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mutS  -  DNA mismatch repair protein MutS

Escherichia coli O157:H7 str. EDL933

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Disease relevance of mutS

  • Mismatch-containing oligonucleotide duplexes bound by the E. coli mutS-encoded protein [1].
  • We have cloned the mutS gene from the human opportunistic pathogen Pseudomonas aeruginosa and analysed the biochemical properties of the encoded protein [2].
  • We tested an alternative to gene shuffling based on plasmid recombination and found that Bacillus subtilis efficiently recombines sequences with 4% divergence, and Escherichia coli mutS is more appropriate for sequences with 22% divergence [3].
  • H. pylori gastritis is more frequent in patients with microsatellite instability-positive gastric cancers, and H. pylori organisms independently of inflammation can reduce DNA mismatch repair protein levels, raising the hypothesis that H. pylori organisms might lead to mutagenesis during infection [4].

High impact information on mutS

  • Enzymatic and chemical protection ("footprinting") experiments have demonstrated that mutS-encoded protein specifically binds to DNA regions containing a single base-pair mismatch [5].
  • These new mutators all mapped at three known mutator loci, mutH, mutL, and mutS, which exhibit the same mutagenic spectrum as the dam- mutator: increased levels of base substitution and frameshift mutations [6].
  • The results shown here indicate that the putative P. aeruginosa mutS, mutL and uvrD genes are mutator genes and that their alteration results in a mutator phenotype [7].
  • A class of catalase-deficient mutants that was unlinked to katE was localized between mutS and cys at 59.0 min on the Escherichia coli genome [8].
  • These include: mismatch recognition by mutS protein in which different mispairs are bound with different affinities; the direct involvement of d(GATC) sites; and strand scission by mutH protein at d(GATC) sequences with strand selection based on methylation of the DNA at those sites [9].

Chemical compound and disease context of mutS

  • This study compared the frequencies of emerging ceftazidime resistance in isogenic wild-type and hyper-mutable mutS CTX-M-3-producing Escherichia coli strains, and sequenced the mutant bla(CTX-M) alleles selected [10].

Associations of mutS with chemical compounds

  • Moreover, although ceftazidime-resistant mutants, or those with reduced susceptibility, were selected in both the wild-type and mutS hosts, many more mutants in the mutS host showed ceftazidimase-type extended-spectrum beta-lactamase (ESBL) activity [11].


  1. Mismatch-containing oligonucleotide duplexes bound by the E. coli mutS-encoded protein. Jiricny, J., Su, S.S., Wood, S.G., Modrich, P. Nucleic Acids Res. (1988) [Pubmed]
  2. Nucleotides and heteroduplex DNA preserve the active conformation of Pseudomonas aeruginosa MutS by preventing protein oligomerization. Pezza, R.J., Smania, A.M., Barra, J.L., Argaraña, C.E. Biochem. J. (2002) [Pubmed]
  3. Creating new genes by plasmid recombination in Escherichia coli and Bacillus subtilis. Gomez, A., Galic, T., Mariet, J.F., Matic, I., Radman, M., Petit, M.A. Appl. Environ. Microbiol. (2005) [Pubmed]
  4. Demonstration and characterization of mutations induced by Helicobacter pylori organisms in gastric epithelial cells. Yao, Y., Tao, H., Park, D.I., Sepulveda, J.L., Sepulveda, A.R. Helicobacter (2006) [Pubmed]
  5. Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs. Su, S.S., Modrich, P. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  6. Escherichia coli mutator mutants deficient in methylation-instructed DNA mismatch correction. Glickman, B.W., Radman, M. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  7. The mismatch repair system (mutS, mutL and uvrD genes) in Pseudomonas aeruginosa: molecular characterization of naturally occurring mutants. Oliver, A., Baquero, F., Blázquez, J. Mol. Microbiol. (2002) [Pubmed]
  8. Genetic mapping of katF, a locus that with katE affects the synthesis of a second catalase species in Escherichia coli. Loewen, P.C., Triggs, B.L. J. Bacteriol. (1984) [Pubmed]
  9. Methyl-directed DNA mismatch repair in Escherichia coli. Lahue, R.S., Modrich, P. Mutat. Res. (1988) [Pubmed]
  10. Development of high-level ceftazidime resistance via single-base substitutions of blaCTX-M-3 in hyper-mutable Escherichia coli. Karisik, E., Ellington, M.J., Pike, R., Livermore, D.M., Woodford, N. Clin. Microbiol. Infect. (2006) [Pubmed]
  11. Development of extended-spectrum activity in TEM beta-lactamases in hyper-mutable, mutS Escherichia coli. Ellington, M.J., Livermore, D.M., Pitt, T.L., Hall, L.M., Woodford, N. Clin. Microbiol. Infect. (2006) [Pubmed]
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