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Volumn 106, Issue 11, 2009, Pages 4177-4182

Sequence context effect for hMSH2-hMSH6 mismatch-dependent activation

Author keywords

ATPase; Hereditary nonpolyposis colon cancer; Human mismatch repair; MutS homologs

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA; INTERMEDIN; OLIGONUCLEOTIDE; PROTEIN MSH2; PROTEIN MSH6; PROTEIN MUTS; PROTON; PURINE; PYRIMIDINE; SOLVENT;

EID: 63149199448     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0808572106     Document Type: Article
Times cited : (57)

References (49)
  • 1
    • 0029784320 scopus 로고    scopus 로고
    • Biochemistry and genetics of eukaryotic mismatch repair
    • Kolodner R (1996) Biochemistry and genetics of eukaryotic mismatch repair. Genes Dev 10:1433-1442.
    • (1996) Genes Dev , vol.10 , pp. 1433-1442
    • Kolodner, R.1
  • 2
    • 23244454477 scopus 로고    scopus 로고
    • Lynch syndrome: Form, function, proteins, and basketball
    • Boland CR, Fishel R (2005) Lynch syndrome: Form, function, proteins, and basketball. Gastroenterology 129:751-755.
    • (2005) Gastroenterology , vol.129 , pp. 751-755
    • Boland, C.R.1    Fishel, R.2
  • 3
    • 0032514843 scopus 로고    scopus 로고
    • Crystal structure and ATPase activity of MutL: Implications for DNA repair and mutagenesis
    • Ban C, Yang W (1998) Crystal structure and ATPase activity of MutL: Implications for DNA repair and mutagenesis. Cell 95:541-552.
    • (1998) Cell , vol.95 , pp. 541-552
    • Ban, C.1    Yang, W.2
  • 4
    • 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 LT, Walker GC (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
  • 5
    • 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
  • 6
    • 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
  • 7
    • 0034635517 scopus 로고    scopus 로고
    • Theroleofmismatchednucleotidesin activating the hMSH2-hMSH6 molecular switch
    • GradiaS,AcharyaS,Fishel R(2000)Theroleofmismatchednucleotidesin 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
  • 8
    • 0020332947 scopus 로고
    • Mismatch correction at O6-methylguanine residues in E. coli DNA
    • Karran P, Marinus MG (1982) Mismatch correction at O6-methylguanine residues in E. coli DNA. Nature 296:868-869.
    • (1982) Nature , vol.296 , pp. 868-869
    • Karran, P.1    Marinus, M.G.2
  • 9
    • 0033197818 scopus 로고    scopus 로고
    • MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae
    • Ni TT, Marsischky GT, Kolodner RD (1999) MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae. Mol Cell 4:439-444.
    • (1999) Mol Cell , vol.4 , pp. 439-444
    • Ni, T.T.1    Marsischky, G.T.2    Kolodner, R.D.3
  • 10
    • 0035225455 scopus 로고    scopus 로고
    • Keynote: Past, present,and future aspects of base excision repair
    • Lindahl T(2001)Keynote: Past, present,and future aspects of base excision repair. Prog Nucleic Acid Res Mol Biol 68:xvii-xxx.
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.68
    • Lindahl, T.1
  • 11
    • 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., et al. (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
  • 12
    • 0034641947 scopus 로고    scopus 로고
    • The crystal structure of DNA mismatch repair protein MutS binding to a G × T mismatch
    • Lamers MH, et al. (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
  • 13
    • 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
  • 14
    • 34248572591 scopus 로고    scopus 로고
    • Structure of the human MutSalpha DNA lesion recognition complex
    • Warren JJ, et al. (2007) Structure of the human MutSalpha DNA lesion recognition complex. Mol Cell 26:579-592.
    • (2007) Mol Cell , vol.26 , pp. 579-592
    • Warren, J.J.1
  • 15
    • 0035824627 scopus 로고    scopus 로고
    • The Phe-X-Glu DNA binding motif of MutS. The role of hydrogen bonding in mismatch recognition
    • Schofield MJ, et al. (2001) 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
  • 16
    • 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 (13)C relaxation-based internal dynamics
    • Isaacs RJ, Rayens WS, Spielmann HP (2002) Structural differences in the NOE-derived structure of G-T mismatched DNA relative to normal DNA are correlated with differences in (13)C 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
  • 17
    • 0034979126 scopus 로고    scopus 로고
    • Hydrogen bonding, base stacking, and steric effects in DNA replication
    • Kool ET(2001)Hydrogen bonding, base stacking, and steric effects in DNA replication. Annu Rev Biophys Biomol Struct 30:1-22.
    • (2001) Annu Rev Biophys Biomol Struct , vol.30 , pp. 1-22
    • Kool, E.T.1
  • 18
    • 0030875847 scopus 로고    scopus 로고
    • Thermodynamics and NMR of internal G.T mismatches in DNA
    • Allawi HT,Santa Lucia J, Jr (1997) Thermodynamics and NMR of internal G.T mismatches in DNA. Biochemistry 36:10581-10594.
    • (1997) Biochemistry , vol.36 , pp. 10581-10594
    • Allawi, H.T.1    Santa Lucia Jr, J.2
  • 19
    • 0027318463 scopus 로고
    • Sequence-dependent DNA structure. The role of base stacking interactions
    • Hunter CA (1993) Sequence-dependent DNA structure. The role of base stacking interactions. J Mol Biol 230:1025-1054.
    • (1993) J Mol Biol , vol.230 , pp. 1025-1054
    • Hunter, C.A.1
  • 20
    • 32644434270 scopus 로고    scopus 로고
    • Base-stacking and base- pairing contributions in to thermal stability of the DNA double helix
    • Yakovchuk P, Protozanova E, Frank-Kamenetskii MD (2006) Base-stacking and base- pairing contributions in to thermal stability of the DNA double helix. Nucleic Acids Res 34:564-574.
    • (2006) Nucleic Acids Res , vol.34 , pp. 564-574
    • Yakovchuk, P.1    Protozanova, E.2    Frank-Kamenetskii, M.D.3
  • 21
    • 0023140012 scopus 로고
    • Repair of a mismatch is influenced by the base composition of the surrounding nucleotide sequence
    • Jones M, Wagner R, Radman M (1987) Repair of a mismatch is influenced by the base composition of the surrounding nucleotide sequence. Genetics 115:605-610.
    • (1987) Genetics , vol.115 , pp. 605-610
    • Jones, M.1    Wagner, R.2    Radman, M.3
  • 22
    • 0033578888 scopus 로고    scopus 로고
    • Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA
    • Marsischky GT, Kolodner RD (1999) Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA. J Biol Chem 274:26668-26682.
    • (1999) J Biol Chem , vol.274 , pp. 26668-26682
    • Marsischky, G.T.1    Kolodner, R.D.2
  • 23
    • 0033546282 scopus 로고    scopus 로고
    • Specific binding of human MSH2.MSH6 mismatch-repair protein heterodimers to DNA incorporating thymine- or uracil- containing UV light photoproducts opposite mismatched bases
    • Wang H, Lawrence CW, Li GM, Hays JB (1999) Specific binding of human MSH2.MSH6 mismatch-repair protein heterodimers to DNA incorporating thymine- or uracil- containing UV light photoproducts opposite mismatched bases. J Biol Chem 274:16894-16900.
    • (1999) J Biol Chem , vol.274 , pp. 16894-16900
    • Wang, H.1    Lawrence, C.W.2    Li, G.M.3    Hays, J.B.4
  • 25
    • 0025340001 scopus 로고
    • Strand-specific mismatch correction in nuclear extracts of human and Drosophila melanogaster cell lines
    • Holmes J, Jr, Clark S, Modrich P (1990) Strand-specific mismatch correction in nuclear extracts of human and Drosophila melanogaster cell lines. Proc Natl Acad Sci USA 87:5837-5841.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5837-5841
    • Holmes Jr, J.1    Clark, S.2    Modrich, P.3
  • 26
    • 0025777777 scopus 로고
    • Heteroduplex repair in extracts of human HeLa cells
    • Thomas DC, Roberts JD, Kunkel TA (1991) Heteroduplex repair in extracts of human HeLa cells. J Biol Chem 266:3744-3751.
    • (1991) J Biol Chem , vol.266 , pp. 3744-3751
    • Thomas, D.C.1    Roberts, J.D.2    Kunkel, T.A.3
  • 27
    • 28844503379 scopus 로고    scopus 로고
    • Human mismatch repair: Reconstitution of a nick-directed bidirectional reaction
    • Constantin N, Dzantiev L, Kadyrov FA, Modrich P (2005) Human mismatch repair: Reconstitution of a nick-directed bidirectional reaction. J Biol Chem 280:39752-39761.
    • (2005) J Biol Chem , vol.280 , pp. 39752-39761
    • Constantin, N.1    Dzantiev, L.2    Kadyrov, F.A.3    Modrich, P.4
  • 28
    • 24144447320 scopus 로고    scopus 로고
    • Reconstitution of 5′-directed human mismatch repair in a purified system
    • Zhang Y, et al. (2005) Reconstitution of 5′-directed human mismatch repair in a purified system. Cell 122:693-705.
    • (2005) Cell , vol.122 , pp. 693-705
    • Zhang, Y.1
  • 29
    • 0033083040 scopus 로고    scopus 로고
    • hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA
    • Gradia S, et al. (1999) hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA. Mol Cell 3:255-261.
    • (1999) Mol Cell , vol.3 , pp. 255-261
    • Gradia, S.1
  • 30
    • 0041669372 scopus 로고    scopus 로고
    • The coordinated functions of the E. coli MutS and MutL proteins in mimsatch repair
    • Acharya S, Foster PL, Brooks P, Fishel R (2003) The coordinated functions of the E. coli MutS and MutL proteins in mimsatch 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
  • 31
    • 20444435104 scopus 로고    scopus 로고
    • Analysis of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-blocking system
    • Mendillo ML, Mazur DJ, Kolodner RD (2005) Analysis of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-blocking system. J Biol Chem 280:22245-22257.
    • (2005) J Biol Chem , vol.280 , pp. 22245-22257
    • Mendillo, M.L.1    Mazur, D.J.2    Kolodner, R.D.3
  • 32
    • 0027269844 scopus 로고
    • Human strand-specific mismatch repair occurs by a bidirectional mechanism similar to that of the bacterial reaction
    • Fang WH, Modrich P (1993) Human strand-specific mismatch repair occurs by a bidirectional mechanism similar to that of the bacterial reaction. J Biol Chem 268:11838-11844.
    • (1993) J Biol Chem , vol.268 , pp. 11838-11844
    • Fang, W.H.1    Modrich, P.2
  • 33
    • 0032581024 scopus 로고    scopus 로고
    • Nearest-neighbor thermodynamics of internal A.C mismatches in DNA: Sequence dependence and pH effects
    • Allawi HT, SantaLucia J, Jr (1998) Nearest-neighbor thermodynamics of internal A.C mismatches in DNA: Sequence dependence and pH effects. Biochemistry 37:9435-9444.
    • (1998) Biochemistry , vol.37 , pp. 9435-9444
    • Allawi, H.T.1    SantaLucia Jr, J.2
  • 34
    • 0032562140 scopus 로고    scopus 로고
    • Nearest neighbor thermodynamic parameters for internal G.A mismatches in DNA
    • Allawi HT, SantaLucia J, Jr (1998) Nearest neighbor thermodynamic parameters for internal G.A mismatches in DNA. Biochemistry 37:2170-2179.
    • (1998) Biochemistry , vol.37 , pp. 2170-2179
    • Allawi, H.T.1    SantaLucia Jr, J.2
  • 35
    • 0032102940 scopus 로고    scopus 로고
    • Thermodynamics of internal C.T mismatches in DNA
    • Allawi HT, SantaLucia J, Jr (1998) Thermodynamics of internal C.T mismatches in DNA. Nucleic Acids Res 26:2694-2701.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2694-2701
    • Allawi, H.T.1    SantaLucia Jr, J.2
  • 37
    • 0000826192 scopus 로고
    • Conformational dynamics of DNA and protein-DNA complexes by 31P NMR
    • Gorenstein DG (1994) Conformational dynamics of DNA and protein-DNA complexes by 31P NMR. Chem Rev 94:1315-1338.
    • (1994) Chem Rev , vol.94 , pp. 1315-1338
    • Gorenstein, D.G.1
  • 38
    • 1842526440 scopus 로고    scopus 로고
    • Solution structure of a DNA duplex containing an alpha-anomeric adenosine: Insights into substrate recognition by endonuclease IV
    • Aramini JM, Cleaver SH, Pon RT, Cunningham RP, Germann MW (2004) Solution structure of a DNA duplex containing an alpha-anomeric adenosine: Insights into substrate recognition by endonuclease IV. J Mol Biol 338:77-91.
    • (2004) J Mol Biol , vol.338 , pp. 77-91
    • Aramini, J.M.1    Cleaver, S.H.2    Pon, R.T.3    Cunningham, R.P.4    Germann, M.W.5
  • 39
    • 0023054131 scopus 로고
    • Structures of mismatched base pairs in DNA and their recognition by the Escherichia coli mismatch repair system
    • Fazakerley, et al. (1986) Structures of mismatched base pairs in DNA and their recognition by the Escherichia coli mismatch repair system. EMBO J 5:3697-3703.
    • (1986) EMBO J , vol.5 , pp. 3697-3703
    • Fazakerley1
  • 40
    • 0021191345 scopus 로고
    • Dynamics of DNA duplexes containing internal G-T, G-A, A-C, and T-C pairs: Hydrogen exchange at and adjacent to mismatch sites
    • Patel DJ, Kozlowski SA, Ikuta S, Itakura K (1984) Dynamics of DNA duplexes containing internal G-T, G-A, A-C, and T-C pairs: Hydrogen exchange at and adjacent to mismatch sites. Fed Proc. 43:2663-2670.
    • (1984) Fed Proc , vol.43 , pp. 2663-2670
    • Patel, D.J.1    Kozlowski, S.A.2    Ikuta, S.3    Itakura, K.4
  • 41
    • 0028864424 scopus 로고
    • Studies of base pair kinetics by NMR measurement of proton exchange
    • Gueron M, Leroy JL (1995) Studies of base pair kinetics by NMR measurement of proton exchange. Methods Enzymol 261:383-413.
    • (1995) Methods Enzymol , vol.261 , pp. 383-413
    • Gueron, M.1    Leroy, J.L.2
  • 42
    • 0026737976 scopus 로고
    • Kinetics and energetics of base-pair opening in 5′- d(CGCGAATTCGCG)-3′ and a substituted dodecamer containing G.T mismatches
    • Moe JG, Russu IM (1992) Kinetics and energetics of base-pair opening in 5′- d(CGCGAATTCGCG)-3′ and a substituted dodecamer containing G.T mismatches. Biochemistry 31:8421-8428.
    • (1992) Biochemistry , vol.31 , pp. 8421-8428
    • Moe, J.G.1    Russu, I.M.2
  • 43
    • 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 5:654-666.
    • (2006) DNA Repair , vol.5 , pp. 654-666
    • Yang, W.1
  • 44
    • 0032539693 scopus 로고    scopus 로고
    • A unified view of polymer, dumbbell, and oligonucleotide DNA nearest-neighbor thermodynamics
    • SantaLucia J, Jr (1998) A unified view of polymer, dumbbell, and oligonucleotide DNA nearest-neighbor thermodynamics. Proc Natl Acad Sci USA 95:1460-1465.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1460-1465
    • SantaLucia Jr, J.1
  • 45
    • 0034614487 scopus 로고    scopus 로고
    • Sequence-dependent DNA structure: Tet- ranucleotide conformational maps
    • Packer MJ, Dauncey MP, Hunter CA (2000) Sequence-dependent DNA structure: Tet- ranucleotide conformational maps. J Mol Biol 295:85-103.
    • (2000) J Mol Biol , vol.295 , pp. 85-103
    • Packer, M.J.1    Dauncey, M.P.2    Hunter, C.A.3
  • 47
    • 0037040962 scopus 로고    scopus 로고
    • Activation of human MutS homologs by 8-oxo-guanine DNA damage
    • Mazurek A, Berardini M, Fishel R (2002) Activation of human MutS homologs by 8-oxo-guanine DNA damage. J Biol Chem 277:8260-8266.
    • (2002) J Biol Chem , vol.277 , pp. 8260-8266
    • Mazurek, A.1    Berardini, M.2    Fishel, R.3
  • 48
    • 0029766233 scopus 로고    scopus 로고
    • Structure of a DNA duplex that contains alpha-anomeric nucleotides and 3′-3′ and 5′-5′ phosphodiester linkages: Coexistence of parallel and antiparallel DNA
    • Aramini JM, Kalisch BW, Pon RT, van de Sande JH, Germann MW (1996) Structure of a DNA duplex that contains alpha-anomeric nucleotides and 3′-3′ and 5′-5′ phosphodiester linkages: Coexistence of parallel and antiparallel DNA. Biochemistry 35:9355-9365.
    • (1996) Biochemistry , vol.35 , pp. 9355-9365
    • Aramini, J.M.1    Kalisch, B.W.2    Pon, R.T.3    van de Sande, J.H.4    Germann, M.W.5
  • 49
    • 34248596352 scopus 로고    scopus 로고
    • Catalytic efficiency and kcat/Km: A useful comparator?
    • Eisenthal R, Danson MJ, Hough DW (2007) Catalytic efficiency and kcat/Km: A useful comparator? Trends Biotechnol 25:247-249.
    • (2007) Trends Biotechnol , vol.25 , pp. 247-249
    • Eisenthal, R.1    Danson, M.J.2    Hough, D.W.3


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