메뉴 건너뛰기




Volumn 384, Issue 1, 2008, Pages 31-47

The Role of Nucleotide Cofactor Binding in Cooperativity and Specificity of MutS Recognition

Author keywords

binding cooperativity; binding kinetics; MMR; MutS specificity; nucleotide cofactors

Indexed keywords

ADENYLYLIMIDODIPHOSPHATE; NUCLEOTIDE DERIVATIVE; PROTEIN MUTS;

EID: 54249112805     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.08.052     Document Type: Article
Times cited : (16)

References (50)
  • 1
    • 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
  • 2
    • 0242442569 scopus 로고    scopus 로고
    • DNA mismatch repair: molecular mechanisms and biological function
    • Schofield M.J., and Hsieh P. DNA mismatch repair: molecular mechanisms and biological function. Annu. Rev. Microbiol. 57 (2003) 579-608
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 579-608
    • Schofield, M.J.1    Hsieh, P.2
  • 4
    • 0017222053 scopus 로고
    • Bacterial mutator genes and the control of spontaneous mutation
    • Cox E.C. Bacterial mutator genes and the control of spontaneous mutation. Annu. Rev. Genet. 10 (1976) 135-156
    • (1976) Annu. Rev. Genet. , vol.10 , pp. 135-156
    • Cox, E.C.1
  • 5
    • 0027248156 scopus 로고
    • Genetics, natural history, tumor spectrum, and pathology of hereditary nonpolyposis colorectal cancer: an updated review
    • Lynch H.T., Smyrk T.C., Watson P., Lanspa S.J., Lynch J.F., Lynch P.M., et al. Genetics, natural history, tumor spectrum, and pathology of hereditary nonpolyposis colorectal cancer: an updated review. Gastroenterology 104 (1993) 1535-1549
    • (1993) Gastroenterology , vol.104 , pp. 1535-1549
    • Lynch, H.T.1    Smyrk, T.C.2    Watson, P.3    Lanspa, S.J.4    Lynch, J.F.5    Lynch, P.M.6
  • 6
    • 9544241423 scopus 로고    scopus 로고
    • Germline mutations of hMLH1 and hMSH2 genes in Korean hereditary nonpolyposis colorectal cancer
    • Han H.J., Yuan Y., Ku J.L., Oh J.H., Won Y.J., Kang K.J., et al. Germline mutations of hMLH1 and hMSH2 genes in Korean hereditary nonpolyposis colorectal cancer. J. Natl Cancer Inst. 88 (1996) 1317-1319
    • (1996) J. Natl Cancer Inst. , vol.88 , pp. 1317-1319
    • Han, H.J.1    Yuan, Y.2    Ku, J.L.3    Oh, J.H.4    Won, Y.J.5    Kang, K.J.6
  • 8
    • 0035201633 scopus 로고    scopus 로고
    • The intrinsically unstable life of DNA triplet repeats associated with human hereditary disorders
    • Bowater R.P., and Wells R.D. The intrinsically unstable life of DNA triplet repeats associated with human hereditary disorders. Prog. Nucleic Acid Res. Mol. Biol. 66 (2001) 159-202
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.66 , pp. 159-202
    • Bowater, R.P.1    Wells, R.D.2
  • 9
    • 0030737538 scopus 로고    scopus 로고
    • Trinucleotide repeats associated with human disease
    • Mitas M. Trinucleotide repeats associated with human disease. Nucleic Acids Res. 25 (1997) 2245-2254
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2245-2254
    • Mitas, M.1
  • 10
    • 0029891272 scopus 로고    scopus 로고
    • Repeat offenders: simple repeat sequences and complex genetic problems
    • Richards R.I., and Sutherland G.R. Repeat offenders: simple repeat sequences and complex genetic problems. Hum. Mutat. 8 (1996) 1-7
    • (1996) Hum. Mutat. , vol.8 , pp. 1-7
    • Richards, R.I.1    Sutherland, G.R.2
  • 11
    • 0024469392 scopus 로고
    • The barrier to recombination between Escherichia coli and Salmonella typhimurium is disrupted in mismatch-repair mutants
    • Rayssiguier C., Thaler D.S., and Radman M. The barrier to recombination between Escherichia coli and Salmonella typhimurium is disrupted in mismatch-repair mutants. Nature 342 (1989) 396-401
    • (1989) Nature , vol.342 , pp. 396-401
    • Rayssiguier, C.1    Thaler, D.S.2    Radman, M.3
  • 12
    • 0032127804 scopus 로고    scopus 로고
    • Hot spot focusing of somatic hypermutation in MSH2-deficient mice suggests two stages of mutational targeting
    • Rada C., Ehrenstein M.R., Neuberger M.S., and Milstein C. Hot spot focusing of somatic hypermutation in MSH2-deficient mice suggests two stages of mutational targeting. Immunity 9 (1998) 135-141
    • (1998) Immunity , vol.9 , pp. 135-141
    • Rada, C.1    Ehrenstein, M.R.2    Neuberger, M.S.3    Milstein, C.4
  • 13
    • 0027502938 scopus 로고
    • Defective mismatch binding and a mutator phenotype in cells tolerant to DNA damage
    • Branch P., Aquilina G., Bignami M., and Karran P. Defective mismatch binding and a mutator phenotype in cells tolerant to DNA damage. Nature 362 (1993) 652-654
    • (1993) Nature , vol.362 , pp. 652-654
    • Branch, P.1    Aquilina, G.2    Bignami, M.3    Karran, P.4
  • 14
    • 0031426561 scopus 로고    scopus 로고
    • Alkylation-induced apoptosis of embryonic stem cells in which the gene for DNA-repair, methyltransferase, had been disrupted by gene targeting
    • Tominaga Y., Tsuzuki T., Shiraishi A., Kawate H., and Sekiguchi M. Alkylation-induced apoptosis of embryonic stem cells in which the gene for DNA-repair, methyltransferase, had been disrupted by gene targeting. Carcinogenesis 18 (1997) 889-896
    • (1997) Carcinogenesis , vol.18 , pp. 889-896
    • Tominaga, Y.1    Tsuzuki, T.2    Shiraishi, A.3    Kawate, H.4    Sekiguchi, M.5
  • 15
    • 0000083876 scopus 로고
    • Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs
    • Su S.S., and Modrich P. Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs. Proc. Natl Acad. Sci. USA 83 (1986) 5057-5061
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 5057-5061
    • Su, S.S.1    Modrich, P.2
  • 16
    • 0024287626 scopus 로고
    • Mispair specificity of methyl-directed DNA mismatch correction in vitro
    • Su S.S., Lahue R.S., Au K.G., and Modrich P. Mispair specificity of methyl-directed DNA mismatch correction in vitro. J. Biol. Chem. 263 (1988) 6829-6835
    • (1988) J. Biol. Chem. , vol.263 , pp. 6829-6835
    • Su, S.S.1    Lahue, R.S.2    Au, K.G.3    Modrich, P.4
  • 17
    • 0024431799 scopus 로고
    • Heteroduplex DNA correction in Saccharomyces cerevisiae is mismatch specific and requires functional PMS genes
    • Kramer B., Kramer W., Williamson M.S., and Fogel S. Heteroduplex DNA correction in Saccharomyces cerevisiae is mismatch specific and requires functional PMS genes. Mol. Cell. Biol. 9 (1989) 4432-4440
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4432-4440
    • Kramer, B.1    Kramer, W.2    Williamson, M.S.3    Fogel, S.4
  • 18
  • 19
    • 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
  • 20
    • 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
  • 21
    • 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
  • 23
    • 10744232659 scopus 로고    scopus 로고
    • DNA bending and unbending by MutS govern mismatch recognition and specificity
    • Wang H., Yang Y., Schofield M.J., Du C., Fridman Y., Lee S.D., et al. DNA bending and unbending by MutS govern mismatch recognition and specificity. Proc. Natl Acad. Sci. USA 100 (2003) 14822-14827
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 14822-14827
    • Wang, H.1    Yang, Y.2    Schofield, M.J.3    Du, C.4    Fridman, Y.5    Lee, S.D.6
  • 24
    • 0030962031 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition
    • Alani E., Sokolsky T., Studamire B., Miret J.J., and Lahue R.S. Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition. Mol. Cell. Biol. 17 (1997) 2436-2447
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2436-2447
    • Alani, E.1    Sokolsky, T.2    Studamire, B.3    Miret, J.J.4    Lahue, R.S.5
  • 25
    • 0035951288 scopus 로고    scopus 로고
    • Disruption of the helix-u-turn-helix motif of MutS protein: loss of subunit dimerization, mismatch binding and ATP hydrolysis
    • Biswas I., Obmolova G., Takahashi M., Herr A., Newman M.A., Yang W., and Hsieh P. Disruption of the helix-u-turn-helix motif of MutS protein: loss of subunit dimerization, mismatch binding and ATP hydrolysis. J. Mol. Biol. 305 (2001) 805-816
    • (2001) J. Mol. Biol. , vol.305 , pp. 805-816
    • Biswas, I.1    Obmolova, G.2    Takahashi, M.3    Herr, A.4    Newman, M.A.5    Yang, W.6    Hsieh, P.7
  • 26
    • 1542782362 scopus 로고    scopus 로고
    • Hydrolytically deficient MutS E694A is defective in the MutL-dependent activation of MutH and in the mismatch-dependent assembly of the MutS·MutL·heteroduplex complex
    • Baitinger C., Burdett V., and Modrich P. Hydrolytically deficient MutS E694A is defective in the MutL-dependent activation of MutH and in the mismatch-dependent assembly of the MutS·MutL·heteroduplex complex. J. Biol. Chem. 278 (2003) 49505-49511
    • (2003) J. Biol. Chem. , vol.278 , pp. 49505-49511
    • Baitinger, C.1    Burdett, V.2    Modrich, P.3
  • 28
    • 0035823513 scopus 로고    scopus 로고
    • Distinct MutS DNA-binding modes that are differentially modulated by ATP binding and hydrolysis
    • Blackwell L.J., Bjornson K.P., Allen D.J., and Modrich P. Distinct MutS DNA-binding modes that are differentially modulated by ATP binding and hydrolysis. J. Biol. Chem. 276 (2001) 34339-34347
    • (2001) J. Biol. Chem. , vol.276 , pp. 34339-34347
    • Blackwell, L.J.1    Bjornson, K.P.2    Allen, D.J.3    Modrich, P.4
  • 29
    • 0038719734 scopus 로고    scopus 로고
    • Differential and simultaneous adenosine di- and triphosphate binding by MutS
    • Bjornson K.P., and Modrich P. Differential and simultaneous adenosine di- and triphosphate binding by MutS. J. Biol. Chem. 278 (2003) 18557-18562
    • (2003) J. Biol. Chem. , vol.278 , pp. 18557-18562
    • Bjornson, K.P.1    Modrich, P.2
  • 30
    • 5444242432 scopus 로고    scopus 로고
    • Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA
    • Antony E., and Hingorani M.M. Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA. Biochemistry 43 (2004) 13115-13128
    • (2004) Biochemistry , vol.43 , pp. 13115-13128
    • Antony, E.1    Hingorani, M.M.2
  • 31
    • 3142582009 scopus 로고    scopus 로고
    • Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites
    • Martik D., Baitinger C., and Modrich P. Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites. J. Biol. Chem. 279 (2004) 28402-28410
    • (2004) J. Biol. Chem. , vol.279 , pp. 28402-28410
    • Martik, D.1    Baitinger, C.2    Modrich, P.3
  • 32
    • 0032530155 scopus 로고    scopus 로고
    • A phylogenomic study of the MutS family of proteins
    • Eisen J.A. A phylogenomic study of the MutS family of proteins. Nucleic Acids Res. 26 (1998) 4291-4300
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4291-4300
    • Eisen, J.A.1
  • 33
    • 0033551850 scopus 로고    scopus 로고
    • Oligomerization of a MutS mismatch repair protein from Thermus aquaticus
    • Biswas I., Ban C., Fleming K.G., Qin J., Lary J.W., Yphantis D.A., et al. Oligomerization of a MutS mismatch repair protein from Thermus aquaticus. J. Biol. Chem. 274 (1999) 23673-23678
    • (1999) J. Biol. Chem. , vol.274 , pp. 23673-23678
    • Biswas, I.1    Ban, C.2    Fleming, K.G.3    Qin, J.4    Lary, J.W.5    Yphantis, D.A.6
  • 35
    • 34447255483 scopus 로고    scopus 로고
    • Escherichia coli MutS tetramerization domain structure reveals that stable dimers but not tetramers are essential for DNA mismatch repair in vivo
    • Mendillo M.L., Putnam C.D., and Kolodner R.D. Escherichia coli MutS tetramerization domain structure reveals that stable dimers but not tetramers are essential for DNA mismatch repair in vivo. J. Biol. Chem. 282 (2007) 16345-16354
    • (2007) J. Biol. Chem. , vol.282 , pp. 16345-16354
    • Mendillo, M.L.1    Putnam, C.D.2    Kolodner, R.D.3
  • 36
    • 24944454193 scopus 로고    scopus 로고
    • The MutS C terminus is essential for mismatch repair activity in vivo
    • Calmann M.A., Nowosielska A., and Marinus M.G. The MutS C terminus is essential for mismatch repair activity in vivo. J. Bacteriol. 187 (2005) 6577-6579
    • (2005) J. Bacteriol. , vol.187 , pp. 6577-6579
    • Calmann, M.A.1    Nowosielska, A.2    Marinus, M.G.3
  • 37
    • 0345304712 scopus 로고    scopus 로고
    • Formation of a DNA mismatch repair complex mediated by ATP
    • Selmane T., Schofield M.J., Nayak S., Du C., and Hsieh P. Formation of a DNA mismatch repair complex mediated by ATP. J. Mol. Biol. 334 (2003) 949-965
    • (2003) J. Mol. Biol. , vol.334 , pp. 949-965
    • Selmane, T.1    Schofield, M.J.2    Nayak, S.3    Du, C.4    Hsieh, P.5
  • 39
    • 0037445248 scopus 로고    scopus 로고
    • Role of DNA mismatch repair defects in the pathogenesis of human cancer
    • Peltomaki P. Role of DNA mismatch repair defects in the pathogenesis of human cancer. J. Clin. Oncol. 21 (2003) 1174-1179
    • (2003) J. Clin. Oncol. , vol.21 , pp. 1174-1179
    • Peltomaki, P.1
  • 41
    • 0028972305 scopus 로고
    • Single-step purifications of His6-MutH, His6-MutL and His6-MutS repair proteins of Escherichia coli K-12
    • Feng G., and Winkler M.E. Single-step purifications of His6-MutH, His6-MutL and His6-MutS repair proteins of Escherichia coli K-12. BioTechniques 19 (1995) 956-965
    • (1995) BioTechniques , vol.19 , pp. 956-965
    • Feng, G.1    Winkler, M.E.2
  • 42
    • 14444280136 scopus 로고    scopus 로고
    • Role of MutS ATPase activity in MutS,L-dependent block of in vitro strand transfer
    • Worth Jr. L., Bader T., Yang J., and Clark S. Role of MutS ATPase activity in MutS,L-dependent block of in vitro strand transfer. J. Biol. Chem. 273 (1998) 23176-23182
    • (1998) J. Biol. Chem. , vol.273 , pp. 23176-23182
    • Worth Jr., L.1    Bader, T.2    Yang, J.3    Clark, S.4
  • 43
    • 33846610053 scopus 로고    scopus 로고
    • The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair
    • Jacobs-Palmer E., and Hingorani M.M. The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair. J. Mol. Biol. 366 (2007) 1087-1098
    • (2007) J. Mol. Biol. , vol.366 , pp. 1087-1098
    • Jacobs-Palmer, E.1    Hingorani, M.M.2
  • 44
    • 0035868383 scopus 로고    scopus 로고
    • Affinity of mismatch-binding protein MutS for heteroduplexes containing different mismatches
    • Brown J., Brown T., and Fox K.R. Affinity of mismatch-binding protein MutS for heteroduplexes containing different mismatches. Biochem. J. 354 (2001) 627-633
    • (2001) Biochem. J. , vol.354 , pp. 627-633
    • Brown, J.1    Brown, T.2    Fox, K.R.3
  • 45
    • 0034696643 scopus 로고    scopus 로고
    • Modulation of MutS ATP hydrolysis by DNA cofactors
    • Bjornson K.P., Allen D.J., and Modrich P. Modulation of MutS ATP hydrolysis by DNA cofactors. Biochemistry 39 (2000) 3176-3183
    • (2000) Biochemistry , vol.39 , pp. 3176-3183
    • Bjornson, K.P.1    Allen, D.J.2    Modrich, P.3
  • 47
    • 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
  • 48
    • 23444433228 scopus 로고    scopus 로고
    • Determination of protein-DNA binding constants and specificities from statistical analyses of single molecules: MutS-DNA interactions
    • Yang Y., Sass L.E., Du C., Hsieh P., and Erie D.A. Determination of protein-DNA binding constants and specificities from statistical analyses of single molecules: MutS-DNA interactions. Nucleic Acids Res. 33 (2005) 4322-4334
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4322-4334
    • Yang, Y.1    Sass, L.E.2    Du, C.3    Hsieh, P.4    Erie, D.A.5
  • 49
    • 0035102126 scopus 로고    scopus 로고
    • Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair
    • Junop M.S., Obmolova G., Rausch K., Hsieh P., and Yang W. Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair. Mol. Cell 7 (2001) 1-12
    • (2001) Mol. Cell , vol.7 , pp. 1-12
    • Junop, M.S.1    Obmolova, G.2    Rausch, K.3    Hsieh, P.4    Yang, W.5
  • 50
    • 0035958857 scopus 로고    scopus 로고
    • Interaction of Escherichia coli MutS and MutL at a DNA mismatch
    • Schofield M.J., Nayak S., Scott T.H., Du C., and Hsieh P. Interaction of Escherichia coli MutS and MutL at a DNA mismatch. J. Biol. Chem. 276 (2001) 28291-28299
    • (2001) J. Biol. Chem. , vol.276 , pp. 28291-28299
    • Schofield, M.J.1    Nayak, S.2    Scott, T.H.3    Du, C.4    Hsieh, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.