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Gene Review

mutT  -  dGTP-preferring nucleoside triphosphate...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0100, JW0097, nudA
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Disease relevance of mutT

  • This error-avoiding process is catalysed by a protein encoded by the mutT gene of Escherichia coli, mutations of which increase the occurrence of A.T----C.G transversions 100 to 10,000 times the level of the wild type [1].
  • Sequence and characterization of mutT from Proteus vulgaris [2].
  • 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 [3].

High impact information on mutT


Biological context of mutT

  • Spontaneous mutagenesis is monitored in Test B, which is performed with two mutator strains, one mismatch repair-deficient (mutS) and another deficient in 8-oxo-dGTP-ase activity (mutT) [8].
  • (Akiyama, M., Horiuchi, T., and Sekiguchi, M. (1987) Mol. Gen. Genet. 206, 9-16) and indicate that the first of the potential initiation codons (position 164) of the open reading frame in the PvuII fragment carrying the mutT gene is the site of initiation of translation of the 15,000-Da polypeptide [9].
  • Unlike mutT, a gene for another conserved nucleotide triphosphate pyrophosphohydrolase that functions as a mutator gene, the mazG deletion did not result in a mutator phenotype in E. coli [10].
  • The nucleotide sequence of the mutT gene was determined by the dideoxy method [11].
  • The protein was overproduced when the mutT gene was placed under the control of the lac regulatory region on a multicopy runaway plasmid [11].

Anatomical context of mutT


Associations of mutT with chemical compounds

  • However, because others have shown mutT mutations to be mutagenic under some conditions of anaerobic growth, and have shown 8-oxo-dGTP to be a poor DNA polymerase substrate, there is reason to question this model [5].
  • Strong mutator phenotypes of cells defective in both mutM and mutY genes or ones lacking mutT gene were completely suppressed under the anaerobic condition, indicative of an absence of hydroxyl radicals in the cells [12].
  • In addition, the sequence of the P. aeruginosa mutT gene strongly suggested that the product of this gene has a bifunctional activity in P. aeruginosa, being the C-terminal part 40% identical to a consensus sequence of thiamine monophosphate synthases [3].

Enzymatic interactions of mutT

  • The mutT gene product specifically hydrolyzes 8-oxo-dGTP to the monophosphate form while the mutM and the mutY gene products function to correct mispairs caused by incorporation of 8-oxoguanine into DNA [13].

Other interactions of mutT

  • Mutation rates were reduced in both mutL and mutT backgrounds, but mutagenesis by ultraviolet light was not significantly affected, suggesting that the antimutator effect may be largely restricted to normal DNA replication [14].
  • The interaction of the Escherichia coli mutD and mutT pathways in the prevention of A:T-->C:G transversions [15].

Analytical, diagnostic and therapeutic context of mutT


  1. MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Maki, H., Sekiguchi, M. Nature (1992) [Pubmed]
  2. Sequence and characterization of mutT from Proteus vulgaris. Kamath, A.V., Yanofsky, C. Gene (1993) [Pubmed]
  3. Characterization of the GO system of Pseudomonas aeruginosa. Oliver, A., Sánchez, J.M., Blázquez, J. FEMS Microbiol. Lett. (2002) [Pubmed]
  4. Escherichia coli mutY gene product is required for specific A-G----C.G mismatch correction. Au, K.G., Cabrera, M., Miller, J.H., Modrich, P. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  5. Assessing the metabolic function of the MutT 8-oxodeoxyguanosine triphosphatase in Escherichia coli by nucleotide pool analysis. Tassotto, M.L., Mathews, C.K. J. Biol. Chem. (2002) [Pubmed]
  6. Characterization of the mutT nucleoside triphosphatase of Escherichia coli. Bhatnagar, S.K., Bullions, L.C., Bessman, M.J. J. Biol. Chem. (1991) [Pubmed]
  7. Crystallization and preliminary X-ray diffraction studies on the mutT nucleoside triphosphate pyrophosphohydrolase of Escherichia coli. Bessman, M.J., Bullions, L.C., Bhatnagar, S.K., Braden, B.C., Love, W.E. J. Biol. Chem. (1991) [Pubmed]
  8. Comparative study of the antimutagenic potential of Vitamin E in different E. coli strains. Nikolić, B., Stanojević, J., Mitić, D., Vuković-Gacić, B., Knezević-Vukcević, J., Simić, D. Mutat. Res. (2004) [Pubmed]
  9. Studies on the mutator gene, mutT of Escherichia coli. Molecular cloning of the gene, purification of the gene product, and identification of a novel nucleoside triphosphatase. Bhatnagar, S.K., Bessman, M.J. J. Biol. Chem. (1988) [Pubmed]
  10. MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era, an essential GTPase in Escherichia coli. Zhang, J., Inouye, M. J. Bacteriol. (2002) [Pubmed]
  11. Molecular cloning and nucleotide sequence of the mutT mutator of Escherichia coli that causes A:T to C:G transversion. Akiyama, M., Horiuchi, T., Sekiguchi, M. Mol. Gen. Genet. (1987) [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. Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli. Tajiri, T., Maki, H., Sekiguchi, M. Mutat. Res. (1995) [Pubmed]
  14. Mutants of Escherichia coli with increased fidelity of DNA replication. Fijalkowska, I.J., Dunn, R.L., Schaaper, R.M. Genetics (1993) [Pubmed]
  15. The interaction of the Escherichia coli mutD and mutT pathways in the prevention of A:T-->C:G transversions. Fowler, R.G., Amutan, M.V., Isbell, R.J. Mutat. Res. (1992) [Pubmed]
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