oliver, A., Sánchez, J.M., Blázquez, J. FEMS Microbiol. Lett. (2002) [Pubmed]
  3. Antimutator role of the DNA glycosylase mutY gene in Helicobacter pylori. Huang, S., Kang, J., Blaser, M.J. J. Bacteriol. (2006) [Pubmed]
  4. Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase. Rosenquist, T.A., Zharkov, D.O., Grollman, A.P. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA. Michaels, M.L., Cruz, C., Grollman, A.P., Miller, J.H. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  6. Reaction intermediates in the catalytic mechanism of Escherichia coli MutY DNA glycosylase. Manuel, R.C., Hitomi, K., Arvai, A.S., House, P.G., Kurtz, A.J., Dodson, M.L., McCullough, A.K., Tainer, J.A., Lloyd, R.S. J. Biol. Chem. (2004) [Pubmed]
  7. MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III. Michaels, M.L., Pham, L., Nghiem, Y., Cruz, C., Miller, J.H. Nucleic Acids Res. (1990) [Pubmed]
  8. 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]
  9. An Escherichia coli MutY mutant without the six-helix barrel domain is a dimer in solution and assembles cooperatively into multisubunit complexes with DNA. Lee, C.Y., Bai, H., Houle, R., Wilson, G.M., Lu, A.L. J. Biol. Chem. (2004) [Pubmed]
  10. Specificity of spontaneous and t-butyl hydroperoxide-induced mutations in delta oxyR strains of Escherichia coli differing with respect to the SOS mutagenesis proficiency and to the MutY and MutM functions. Urios, A., Blanco, M. Mutat. Res. (1996) [Pubmed]
  11. Nucleotide sequence of the Escherichia coli micA gene required for A/G-specific mismatch repair: identity of micA and mutY. Tsai-Wu, J.J., Radicella, J.P., Lu, A.L. J. Bacteriol. (1991) [Pubmed]
  12. Impact of reactive oxygen species on spontaneous mutagenesis in Escherichia coli. Sakai, A., Nakanishi, M., Yoshiyama, K., Maki, H. Genes Cells (2006) [Pubmed]
  13. Specificity of mutations induced by riboflavin mediated photosensitization in the supF gene of Escherichia coli. Tano, K., Akasaka, S., Hashimoto, M., Asano, M., Yamamoto, K., Utsumi, H., Takimoto, K. Mutat. Res. (1998) [Pubmed]
  14. Analysis of spontaneous base substitutions generated in mutator strains of Bacillus subtilis. Sasaki, M., Kurusu, Y. FEMS Microbiol. Lett. (2004) [Pubmed]
  15. The C-terminal domain of the adenine-DNA glycosylase MutY confers specificity for 8-oxoguanine.adenine mispairs and may have evolved from MutT, an 8-oxo-dGTPase. Noll, D.M., Gogos, A., Granek, J.A., Clarke, N.D. Biochemistry (1999) [Pubmed]
  16. Escherichia coli mutY-dependent mismatch repair involves DNA polymerase I and a short repair tract. Tsai-Wu, J.J., Lu, A.L. Mol. Gen. Genet. (1994) [Pubmed]
 
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