메뉴 건너뛰기




Volumn 69, Issue 6, 2008, Pages 1544-1559

Mutations in the signature motif in MutS affect ATP-induced clamp formation and mismatch repair

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; PROTEIN MUTS;

EID: 50049120505     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06386.x     Document Type: Article
Times cited : (8)

References (71)
  • 1
    • 0041669372 scopus 로고    scopus 로고
    • The coordinated functions of the E. coli MutS and MutL proteins in mismatch repair
    • Acharya, S., Foster, P.L., Brooks, P. Fishel, R. (2003) The coordinated functions of the E. coli MutS and MutL proteins in mismatch repair. Mol Cell 12 : 233 246.
    • (2003) Mol Cell , vol.12 , pp. 233-246
    • Acharya, S.1    Foster, P.L.2    Brooks, P.3    Fishel, R.4
  • 2
    • 0038797998 scopus 로고    scopus 로고
    • Crystal structure and biochemical analysis of the MutS·ADP· beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair
    • Alani, E., Lee, J.Y., Schofield, M.J., Kijas, A.W., Hsieh, P. Yang, W. (2003) Crystal structure and biochemical analysis of the MutS·ADP· beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair. J Biol Chem 278 : 16088 16094.
    • (2003) J Biol Chem , vol.278 , pp. 16088-16094
    • Alani, E.1    Lee, J.Y.2    Schofield, M.J.3    Kijas, A.W.4    Hsieh, P.5    Yang, W.6
  • 4
    • 0038677940 scopus 로고    scopus 로고
    • Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair
    • Antony, E. Hingorani, M.M. (2003) Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair. Biochemistry 42 : 7682 7693.
    • (2003) Biochemistry , vol.42 , pp. 7682-7693
    • Antony, E.1    Hingorani, M.M.2
  • 5
    • 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. Hingorani, M.M. (2004) Asymmetric ATP binding and hydrolysis activity of the Thermus aquaticus MutS dimer is key to modulation of its interactions with mismatched DNA. Biochemistry 43 : 13115 13128.
    • (2004) Biochemistry , vol.43 , pp. 13115-13128
    • Antony, E.1    Hingorani, M.M.2
  • 6
    • 0034696643 scopus 로고    scopus 로고
    • Modulation of MutS ATP hydrolysis by DNA cofactors
    • Bjornson, K.P., Allen, D.J. Modrich, P. (2000) Modulation of MutS ATP hydrolysis by DNA cofactors. Biochemistry 39 : 3176 3183.
    • (2000) Biochemistry , vol.39 , pp. 3176-3183
    • Bjornson, K.P.1    Allen, D.J.2    Modrich, P.3
  • 7
    • 0038719734 scopus 로고    scopus 로고
    • Differential and simultaneous adenosine di- and triphosphate binding by MutS
    • Bjornson, K.P. Modrich, P. (2003) Differential and simultaneous adenosine di- and triphosphate binding by MutS. J Biol Chem 278 : 18557 18562.
    • (2003) J Biol Chem , vol.278 , pp. 18557-18562
    • Bjornson, K.P.1    Modrich, P.2
  • 8
    • 0033610878 scopus 로고    scopus 로고
    • Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism
    • Blackwell, L.J., Martik, D., Bjornson, K.P., Bjornson, E.S. Modrich, P. (1998) Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism. J Biol Chem 273 : 32055 32062.
    • (1998) J Biol Chem , vol.273 , pp. 32055-32062
    • Blackwell, L.J.1    Martik, D.2    Bjornson, K.P.3    Bjornson, E.S.4    Modrich, P.5
  • 9
    • 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. Modrich, P. (2001) Distinct MutS DNA-binding modes that are differentially modulated by ATP binding and hydrolysis. J Biol Chem 276 : 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
  • 10
    • 0028221943 scopus 로고
    • Mutation in the DNA mismatch repair gene homologue hMLH1 is associated with hereditary non-polyposis colon cancer
    • Bronner, C.E., Baker, S.M., Morrison, P.T., Warren, G., Smith, L.G., Lescoe, M.K., et al. (1994) Mutation in the DNA mismatch repair gene homologue hMLH1 is associated with hereditary non-polyposis colon cancer. Nature 368 : 258 261.
    • (1994) Nature , vol.368 , pp. 258-261
    • Bronner, C.E.1    Baker, S.M.2    Morrison, P.T.3    Warren, G.4    Smith, L.G.5    Lescoe, M.K.6
  • 11
    • 0034933542 scopus 로고    scopus 로고
    • Hereditary and somatic DNA mismatch repair gene mutations in sporadic endometrial carcinoma
    • Chadwick, R.B., Pyatt, R.E., Niemann, T.H., Richards, S.K., Johnson, C.K., Stevens, M.W., et al. (2001) Hereditary and somatic DNA mismatch repair gene mutations in sporadic endometrial carcinoma. J Med Genet 38 : 461 466.
    • (2001) J Med Genet , vol.38 , pp. 461-466
    • Chadwick, R.B.1    Pyatt, R.E.2    Niemann, T.H.3    Richards, S.K.4    Johnson, C.K.5    Stevens, M.W.6
  • 12
    • 35648963623 scopus 로고    scopus 로고
    • ABC transporters: How small machines do a big job
    • Davidson, A.L. Maloney, P.C. (2007) ABC transporters: how small machines do a big job. Trends Microbiol 15 : 448.
    • (2007) Trends Microbiol , vol.15 , pp. 448
    • Davidson, A.L.1    Maloney, P.C.2
  • 13
    • 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. Kunkel, T.A. (2001) Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6. J Biol Chem 276 : 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
  • 14
    • 0037019605 scopus 로고    scopus 로고
    • Evidence for sequential action of two ATPase active sites in yeast Msh2-Msh6
    • Drotschmann, K., Yang, W. Kunkel, T.A. (2002) Evidence for sequential action of two ATPase active sites in yeast Msh2-Msh6. DNA Repair 1 : 743 753.
    • (2002) DNA Repair , vol.1 , pp. 743-753
    • Drotschmann, K.1    Yang, W.2    Kunkel, T.A.3
  • 15
    • 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. Jiricny, J. (2000) 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 : 36550 36555.
    • (2000) J Biol Chem , vol.275 , pp. 36550-36555
    • Dufner, P.1    Marra, G.2    Raschle, M.3    Jiricny, J.4
  • 16
    • 0032527704 scopus 로고    scopus 로고
    • Mismatch repair, molecular switches, and signal transduction
    • Fishel, R. (1998) Mismatch repair, molecular switches, and signal transduction. Genes Dev 12 : 2096 2101.
    • (1998) Genes Dev , vol.12 , pp. 2096-2101
    • Fishel, R.1
  • 17
    • 0031059532 scopus 로고    scopus 로고
    • MutS homologs in mammalian cells
    • Fishel, R. Wilson, T. (1997) MutS homologs in mammalian cells. Curr Opin Genet Dev 7 : 105 113.
    • (1997) Curr Opin Genet Dev , vol.7 , pp. 105-113
    • Fishel, R.1    Wilson, T.2
  • 18
    • 0027742295 scopus 로고
    • The human mutator gene homolog MSH2 and its association with hereditary nonpolyposis colon cancer
    • [erratum appears in Cell 1994; 77: 167].
    • Fishel, R., Lescoe, M.K., Rao, M.R., Copeland, N.G., Jenkins, N.A., Garber, J., et al. (1993) The human mutator gene homolog MSH2 and its association with hereditary nonpolyposis colon cancer. Cell 75 : 1027 1038 [erratum appears in Cell 1994; 77: 167].
    • (1993) Cell , vol.75 , pp. 1027-1038
    • Fishel, R.1    Lescoe, M.K.2    Rao, M.R.3    Copeland, N.G.4    Jenkins, N.A.5    Garber, J.6
  • 21
    • 0031456973 scopus 로고    scopus 로고
    • The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch
    • Gradia, S., Acharya, S. Fishel, R. (1997) The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch. Cell 91 : 995 1005.
    • (1997) Cell , vol.91 , pp. 995-1005
    • Gradia, S.1    Acharya, S.2    Fishel, R.3
  • 23
    • 0034635517 scopus 로고    scopus 로고
    • The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch
    • Gradia, S., Acharya, S. Fishel, R. (2000) The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch. J Biol Chem 275 : 3922 3930.
    • (2000) J Biol Chem , vol.275 , pp. 3922-3930
    • Gradia, S.1    Acharya, S.2    Fishel, R.3
  • 24
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J. Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177 : 4121 4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 25
    • 0025734115 scopus 로고
    • Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities
    • Haber, L.T. Walker, G.C. (1991) Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities. EMBO J 10 : 2707 2715.
    • (1991) EMBO J , vol.10 , pp. 2707-2715
    • Haber, L.T.1    Walker, G.C.2
  • 26
    • 0034500024 scopus 로고    scopus 로고
    • DNA mismatch repair and genetic instability
    • Harfe, B.D. Jinks-Robertson, S. (2000) DNA mismatch repair and genetic instability. Annu Rev Genet 34 : 359 399.
    • (2000) Annu Rev Genet , vol.34 , pp. 359-399
    • Harfe, B.D.1    Jinks-Robertson, S.2
  • 27
    • 0037067689 scopus 로고    scopus 로고
    • Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP
    • Hess, M.T., Gupta, R.D. Kolodner, R.D. (2002) Dominant Saccharomyces cerevisiae msh6 mutations cause increased mispair binding and decreased dissociation from mispairs by Msh2-Msh6 in the presence of ATP. J Biol Chem 277 : 25545 25553.
    • (2002) J Biol Chem , vol.277 , pp. 25545-25553
    • Hess, M.T.1    Gupta, R.D.2    Kolodner, R.D.3
  • 28
    • 33847256553 scopus 로고    scopus 로고
    • Specialized mismatch repair function of Glu339 in the Phe-X-Glu motif of yeast Msh6
    • Holmes, S.F., Scarpinato, K.D., McCulloch, S.D., Schaaper, R.M. Kunkel, T.A. (2007) Specialized mismatch repair function of Glu339 in the Phe-X-Glu motif of yeast Msh6. DNA Repair 6 : 293 303.
    • (2007) DNA Repair , vol.6 , pp. 293-303
    • Holmes, S.F.1    Scarpinato, K.D.2    McCulloch, S.D.3    Schaaper, R.M.4    Kunkel, T.A.5
  • 29
    • 0037398027 scopus 로고    scopus 로고
    • Rad50/SMC proteins and ABC transporters: Unifying concepts from high-resolution structures
    • Hopfner, K.-P. Tainer, J.A. (2003) Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures. Current Opinion Structural Biology 13 : 249 255.
    • (2003) Current Opinion Structural Biology , vol.13 , pp. 249-255
    • Hopfner, K.-P.1    Tainer, J.A.2
  • 30
    • 0036306877 scopus 로고    scopus 로고
    • Structural differences in the NOE-derived structure of G-T mismatched DNA relative to normal DNA are correlated with differences in 13C relaxation-based internal dynamics
    • Isaacs, R.J., Rayens, W.S. Spielmann, H.P. (2002) Structural differences in the NOE-derived structure of G-T mismatched DNA relative to normal DNA are correlated with differences in 13C relaxation-based internal dynamics. J Mol Biol 319 : 191 207.
    • (2002) J Mol Biol , vol.319 , pp. 191-207
    • Isaacs, R.J.1    Rayens, W.S.2    Spielmann, H.P.3
  • 31
    • 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. Hingorani, M.M. (2007) The effects of nucleotides on MutS-DNA binding kinetics clarify the role of MutS ATPase activity in mismatch repair. J Mol Biol 366 : 1087 1098.
    • (2007) J Mol Biol , vol.366 , pp. 1087-1098
    • Jacobs-Palmer, E.1    Hingorani, M.M.2
  • 32
    • 33646187811 scopus 로고    scopus 로고
    • The multifaceted mismatch-repair system
    • Jiricny, J. (2006) The multifaceted mismatch-repair system. Nat Rev Mol Cell Biol 7 : 335 346.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 335-346
    • Jiricny, J.1
  • 33
    • 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. Yang, W. (2001) Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair. Mol Cell 7 : 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
  • 34
    • 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. Miller, J.H. (2003) In vitro and in vivo studies of MutS, MutL and MutH mutants: correlation of mismatch repair and DNA recombination. DNA Repair 2 : 387 405.
    • (2003) DNA Repair , vol.2 , pp. 387-405
    • Junop, M.S.1    Yang, W.2    Funchain, P.3    Clendenin, W.4    Miller, J.H.5
  • 37
    • 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. Sixma, T.K. (2000) The crystal structure of DNA mismatch repair protein MutS binding to a G × T mismatch. Nature 407 : 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
  • 38
    • 0037415693 scopus 로고    scopus 로고
    • The alternating ATPase domains of MutS control DNA mismatch repair
    • Lamers, M.H., Winterwerp, H.H. Sixma, T.K. (2003) The alternating ATPase domains of MutS control DNA mismatch repair. EMBO J 22 : 746 756.
    • (2003) EMBO J , vol.22 , pp. 746-756
    • Lamers, M.H.1    Winterwerp, H.H.2    Sixma, T.K.3
  • 39
    • 6344226679 scopus 로고    scopus 로고
    • ATP increases the affinity between MutS ATPase domains. Implications for ATP hydrolysis and conformational changes
    • Lamers, M.H., Georgijevic, D., Lebbink, J.H., Winterwerp, H.H.K., Agianian, B., de Wind, N. Sixma, T.K. (2004) ATP increases the affinity between MutS ATPase domains. Implications for ATP hydrolysis and conformational changes. J Biol Chem 279 : 43879 43885.
    • (2004) J Biol Chem , vol.279 , pp. 43879-43885
    • Lamers, M.H.1    Georgijevic, D.2    Lebbink, J.H.3    Winterwerp, H.H.K.4    Agianian, B.5    De Wind, N.6    Sixma, T.K.7
  • 40
    • 38349016587 scopus 로고    scopus 로고
    • Structure-based interpretation of the mutagenesis database for the nucleotide binding domains of P-glycoprotein
    • Lawson, J., O'Mara, M.L. Kerr, I.D. (2008) Structure-based interpretation of the mutagenesis database for the nucleotide binding domains of P-glycoprotein. Biochim Biophys Acta (BBA) - Biomembranes 1778 : 376.
    • (2008) Biochim Biophys Acta (BBA) - Biomembranes , vol.1778 , pp. 376
    • Lawson, J.1    O'Mara, M.L.2    Kerr, I.D.3
  • 41
    • 33846688359 scopus 로고    scopus 로고
    • Structure and function of ABC transporters: The ATP switch provides flexible control
    • Linton, K.J. Higgins, C.F. (2007) Structure and function of ABC transporters: the ATP switch provides flexible control. Eur J Physiol 453 : 555 567.
    • (2007) Eur J Physiol , vol.453 , pp. 555-567
    • Linton, K.J.1    Higgins, C.F.2
  • 42
    • 0028264035 scopus 로고
    • Cystic fibrosis transmembrane conductance regulator mutations that disrupt nucleotide binding
    • Logan, J., Hiestand, D., Daram, P., Huang, Z., Muccio, D.D., Hartman, J., et al. (1994) Cystic fibrosis transmembrane conductance regulator mutations that disrupt nucleotide binding. J Clin Invest 94 : 228 236.
    • (1994) J Clin Invest , vol.94 , pp. 228-236
    • Logan, J.1    Hiestand, D.2    Daram, P.3    Huang, Z.4    Muccio, D.D.5    Hartman, J.6
  • 43
    • 0032730774 scopus 로고    scopus 로고
    • Genetic susceptibility to non-polyposis colorectal cancer
    • Lynch, H.T. de la Chapelle, A. (1999) Genetic susceptibility to non-polyposis colorectal cancer. J Med Genet 36 : 801 818.
    • (1999) J Med Genet , vol.36 , pp. 801-818
    • Lynch, H.T.1    De La Chapelle, A.2
  • 45
    • 3142582009 scopus 로고    scopus 로고
    • Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites
    • Martik, D., Baitinger, C. Modrich, P. (2004) Differential specificities and simultaneous occupancy of human MutSalpha nucleotide binding sites. J Biol Chem 279 : 28402 28410.
    • (2004) J Biol Chem , vol.279 , pp. 28402-28410
    • Martik, D.1    Baitinger, C.2    Modrich, P.3
  • 46
    • 33646491402 scopus 로고    scopus 로고
    • Inhibition of Msh6 ATPase activity by mispaired DNA induces a Msh2(ATP)-Msh6(ATP) state capable of hydrolysis-independent movement along DNA
    • Mazur, D.J., Mendillo, M.L. Kolodner, R.D. (2006) Inhibition of Msh6 ATPase activity by mispaired DNA induces a Msh2(ATP)-Msh6(ATP) state capable of hydrolysis-independent movement along DNA. Mol Cell 22 : 39 49.
    • (2006) Mol Cell , vol.22 , pp. 39-49
    • Mazur, D.J.1    Mendillo, M.L.2    Kolodner, R.D.3
  • 47
    • 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. Kolodner, R.D. (2007) 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 : 16345 16354.
    • (2007) J Biol Chem , vol.282 , pp. 16345-16354
    • Mendillo, M.L.1    Putnam, C.D.2    Kolodner, R.D.3
  • 48
    • 0023062989 scopus 로고
    • DNA mismatch correction
    • Modrich, P. (1987) DNA mismatch correction. Annu Rev Biochem 56 : 435 466.
    • (1987) Annu Rev Biochem , vol.56 , pp. 435-466
    • Modrich, P.1
  • 49
    • 0024596295 scopus 로고
    • Methyl-directed DNA mismatch correction
    • Modrich, P. (1989) Methyl-directed DNA mismatch correction. J Biol Chem 264 : 6597 6600.
    • (1989) J Biol Chem , vol.264 , pp. 6597-6600
    • Modrich, P.1
  • 50
    • 0030803659 scopus 로고    scopus 로고
    • Strand-specific mismatch repair in mammalian cells
    • Modrich, P. (1997) Strand-specific mismatch repair in mammalian cells. J Biol Chem 272 : 24727 24730.
    • (1997) J Biol Chem , vol.272 , pp. 24727-24730
    • Modrich, P.1
  • 52
    • 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. Sixma, T.K. (2003) 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 : 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
  • 53
    • 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. Yang, W. (2000) Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature 407 : 703 710.
    • (2000) Nature , vol.407 , pp. 703-710
    • Obmolova, G.1    Ban, C.2    Hsieh, P.3    Yang, W.4
  • 54
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham, M.L., Khare, D., Quiocho, F.A., Davidson, A.L. Chen, J. (2007) Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450 : 515 521.
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 55
    • 0027137935 scopus 로고
    • Hypermutability and mismatch repair deficiency in RER+ tumor cells
    • Parsons, R., Li, G.M., Longley, M.J., Fang, W.H., Papadopoulos, N., Jen, J., et al. (1993) Hypermutability and mismatch repair deficiency in RER+ tumor cells. Cell 75 : 1227 1236.
    • (1993) Cell , vol.75 , pp. 1227-1236
    • Parsons, R.1    Li, G.M.2    Longley, M.J.3    Fang, W.H.4    Papadopoulos, N.5    Jen, J.6
  • 56
    • 0037445248 scopus 로고    scopus 로고
    • Role of DNA mismatch repair defects in the pathogenesis of human cancer
    • Peltomaki, P. (2003) Role of DNA mismatch repair defects in the pathogenesis of human cancer. J Clin Oncol 21 : 1174 1179.
    • (2003) J Clin Oncol , vol.21 , pp. 1174-1179
    • Peltomaki, P.1
  • 57
    • 0022961641 scopus 로고
    • Mismatch repair in Escherichia coli
    • Radman, M. Wagner, R. (1986) Mismatch repair in Escherichia coli. Annu Rev Genet 20 : 523 538.
    • (1986) Annu Rev Genet , vol.20 , pp. 523-538
    • Radman, M.1    Wagner, R.2
  • 58
    • 33846794508 scopus 로고    scopus 로고
    • About a switch: How P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work
    • Sauna, Z.E. Ambudkar, S.V. (2007) About a switch: how P-glycoprotein (ABCB1) harnesses the energy of ATP binding and hydrolysis to do mechanical work. Mol Cancer Ther 6 : 13 23.
    • (2007) Mol Cancer Ther , vol.6 , pp. 13-23
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 59
    • 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. Hsieh, P. (2001a) Interaction of Escherichia coli MutS and MutL at a DNA mismatch. J Biol Chem 276 : 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
  • 60
    • 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. Hsieh, P. (2001b) The Phe-X-Glu DNA binding motif of MutS. The role of hydrogen bonding in mismatch recognition. J Biol Chem 276 : 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
  • 61
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P.C., Karpowich, N., Millen, L., Moody, J.E., Rosen, J., Thomas, P.J. Hunt, J.F. (2002) ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol Cell 10 : 139 149.
    • (2002) Mol Cell , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 62
    • 0000083876 scopus 로고
    • Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs
    • Su, S.S. Modrich, P. (1986) Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs. Proc Natl Acad Sci USA 83 : 5057 5061.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 5057-5061
    • Su, S.S.1    Modrich, P.2
  • 63
    • 10344228783 scopus 로고    scopus 로고
    • Altered expression of hMSH2 and hMLH1 in tumors with microsatellite instability and genetic alterations in mismatch repair genes
    • Thibodeau, S.N., French, A.J., Roche, P.C., Cunningham, J.M., Tester, D.J., Lindor, N.M., et al. (1996) Altered expression of hMSH2 and hMLH1 in tumors with microsatellite instability and genetic alterations in mismatch repair genes. Cancer Res 56 : 4836 4840.
    • (1996) Cancer Res , vol.56 , pp. 4836-4840
    • Thibodeau, S.N.1    French, A.J.2    Roche, P.C.3    Cunningham, J.M.4    Tester, D.J.5    Lindor, N.M.6
  • 64
    • 1242272074 scopus 로고    scopus 로고
    • Synergy between conserved ABC signature Ser residues in P-glycoprotein catalysis
    • Tombline, G., Bartholomew, L.A., Gimi, K., Tyndall, G.A. Senior, A.E. (2004) Synergy between conserved ABC signature Ser residues in P-glycoprotein catalysis. J Biol Chem 279 : 5363 5373.
    • (2004) J Biol Chem , vol.279 , pp. 5363-5373
    • Tombline, G.1    Bartholomew, L.A.2    Gimi, K.3    Tyndall, G.A.4    Senior, A.E.5
  • 65
    • 25444460555 scopus 로고    scopus 로고
    • Involvement of the 'occluded nucleotide conformation' of P-glycoprotein in the catalytic pathway
    • Tombline, G., Muharemagic, A., White, L.B. Senior, A.E. (2005) Involvement of the 'occluded nucleotide conformation' of P-glycoprotein in the catalytic pathway. Biochemistry 44 : 12879 12886.
    • (2005) Biochemistry , vol.44 , pp. 12879-12886
    • Tombline, G.1    Muharemagic, A.2    White, L.B.3    Senior, A.E.4
  • 66
    • 33646541093 scopus 로고    scopus 로고
    • The occluded nucleotide conformation of P-glycoprotein
    • Tombline, G. Senior, A.E. (2005) The occluded nucleotide conformation of P-glycoprotein. J Bioenerg Biomembr 37 : 497 500.
    • (2005) J Bioenerg Biomembr , vol.37 , pp. 497-500
    • Tombline, G.1    Senior, A.E.2
  • 67
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J. Gay, N.J. (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1 : 945 951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 69
    • 0033618407 scopus 로고    scopus 로고
    • Dissociation of mismatch recognition and ATPase activity by hMSH2-hMSH3
    • Wilson, T., Guerrette, S. Fishel, R. (1999) Dissociation of mismatch recognition and ATPase activity by hMSH2-hMSH3. J Biol Chem 274 : 21659 21664.
    • (1999) J Biol Chem , vol.274 , pp. 21659-21664
    • Wilson, T.1    Guerrette, S.2    Fishel, R.3
  • 70
    • 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. Hsieh, P. (2000) Requirement for Phe36 for DNA binding and mismatch repair by Escherichia coli MutS protein. Nucleic Acids Res 28 : 3564 3569.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3564-3569
    • Yamamoto, A.1    Schofield, M.J.2    Biswas, I.3    Hsieh, P.4
  • 71
    • 33646768613 scopus 로고    scopus 로고
    • Poor base stacking at DNA lesions may initiate recognition by many repair proteins
    • Yang, W. (2006) Poor base stacking at DNA lesions may initiate recognition by many repair proteins. DNA Repair 5 : 654.
    • (2006) DNA Repair , vol.5 , pp. 654
    • Yang, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.