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Volumn 6, Issue 3, 2007, Pages 293-303

Specialized mismatch repair function of Glu339 in the Phe-X-Glu motif of yeast Msh6

Author keywords

Mismatch repair; Msh6; MutS; Oxidative damage

Indexed keywords

8 HYDROXYDEOXYGUANOSINE; ALANINE; PROTEIN MSH6;

EID: 33847256553     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2006.10.023     Document Type: Article
Times cited : (9)

References (48)
  • 3
    • 0029943449 scopus 로고    scopus 로고
    • Mismatch repair in replication fidelity, genetic recombination, and cancer biology
    • Modrich P., and Lahue R. Mismatch repair in replication fidelity, genetic recombination, and cancer biology. Annu. Rev. Biochem. 65 (1996) 101-133
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 101-133
    • Modrich, P.1    Lahue, R.2
  • 5
    • 0034641947 scopus 로고    scopus 로고
    • The crystal structure of DNA mismatch repair protein MutS binding to a G × T mismatch
    • Lamers M.H., Perrakis A., Enzlin J.H., Winterwerp H.H., de Wind N., and Sixma T.K. The crystal structure of DNA mismatch repair protein MutS binding to a G × T mismatch. Nature 407 (2000) 711-717
    • (2000) Nature , vol.407 , pp. 711-717
    • Lamers, M.H.1    Perrakis, A.2    Enzlin, J.H.3    Winterwerp, H.H.4    de Wind, N.5    Sixma, T.K.6
  • 6
    • 0345138990 scopus 로고    scopus 로고
    • Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates
    • Natrajan G., Lamers M.H., Enzlin J.H., Winterwerp H.H., Perrakis A., and Sixma T.K. Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates. Nucleic Acids Res. 31 (2003) 4814-4821
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4814-4821
    • Natrajan, G.1    Lamers, M.H.2    Enzlin, J.H.3    Winterwerp, H.H.4    Perrakis, A.5    Sixma, T.K.6
  • 7
    • 0034641938 scopus 로고    scopus 로고
    • Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA
    • Obmolova G., Ban C., Hsieh P., and Yang W. Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature 407 (2000) 703-710
    • (2000) Nature , vol.407 , pp. 703-710
    • Obmolova, G.1    Ban, C.2    Hsieh, P.3    Yang, W.4
  • 8
    • 0034711294 scopus 로고    scopus 로고
    • Mismatch recognition and DNA-dependent stimulation of the ATPase activity of hMutSalpha is abolished by a single mutation in the hMSH6 subunit
    • Dufner P., Marra G., Raschle M., and Jiricny J. Mismatch recognition and DNA-dependent stimulation of the ATPase activity of hMutSalpha is abolished by a single mutation in the hMSH6 subunit. J. Biol. Chem. 275 (2000) 36550-36555
    • (2000) J. Biol. Chem. , vol.275 , pp. 36550-36555
    • Dufner, P.1    Marra, G.2    Raschle, M.3    Jiricny, J.4
  • 9
    • 0033523013 scopus 로고    scopus 로고
    • A mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition
    • Bowers J., Sokolsky T., Quach T., and Alani E. A mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition. J. Biol. Chem. 274 (1999) 16115-16125
    • (1999) J. Biol. Chem. , vol.274 , pp. 16115-16125
    • Bowers, J.1    Sokolsky, T.2    Quach, T.3    Alani, E.4
  • 10
    • 0034666177 scopus 로고    scopus 로고
    • Requirement for Phe36 for DNA binding and mismatch repair by Escherichia coli MutS protein
    • Yamamoto A., Schofield M.J., Biswas I., and Hsieh P. Requirement for Phe36 for DNA binding and mismatch repair by Escherichia coli MutS protein. Nucleic Acids Res. 28 (2000) 3564-3569
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3564-3569
    • Yamamoto, A.1    Schofield, M.J.2    Biswas, I.3    Hsieh, P.4
  • 11
    • 0030612650 scopus 로고    scopus 로고
    • Photocross-linking of the NH2-terminal region of Taq MutS protein to the major groove of a heteroduplex DNA
    • Malkov V.A., Biswas I., Camerini-Otero R.D., and Hsieh P. Photocross-linking of the NH2-terminal region of Taq MutS protein to the major groove of a heteroduplex DNA. J. Biol. Chem. 272 (1997) 23811-23817
    • (1997) J. Biol. Chem. , vol.272 , pp. 23811-23817
    • Malkov, V.A.1    Biswas, I.2    Camerini-Otero, R.D.3    Hsieh, P.4
  • 12
    • 0037414350 scopus 로고    scopus 로고
    • In vitro and in vivo studies of MutS, MutL and MutH mutants: correlation of mismatch repair and DNA recombination
    • Junop M.S., Yang W., Funchain P., Clendenin W., and Miller J.H. In vitro and in vivo studies of MutS, MutL and MutH mutants: correlation of mismatch repair and DNA recombination. DNA Repair (Amst.) 2 (2003) 387-405
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 387-405
    • Junop, M.S.1    Yang, W.2    Funchain, P.3    Clendenin, W.4    Miller, J.H.5
  • 13
    • 0035824627 scopus 로고    scopus 로고
    • The Phe-X-Glu DNA binding motif of MutS. The role of hydrogen bonding in mismatch recognition
    • Schofield M.J., Brownewell F.E., Nayak S., Du C., Kool E.T., and Hsieh P. The Phe-X-Glu DNA binding motif of MutS. The role of hydrogen bonding in mismatch recognition. J. Biol. Chem. 276 (2001) 45505-45508
    • (2001) J. Biol. Chem. , vol.276 , pp. 45505-45508
    • Schofield, M.J.1    Brownewell, F.E.2    Nayak, S.3    Du, C.4    Kool, E.T.5    Hsieh, P.6
  • 14
    • 0034500024 scopus 로고    scopus 로고
    • DNA mismatch repair and genetic instability
    • Harfe B.D., and Jinks-Robertson S. DNA mismatch repair and genetic instability. Annu. Rev. Genet. 34 (2000) 359-399
    • (2000) Annu. Rev. Genet. , vol.34 , pp. 359-399
    • Harfe, B.D.1    Jinks-Robertson, S.2
  • 16
    • 0035824554 scopus 로고    scopus 로고
    • Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6
    • Drotschmann K., Yang W., Brownewell F.E., Kool E.T., and Kunkel T.A. Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6. J. Biol. Chem. 276 (2001) 46225-46229
    • (2001) J. Biol. Chem. , vol.276 , pp. 46225-46229
    • Drotschmann, K.1    Yang, W.2    Brownewell, F.E.3    Kool, E.T.4    Kunkel, T.A.5
  • 17
    • 33744508935 scopus 로고    scopus 로고
    • The molecular mechanism of DNA damage recognition by MutS homologs and its consequences for cell death response
    • Salsbury Jr. F.R., Clodfelter J.E., Gentry M.B., Hollis T., and Scarpinato K.D. The molecular mechanism of DNA damage recognition by MutS homologs and its consequences for cell death response. Nucleic Acids Res. 34 (2006) 2173-2185
    • (2006) Nucleic Acids Res. , vol.34 , pp. 2173-2185
    • Salsbury Jr., F.R.1    Clodfelter, J.E.2    Gentry, M.B.3    Hollis, T.4    Scarpinato, K.D.5
  • 18
    • 0022381352 scopus 로고
    • Rapid repeated cloning of mutant lac repressor genes
    • Schaaper R.M., Danforth B.N., and Glickman B.W. Rapid repeated cloning of mutant lac repressor genes. Gene 39 (1985) 181-189
    • (1985) Gene , vol.39 , pp. 181-189
    • Schaaper, R.M.1    Danforth, B.N.2    Glickman, B.W.3
  • 19
    • 0021329185 scopus 로고
    • Use of bacteriophage P1 as a vector for Tn5 insertion mutagenesis
    • Quinto M., and Bender R.A. Use of bacteriophage P1 as a vector for Tn5 insertion mutagenesis. Appl. Environ. Microbiol. 47 (1984) 436-438
    • (1984) Appl. Environ. Microbiol. , vol.47 , pp. 436-438
    • Quinto, M.1    Bender, R.A.2
  • 20
    • 0020057063 scopus 로고
    • Mutator mutations in Escherichia coli induced by the insertion of phage mu and the transposable resistance elements Tn5 and Tn10
    • Siegel E.C., Wain S.L., Meltzer S.F., Binion M.L., and Steinberg J.L. Mutator mutations in Escherichia coli induced by the insertion of phage mu and the transposable resistance elements Tn5 and Tn10. Mutat. Res. 93 (1982) 25-33
    • (1982) Mutat. Res. , vol.93 , pp. 25-33
    • Siegel, E.C.1    Wain, S.L.2    Meltzer, S.F.3    Binion, M.L.4    Steinberg, J.L.5
  • 21
    • 0025953766 scopus 로고
    • Spontaneous mutation in the Escherichia coli lacI gene
    • Schaaper R.M., and Dunn R.L. Spontaneous mutation in the Escherichia coli lacI gene. Genetics 129 (1991) 317-326
    • (1991) Genetics , vol.129 , pp. 317-326
    • Schaaper, R.M.1    Dunn, R.L.2
  • 23
    • 0027980253 scopus 로고
    • Dominant negative mutator mutations in the mutS gene of Escherichia coli
    • Wu T.H., and Marinus M.G. Dominant negative mutator mutations in the mutS gene of Escherichia coli. J. Bacteriol. 176 (1994) 5393-5400
    • (1994) J. Bacteriol. , vol.176 , pp. 5393-5400
    • Wu, T.H.1    Marinus, M.G.2
  • 24
    • 0033950229 scopus 로고    scopus 로고
    • Gene replacement in gram-negative bacteria: the pMAKSAC vectors
    • 198-200, 202, 204
    • Favre D., and Viret J.F. Gene replacement in gram-negative bacteria: the pMAKSAC vectors. Biotechniques 28 (2000) 198-200, 202, 204
    • (2000) Biotechniques , vol.28
    • Favre, D.1    Viret, J.F.2
  • 25
  • 26
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: partial purification and some properties
    • Vogel H.J., and Bonner D.M. Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218 (1956) 97-106
    • (1956) J. Biol. Chem. , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 27
    • 0027323808 scopus 로고
    • The mutational specificity of two Escherichia coli dnaE antimutator alleles as determined from lacI mutation spectra
    • Schaaper R.M. The mutational specificity of two Escherichia coli dnaE antimutator alleles as determined from lacI mutation spectra. Genetics 134 (1993) 1031-1038
    • (1993) Genetics , vol.134 , pp. 1031-1038
    • Schaaper, R.M.1
  • 29
    • 0032915375 scopus 로고    scopus 로고
    • Mutator phenotypes conferred by MLH1 overexpression and by heterozygosity for mlh1 mutations
    • Shcherbakova P.V., and Kunkel T.A. Mutator phenotypes conferred by MLH1 overexpression and by heterozygosity for mlh1 mutations. Mol. Cell Biol. 19 (1999) 3177-3183
    • (1999) Mol. Cell Biol. , vol.19 , pp. 3177-3183
    • Shcherbakova, P.V.1    Kunkel, T.A.2
  • 30
    • 0030962035 scopus 로고    scopus 로고
    • Hypermutability of homonucleotide runs in mismatch repair and DNA polymerase proofreading yeast mutants
    • Tran H.T., Keen J.D., Kricker M., Resnick M.A., and Gordenin D.A. Hypermutability of homonucleotide runs in mismatch repair and DNA polymerase proofreading yeast mutants. Mol. Cell. Biol. 17 (1997) 2859-2865
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2859-2865
    • Tran, H.T.1    Keen, J.D.2    Kricker, M.3    Resnick, M.A.4    Gordenin, D.A.5
  • 31
    • 0023410420 scopus 로고
    • Spectra of spontaneous mutations in Escherichia coli strains defective in mismatch correction: the nature of in vivo DNA replication errors
    • Schaaper R.M., and Dunn R.L. Spectra of spontaneous mutations in Escherichia coli strains defective in mismatch correction: the nature of in vivo DNA replication errors. Proc. Natl. Acad. Sci. U.S.A. 84 (1987) 6220-6224
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6220-6224
    • Schaaper, R.M.1    Dunn, R.L.2
  • 32
    • 0029868110 scopus 로고    scopus 로고
    • Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair
    • Marsischky G.T., Filosi N., Kane M.F., and Kolodner R. Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair. Genes Dev. 10 (1996) 407-420
    • (1996) Genes Dev. , vol.10 , pp. 407-420
    • Marsischky, G.T.1    Filosi, N.2    Kane, M.F.3    Kolodner, R.4
  • 33
    • 0032416476 scopus 로고    scopus 로고
    • The role of mismatch repair in the prevention of base pair mutations in Saccharomyces cerevisiae
    • Earley M.C., and Crouse G.F. The role of mismatch repair in the prevention of base pair mutations in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 15487-15491
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 15487-15491
    • Earley, M.C.1    Crouse, G.F.2
  • 34
    • 0033197818 scopus 로고    scopus 로고
    • MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae
    • Ni T.T., Marsischky G.T., and Kolodner R.D. MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae. Mol. Cell 4 (1999) 439-444
    • (1999) Mol. Cell , vol.4 , pp. 439-444
    • Ni, T.T.1    Marsischky, G.T.2    Kolodner, R.D.3
  • 36
    • 0037040962 scopus 로고    scopus 로고
    • Activation of human MutS homologs by 8-oxo-guanine DNA damage
    • Mazurek A., Berardini M., and Fishel R. Activation of human MutS homologs by 8-oxo-guanine DNA damage. J. Biol. Chem. 277 (2002) 8260-8266
    • (2002) J. Biol. Chem. , vol.277 , pp. 8260-8266
    • Mazurek, A.1    Berardini, M.2    Fishel, R.3
  • 37
    • 0242365581 scopus 로고    scopus 로고
    • Strand-specific processing of 8-oxoguanine by the human mismatch repair pathway: inefficient removal of 8-oxoguanine paired with adenine or cytosine
    • Larson E.D., Iams K., and Drummond J.T. Strand-specific processing of 8-oxoguanine by the human mismatch repair pathway: inefficient removal of 8-oxoguanine paired with adenine or cytosine. DNA Repair (Amst.) 2 (2003) 1199-1210
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 1199-1210
    • Larson, E.D.1    Iams, K.2    Drummond, J.T.3
  • 39
    • 0035830851 scopus 로고    scopus 로고
    • Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase delta. Steady-state and pre-steady-state kinetic analysis
    • Einolf H.J., and Guengerich F.P. Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase delta. Steady-state and pre-steady-state kinetic analysis. J. Biol. Chem. 276 (2001) 3764-3771
    • (2001) J. Biol. Chem. , vol.276 , pp. 3764-3771
    • Einolf, H.J.1    Guengerich, F.P.2
  • 40
    • 14644406927 scopus 로고    scopus 로고
    • UVR-induced G-C to C-G transversions from oxidative DNA damage
    • Kino K., and Sugiyama H. UVR-induced G-C to C-G transversions from oxidative DNA damage. Mutat. Res. 571 (2005) 33-42
    • (2005) Mutat. Res. , vol.571 , pp. 33-42
    • Kino, K.1    Sugiyama, H.2
  • 41
    • 0028266940 scopus 로고
    • DNA replication fidelity with 8-oxodeoxyguanosine triphosphate
    • Pavlov Y.I., Minnick D.T., Izuta S., and Kunkel T.A. DNA replication fidelity with 8-oxodeoxyguanosine triphosphate. Biochemistry 33 (1994) 4695-4701
    • (1994) Biochemistry , vol.33 , pp. 4695-4701
    • Pavlov, Y.I.1    Minnick, D.T.2    Izuta, S.3    Kunkel, T.A.4
  • 42
    • 0028566564 scopus 로고
    • The fidelity of the human leading and lagging strand DNA replication apparatus with 8-oxodeoxyguanosine triphosphate
    • Minnick D.T., Pavlov Y.I., and Kunkel T.A. The fidelity of the human leading and lagging strand DNA replication apparatus with 8-oxodeoxyguanosine triphosphate. Nucleic Acids Res. 22 (1994) 5658-5664
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5658-5664
    • Minnick, D.T.1    Pavlov, Y.I.2    Kunkel, T.A.3
  • 43
    • 0032558424 scopus 로고    scopus 로고
    • Steady-state and pre-steady-state kinetic analysis of 8-oxo-7,8-dihydroguanosine triphosphate incorporation and extension by replicative and repair DNA polymerases
    • Einolf H.J., Schnetz-Boutaud N., and Guengerich F.P. Steady-state and pre-steady-state kinetic analysis of 8-oxo-7,8-dihydroguanosine triphosphate incorporation and extension by replicative and repair DNA polymerases. Biochemistry 37 (1998) 13300-13312
    • (1998) Biochemistry , vol.37 , pp. 13300-13312
    • Einolf, H.J.1    Schnetz-Boutaud, N.2    Guengerich, F.P.3
  • 45
    • 0037036363 scopus 로고    scopus 로고
    • Flipping duplex DNA inside out: a double base-flipping reaction mechanism by Escherichia coli MutY adenine glycosylase
    • Bernards A.S., Miller J.K., Bao K.K., and Wong I. Flipping duplex DNA inside out: a double base-flipping reaction mechanism by Escherichia coli MutY adenine glycosylase. J. Biol. Chem. 277 (2002) 20960-20964
    • (2002) J. Biol. Chem. , vol.277 , pp. 20960-20964
    • Bernards, A.S.1    Miller, J.K.2    Bao, K.K.3    Wong, I.4
  • 48
    • 3843090592 scopus 로고    scopus 로고
    • The coupling of tight DNA binding and base flipping: identification of a conserved structural motif in base flipping enzymes
    • Estabrook R.A., Lipson R., Hopkins B., and Reich N. The coupling of tight DNA binding and base flipping: identification of a conserved structural motif in base flipping enzymes. J. Biol. Chem. 279 (2004) 31419-31428
    • (2004) J. Biol. Chem. , vol.279 , pp. 31419-31428
    • Estabrook, R.A.1    Lipson, R.2    Hopkins, B.3    Reich, N.4


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