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Gene Review

mutS  -  methyl-directed mismatch repair protein

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2728, JW2703, ant, fdv, plm
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Disease relevance of mutS


High impact information on mutS

  • The repair is severely impaired in host strains carrying a mutation in any of the three loci dcm, mutL and mutS [3].
  • The phenotypes of the mutants indicate that the gene products of mutS and recD act independently [4].
  • Both adducts were site-specifically incorporated into M13MB102 DNA, and the adducted genomes were electroporated into wild-type or mutS-deficient Escherichia coli strains [5].
  • Expression of the T. aquaticus mutS gene in Escherichia coli results in a dominant mutator phenotype [6].
  • Sequencing of the mutS gene predicts an 89.3-kDa polypeptide sharing extensive amino acid sequence homology with MutS homologs from both prokaryotes and eukaryotes [6].

Chemical compound and disease context of mutS


Biological context of mutS

  • The repair of both the mismatch and the loops was directed by the state of dam methylation of the DNA chains and was dependent on the product of the mutS gene [10].
  • 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) [11].
  • The fourth mutS strain showed a 3.3 kb insertion after the 10th nucleotide of the mutS gene, and a 54 nucleotide deletion between two eight nucleotide direct repeats [12].
  • The Escherichia coli fdv gene probably encodes mutS and is located at minute 58.8 adjacent to the hyc-hyp gene cluster [13].
  • A computer-assisted database search of homologous sequences revealed that the plm-1 locus is identical to the mutS gene; the mini-Mu insertion most probably results in the production of a truncated MutS protein [14].

Anatomical context of mutS

  • The presence of a mutS gene homologue, which has not been reported to occur in any other known mtDNA, suggests that there is mismatch repair activity in S. glaucum mitochondria [15].

Associations of mutS with chemical compounds

  • Chlorambucil-induced mutants in mutS cells, implying the importance of mismatch repair in preventing CLB-induced mutations [8].
  • 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 [16].

Other interactions of mutS

  • The frequencies of targeted G-->T transversions increased markedly in mutY strains, while this mutagenic event was not affected in mutM or mutS strains [17].
  • Genomic variability among enteric pathogens: the case of the mutS-rpoS intergenic region [18].
  • The nucleotide sequence and the deduced amino acid sequence showed very strong identities to the sequence of the glmS (also called mutS) gene (80%) and to component S (82%) from the related C. tetanomorphum, respectively [19].
  • Comparison of mutS phylogeny against predicted E. coli "whole-chromosome" phylogenies (derived from multilocus enzyme electrophoresis and mdh sequences) revealed striking levels of phylogenetic discordance among mutS alleles and their respective strains [20].

Analytical, diagnostic and therapeutic context of mutS

  • In interspecies genetic crosses, however, recipients with the mutSDelta800 mutation show increased recombination by up to 280-fold relative to mutS+ [21].
  • The mutS gene from the thermophilic bacterium Thermus thermophilus was PCR amplified, cloned, and expressed in Escherichia coli [22].


  1. Products of DNA mismatch repair genes mutS and mutL are required for transcription-coupled nucleotide-excision repair of the lactose operon in Escherichia coli. Mellon, I., Champe, G.N. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  2. 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]
  3. DNA mismatch-repair in Escherichia coli counteracting the hydrolytic deamination of 5-methyl-cytosine residues. Zell, R., Fritz, H.J. EMBO J. (1987) [Pubmed]
  4. Barriers to recombination between closely related bacteria: MutS and RecBCD inhibit recombination between Salmonella typhimurium and Salmonella typhi. Zahrt, T.C., Maloy, S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. MutS recognition of exocyclic DNA adducts that are endogenous products of lipid oxidation. Johnson, K.A., Mierzwa, M.L., Fink, S.P., Marnett, L.J. J. Biol. Chem. (1999) [Pubmed]
  6. Identification and characterization of a thermostable MutS homolog from Thermus aquaticus. Biswas, I., Hsieh, P. J. Biol. Chem. (1996) [Pubmed]
  7. Effects of Escherichia coli mutator genes mutH, mutL and mutS on 2-aminopurine induced DNA repair. Maenhaut-Michel, G., Caillet-Fauquet, P. Biochimie (1982) [Pubmed]
  8. Induction of SOS response, cellular efflux and oxidative stress response genes by chlorambucil in DNA repair-deficient Escherichia coli cells (ada, ogt and mutS). Salmelin, C., Vilpo, J. Mutat. Res. (2003) [Pubmed]
  9. 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]
  10. Repair of heteroduplex DNA molecules with multibase loops in Escherichia coli. Carraway, M., Marinus, M.G. J. Bacteriol. (1993) [Pubmed]
  11. 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]
  12. 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]
  13. The Escherichia coli fdv gene probably encodes mutS and is located at minute 58.8 adjacent to the hyc-hyp gene cluster. Schlensog, V., Böck, A. J. Bacteriol. (1991) [Pubmed]
  14. Preferential mutagenesis of lacZ integrated at unique sites in the Escherichia coli chromosome. Liu, S.K., Tseng, J.N., Shiuan, D., Hanawalt, P.C. Mol. Gen. Genet. (1997) [Pubmed]
  15. Mitochondrial DNA of the coral Sarcophyton glaucum contains a gene for a homologue of bacterial MutS: a possible case of gene transfer from the nucleus to the mitochondrion. Pont-Kingdon, G., Okada, N.A., Macfarlane, J.L., Beagley, C.T., Watkins-Sims, C.D., Cavalier-Smith, T., Clark-Walker, G.D., Wolstenholme, D.R. J. Mol. Evol. (1998) [Pubmed]
  16. 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]
  17. 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]
  18. Genomic variability among enteric pathogens: the case of the mutS-rpoS intergenic region. Kotewicz, M.L., Brown, E.W., Eugene LeClerc, J., Cebula, T.A. Trends Microbiol. (2003) [Pubmed]
  19. Cloning, sequencing and expression in Escherichia coli of the gene encoding component S of the coenzyme B12-dependent glutamate mutase from Clostridium cochlearium. Zelder, O., Beatrix, B., Buckel, W. FEMS Microbiol. Lett. (1994) [Pubmed]
  20. Phylogenetic evidence for horizontal transfer of mutS alleles among naturally occurring Escherichia coli strains. Brown, E.W., LeClerc, J.E., Li, B., Payne, W.L., Cebula, T.A. J. Bacteriol. (2001) [Pubmed]
  21. Separation of mutation avoidance and antirecombination functions in an Escherichia coli mutS mutant. Calmann, M.A., Nowosielska, A., Marinus, M.G. Nucleic Acids Res. (2005) [Pubmed]
  22. Construction and purification of his6-Thermus thermophilus MutS protein. Stanisławska-Sachadyn, A., Sachadyn, P., Jedrzejczak, R., Kur, J. Protein Expr. Purif. (2003) [Pubmed]
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