메뉴 건너뛰기




Volumn , Issue , 2009, Pages 65-75

M-Hhal and MEcoRI: Paradigms for understanding the conformational mechanisms of DNA methyltransferases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 79956042694     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (79)
  • 1
    • 42049091946 scopus 로고    scopus 로고
    • Dna methyltransferase inhibitors: Class effect or unique agents?
    • Griffiths F.A, Gore SD. DNA methyltransferase inhibitors: Class effect or unique agents? Leukemia Lymphoma 2008: 49(4):650-651.
    • (2008) Leukemia Lymphoma , vol.49 , Issue.4 , pp. 650-651
    • Griffiths, F.A.1    Gore, S.D.2
  • 2
    • 28844497663 scopus 로고    scopus 로고
    • Procainamide is a specific inhibitor of dna methyltransferase 1
    • Lee BH, Yegnasubramanian S, Lin XH et al Procainamide is a specific inhibitor of DNA methyltransferase 1. J Biol Chem 2005; 280(49):40749-40756.
    • (2005) J Biol Chem , vol.280 , Issue.49 , pp. 40749-40756
    • Lee, B.H.1    Yegnasubramanian, S.2    Lin, X.H.3
  • 3
    • 33747098537 scopus 로고    scopus 로고
    • Selective inhibitors of bacterial dna adenine methyltransferases
    • Mashhoon N, Pruss C, Carroll M et al Selective inhibitors of bacterial DNA adenine methyltransferases. J Biomol Screen 2006; 11(5):497-510.
    • (2006) J Biomol Screen , vol.11 , Issue.5 , pp. 497-510
    • Mashhoon, N.1    Pruss, C.2    Carroll, M.3
  • 4
    • 54049147814 scopus 로고    scopus 로고
    • Azacytidine causes complex dna méthylation responses in myeloid leukemia
    • Strcsemann C, Bokelmann I, Mahlknecht U et al Azacytidine causes complex DNA méthylation responses in myeloid leukemia. Molecular Cancer Therapeutics 2008; 7(9):2998-3005.
    • (2008) Molecular Cancer Therapeutics , vol.7 , Issue.9 , pp. 2998-3005
    • Strcsemann, C.1    Bokelmann, I.2    Mahlknecht, U.3
  • 5
    • 67349268981 scopus 로고    scopus 로고
    • Zebularine suppresses the apoptotic potential of 5-fiuorouracil via camp/pka/creb pathway against human oral squamous cell carcinoma cells
    • Suzuki M, Shinohara F, Manabu E et al. Zebularine suppresses the apoptotic potential of 5-fiuorouracil via cAMP/PKA/CREB pathway against human oral squamous cell carcinoma cells. Cancer Chemoth Pharm2008; doi:10.1007A00280-008-0833-4.
    • (2008) Cancer Chemoth Pharm
    • Suzuki, M.1    Shinohara, F.2    Manabu, E.3
  • 6
    • 0029848936 scopus 로고    scopus 로고
    • Sequence-specific recognition by cytosine c-5 and adenine n-6 dna methyltransferases requires different deformations of dna
    • Garcia RA, Bustamante CJ, Reich NO. Sequence-specific recognition by cytosine C-5 and adenine N-6 DNA methyltransferases requires different deformations of DNA. Natl Acad Sci USA 1996; 93(15):7618-7622.
    • (1996) Natl Acad Sci USA , vol.93 , Issue.15 , pp. 7618-7622
    • Garcia, R.A.1    Bustamante, C.J.2    Reich, N.O.3
  • 7
    • 47949107313 scopus 로고    scopus 로고
    • Human dnmt2 methylates trna (Asp) molecules using a dna methyltransferase-like catalytic mechanism
    • Jurkowski TP, Meusburger M, Phalkc S et al. Human DNMT2 methylates tRNA (asp) molecules using a DNA methyltransferase-like catalytic mechanism. RNA 2008; 14(8):1663-1670.
    • (2008) RNA , vol.14 , Issue.8 , pp. 1663-1670
    • Jurkowski, T.P.1    Meusburger, M.2    Phalkc, S.3
  • 9
    • 0029163078 scopus 로고
    • Structure and function of dna methyltransferases
    • Cheng XD. Structure and function of DNA methyltransferases. Annu Rev Biophy Biom 1995; 24:293-318.
    • (1995) Annu Rev Biophy Biom , vol.24 , pp. 293-318
    • Cheng, X.D.1
  • 10
    • 0037007175 scopus 로고    scopus 로고
    • Beyond watson and crick: Dna méthylation and molecular enzymology of dna methyltransferases
    • Jeltsch A. Beyond watson and crick: DNA méthylation and molecular enzymology of DNA methyltransferases. Chcmbiochem 2002; 3(4):275-293.
    • (2002) Chcmbiochem , vol.3 , Issue.4 , pp. 275-293
    • Jeltsch, A.1
  • 11
    • 0027338134 scopus 로고
    • Crystal-structure of the hhal dna methyltransferase complexed with s-adenosyl-l-methionine
    • Cheng XD, Kumar S, Posfai J et al Crystal-structure of the Hhal DNA methyltransferase complexed with S-Adenosyl-L-Methionine. Cell 1993; 74(2):299-307.
    • (1993) Cell , vol.74 , Issue.2 , pp. 299-307
    • Cheng, X.D.1    Kumar, S.2    Posfai, J.3
  • 12
    • 33749985758 scopus 로고    scopus 로고
    • Structure, function and mechanism of exocyclic dna methyltransferases
    • Bheemanaik S, Reddy YVR, Rao DN. Structure, function and mechanism of exocyclic DNA methyltransferases. Biochemical J 2006; 399:177-190.
    • (2006) Biochemical J , vol.399 , pp. 177-190
    • Bheemanaik, S.1    Reddy, Y.2    Rao, D.N.3
  • 13
    • 0035883736 scopus 로고    scopus 로고
    • Adomet-dependent méthylation, dna methyltransferases and base flipping
    • Cheng XD, Roberts RJ. AdoMet-dependent méthylation, DNA methyltransferases and base flipping. Nucleic Acids Res 2001; 29(18):3784-3795.
    • (2001) Nucleic Acids Res , vol.29 , Issue.18 , pp. 3784-3795
    • Cheng, X.D.1    Roberts, R.J.2
  • 15
    • 0019522683 scopus 로고
    • Sequence-analysis of the dna encoding the ecori endonuclease and methylase
    • Greene PJ, Gupta M, Boyer HW et al Sequence-analysis of the DNA encoding the EcoRI endonuclease and methylase. J Biol Chem 1981; 256(5):2143-2153.
    • (1981) J Biol Chem , vol.256 , Issue.5 , pp. 2143-2153
    • Greene, P.J.1    Gupta, M.2    Boyer, H.W.3
  • 16
    • 0017730133 scopus 로고
    • Ecori methylase—physical and catalytic properties of homogeneous enzyme
    • Rubin RA, Modrich P. EcoRI methylase—physical and catalytic properties of homogeneous enzyme. J Biol Chem 1977; 252(20):7265-7272.
    • (1977) J Biol Chem , vol.252 , Issue.20 , pp. 7265-7272
    • Rubin, R.A.1    Modrich, P.2
  • 17
    • 0034746572 scopus 로고    scopus 로고
    • Structure of the n6-adenine dna methyltransferase m-taql in complex with dna and a cofactor analog
    • Goedecke K, Pignot M, Goody RS et al Structure of the N6-adenine DNA methyltransferase M-Taql in complex with DNA and a cofactor analog. Nature Structural Biology 2001; 8(2):121-125.
    • (2001) Nature Structural Biology , vol.8 , Issue.2 , pp. 121-125
    • Goedecke, K.1    Pignot, M.2    Goody, R.S.3
  • 18
    • 0025772075 scopus 로고
    • Kinetic mechanism of the ecori dna methyltransferase
    • Reich NO, Mashhoon N. Kinetic mechanism of the EcoRI DNA methyltransferase. Biochemistry 1991; 30(11):2933-2939.
    • (1991) Biochemistry , vol.30 , Issue.11 , pp. 2933-2939
    • Reich, N.O.1    Mashhoon, N.2
  • 19
    • 0033591248 scopus 로고    scopus 로고
    • Kinetic mechanism of cytosine dna methyltransferase mspl
    • Bhattacharya SK, Dubey AK. Kinetic mechanism of cytosine DNA methyltransferase Mspl. J Biol Chem1999; 274(21):14743-14749.
    • (1999) J Biol Chem , vol.274 , Issue.21 , pp. 14743-14749
    • Bhattacharya, S.K.1    Dubey, A.K.2
  • 20
    • 10644244206 scopus 로고    scopus 로고
    • Functional characterization of escherichia coli dna adenine methyltransfetase, a novel target for antibiotics
    • Mashhoon N, Carroll M, Pruss C et al Functional Characterization of Escherichia coli DNA adenine methyltransfetase, a novel target for antibiotics. J Biol Chem 2004; 279(50):52075-52081.
    • (2004) J Biol Chem , vol.279 , Issue.50 , pp. 52075-52081
    • Mashhoon, N.1    Carroll, M.2    Pruss, C.3
  • 21
    • 0034667760 scopus 로고    scopus 로고
    • Substrate binding in vitro and kinetics of rsri [n6-adcnine] dna methyltransferase
    • Szegedi SS, Reich NO, Gumpott RL Substrate binding in vitro and kinetics of RsrI [N6-adcnine] DNA methyltransferase. Nucleic Acids Res 2000; 28(20):3962-3971.
    • (2000) Nucleic Acids Res , vol.28 , Issue.20 , pp. 3962-3971
    • Szegedi, S.S.1    Reich, N.O.2    Gumpott, R.L.3
  • 22
    • 0023176797 scopus 로고
    • Kinetic and catalytic mechanism of hhal methyltransferase
    • Wu JC, Santi DV. Kinetic and catalytic mechanism of Hhal methyltransferase. J Biol Chem 1987; 262(10):4778-4786.
    • (1987) J Biol Chem , vol.262 , Issue.10 , pp. 4778-4786
    • Wu, J.C.1    Santi, D.V.2
  • 23
    • 0031960039 scopus 로고    scopus 로고
    • Phage t4 dna [n-6-adenine] methyltransferase: kinetic studies using oligonucleotides containing native or modified recognition sites
    • Zinoviev W, Evdokimov AA, Gorbunov YA et al Phage T4 DNA [N-6-adenine] methyltransferase: kinetic studies using oligonucleotides containing native or modified recognition sites. Biol Chem 1998; 379(4-5):481-488.
    • (1998) Biol Chem , vol.379 , Issue.4-5 , pp. 481-488
    • Zinoviev, W.1    Evdokimov, A.A.2    Gorbunov, Y.A.3
  • 24
    • 0036300777 scopus 로고    scopus 로고
    • The escherichia coli dam dna mcchyliransicra.Se modifies dna in a highly processive reaction
    • Urig S, Gowher H, Hermann A et al The Escherichia coli Dam DNA mcchyliransicra.se modifies DNA in a highly processive reaction. J Mol Biol 2002; 319(5):1085-1096.
    • (2002) J Mol Biol , vol.319 , Issue.5 , pp. 1085-1096
    • Urig, S.1    Gowher, H.2    Hermann, A.3
  • 25
    • 0030045741 scopus 로고    scopus 로고
    • Contribution of facilitated diffusion and processive catalysis to enzyme efficiency: implications for the ecori restriction-modification system
    • Surby MA, Reich NO. Contribution of facilitated diffusion and processive catalysis to enzyme efficiency: Implications for the EcoRI restriction-modification system. Biochemistry 1996; 35(7):2201-2208.
    • (1996) Biochemistry , vol.35 , Issue.7 , pp. 2201-2208
    • Surby, M.A.1    Reich, N.O.2
  • 26
    • 0030052447 scopus 로고    scopus 로고
    • Facilitated diffusion of the ecori dna rnctliyltransfcra.Se is described by a novel mechanism
    • Surby MA, Reich NO. Facilitated diffusion of the EcoRI DNA rnctliyltransfcra.se is described by a novel mechanism. Biochemistry 1996; 35(7):2209-2217.
    • (1996) Biochemistry , vol.35 , Issue.7 , pp. 2209-2217
    • Surby, M.A.1    Reich, N.O.2
  • 27
    • 0034644729 scopus 로고    scopus 로고
    • Molecular enzymology of the ecorv dna- (Adenine-n6 ())-mcthyltransferase: kinetics of dna binding and bending, kinetic mechanism and linear diffusion of the enzyme on dna
    • Gowher H, Jeltsch A. Molecular enzymology of the EcoRV DNA- (adenine-N6 ())-mcthyltransferase: Kinetics of DNA binding and bending, kinetic mechanism and linear diffusion of the enzyme on DNA. J Mol Biol 2000; 303(1):93-110.
    • (2000) J Mol Biol , vol.303 , Issue.1 , pp. 93-110
    • Gowher, H.1    Jeltsch, A.2
  • 28
    • 0023034951 scopus 로고
    • Differences in the kinetic-properties of bamhi endonuclease and methylase with linear dna substrates
    • Nardone G, George J, Chirikjian JG. Differences in the kinetic-properties of BamHI endonuclease and methylase with linear DNA substrates. J Biol Chem 1986; 261(26):2128-2133.
    • (1986) J Biol Chem , vol.261 , Issue.26 , pp. 2128-2133
    • Nardone, G.1    George, J.2    Chirikjian, J.G.3
  • 29
    • 0030736323 scopus 로고    scopus 로고
    • Protein-dna recognition complexes: Conservation of structure and binding energy in the transition state
    • Jen-Jacobson L. Protein-DNA recognition complexes: Conservation of structure and binding energy in the transition state. Biopolymers 1997; 44(2):153-180.
    • (1997) Biopolymers , vol.44 , Issue.2 , pp. 153-180
    • Jen-Jacobson, L.1
  • 30
    • 0031591392 scopus 로고    scopus 로고
    • Specific binding by ecorv endonuclease to its dna recognition site gatatc
    • Engler LE, Welch KK, Jen-Jacobson L. Specific binding by EcoRV endonuclease to its DNA recognition site GATATC. J Mol Biol 1997; 269(1):82-101.
    • (1997) J Mol Biol , vol.269 , Issue.1 , pp. 82-101
    • Engler, L.E.1    Welch, K.K.2    Jen-Jacobson, L.3
  • 31
    • 0032502924 scopus 로고    scopus 로고
    • Role of protein-induced bending in the specificity of dna recognition: Crystal structure of ecorv endonuclease complexed with d (aaagat) + d (atctt)
    • Horton NC, Perona JJ. Role of protein-induced bending in the specificity of DNA recognition: Crystal structure of EcoRV endonuclease complexed with d (AAAGAT) + d (ATCTT). J Mol Biol 1998; 277(4):779-787.
    • (1998) J Mol Biol , vol.277 , Issue.4 , pp. 779-787
    • Horton, N.C.1    Perona, J.J.2
  • 32
    • 0033614808 scopus 로고    scopus 로고
    • Divalent metal dependence of site-specific dna binding by ecorv endonuclease
    • Martin AM, Horton NC, Lusetti S et al Divalent metal dependence of site-specific DNA binding by EcoRV endonuclease. Biochemistry 1999; 38(26):8430-8439.
    • (1999) Biochemistry , vol.38 , Issue.26 , pp. 8430-8439
    • Martin, A.M.1    Horton, N.C.2    Lusetti, S.3
  • 33
    • 0026720055 scopus 로고
    • In vitro specificity of ecori dna methyltransferase
    • Reich NO, Olsen C, Osti F et al In vitro specificity of EcoRI DNA methyltransferase. J Biol Chem 1992; 267(22):15802-15807.
    • (1992) J Biol Chem , vol.267 , Issue.22 , pp. 15802-15807
    • Reich, N.O.1    Olsen, C.2    Osti, F.3
  • 34
    • 33747786756 scopus 로고    scopus 로고
    • Engineered extrahelical base destabilization enhances sequence discrimination of dna methyltransferase m-hhai
    • Youngblood B, Shieh FK, Los Rios S et al Engineered extrahelical base destabilization enhances sequence discrimination of DNA methyltransferase M-HhaI. J Mol Biol 2006; 362(2):334-346.
    • (2006) J Mol Biol , vol.362 , Issue.2 , pp. 334-346
    • Youngblood, B.1    Shieh, F.K.2    Los Rios, S.3
  • 35
    • 33845921607 scopus 로고    scopus 로고
    • Determinants of sequence-specific dna méthylation: Target recognition and catalysis are coupled in m-hhai
    • Youngblood B, Buller F, Reich NO. Determinants of sequence-specific DNA méthylation: Target recognition and catalysis are coupled in M-HhaI. Biochemistry 2006; 45(51):15563-15572.
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15563-15572
    • Youngblood, B.1    Buller, F.2    Reich, N.O.3
  • 36
    • 0026409241 scopus 로고
    • Non-additivity of sequence-specific enzyme-dna interactions in the ecori dna methyltransferase
    • Reich NO, Danzitz MJ. Non-additivity of sequence-specific enzyme-dna interactions in the EcoRI DNA methyltransferase. Nucleic Acids Res 1991; 19(23):6587-6594.
    • (1991) Nucleic Acids Res , vol.19 , Issue.23 , pp. 6587-6594
    • Reich, N.O.1    Danzitz, M.J.2
  • 37
    • 0026623106 scopus 로고
    • Ecori dna methyltransferase dna interactions
    • Reich NO, Danzitz MJ. EcoRI DNA methyltransferase DNA interactions. Biochemistry 1992; 31(7): 1937-1945.
    • (1992) Biochemistry , vol.31 , Issue.7 , pp. 1937-1945
    • Reich, N.O.1    Danzitz, M.J.2
  • 38
    • 0026078020 scopus 로고
    • Stereochemical studies of the c-methylation of deoxycytidine catalyzed by hhal methylase and the n-methylation of deoxyadenosine catalyzed by ecori methylase
    • Ho DK, Wu JC, Santi DV et al Stereochemical studies of the C-methylation of deoxycytidine catalyzed by Hhal methylase and the N-methylation of deoxyadenosine catalyzed by EcoRI methylase. Arch Biochem and Biophys 1991; 284(2):264-269.
    • (1991) Arch Biochem and Biophys , vol.284 , Issue.2 , pp. 264-269
    • Ho, D.K.1    Wu, J.C.2    Santi, D.V.3
  • 39
    • 0037062402 scopus 로고    scopus 로고
    • A theoretical examination of the factors controlling the catalytic efficiency of the dna- (Adenine-n-6)-methyltransferase from thermus aquaticus
    • Newby ZER, Lau EY, Bruice TC. A theoretical examination of the factors controlling the catalytic efficiency of the DNA- (adenine-N-6)-methyltransferase from Thermus aquaticus. Natl Acad Sei USA 2002; 99(12):7922-7927.
    • (2002) Natl Acad Sei USA , vol.99 , Issue.12 , pp. 7922-7927
    • Newby, Z.1    Lau, E.Y.2    Bruice, T.C.3
  • 40
    • 0033516566 scopus 로고    scopus 로고
    • Dna bending by ecori dna methyltransferase accelerates base flipping but compromises specificity
    • Allan BW, Garcia R, Maegley K et al DNA bending by EcoRI DNA methyltransferase accelerates base flipping but compromises specificity. J Biol Chem 1999; 274(27):19269-19275.
    • (1999) J Biol Chem , vol.274 , Issue.27 , pp. 19269-19275
    • Allan, B.W.1    Garcia, R.2    Maegley, K.3
  • 41
    • 4344685527 scopus 로고    scopus 로고
    • Simultaneous dna binding, bending and base flipping—evidence for a novel m-ecori methyltransferase-dna complex
    • Hopkins BB, Reich NO. Simultaneous DNA binding, bending and base flipping—evidence for a novel M-EcoRI methyltransferase-DNA complex. J Biol Chem 2004; 279(35):37049-37060.
    • (2004) J Biol Chem , vol.279 , Issue.35 , pp. 37049-37060
    • Hopkins, B.B.1    Reich, N.O.2
  • 42
    • 33748754248 scopus 로고    scopus 로고
    • Conformational transitions as determinants of specificity for the dna methyltransferase ecori
    • Youngblood B, Reich NO. Conformational transitions as determinants of specificity for the DNA methyltransferase EcoRI. J Biol Chem 2006; 281(37):26821-26831.
    • (2006) J Biol Chem , vol.281 , Issue.37 , pp. 26821-26831
    • Youngblood, B.1    Reich, N.O.2
  • 43
    • 33747689885 scopus 로고    scopus 로고
    • Alteration of sequence specificity of the type ii restriction endonuclease hindi through an indirect readout mechanism
    • Joshi HK, Etzkorn C, Chatwcl] L et al. Alteration of sequence specificity of the type II restriction endonuclease Hindi through an indirect readout mechanism. J Biol Chem 2006; 281(33):23852-23869.
    • (2006) J Biol Chem , vol.281 , Issue.33 , pp. 23852-23869
    • Joshi, H.K.1    Etzkorn, C.2    Chatwcl], L.3
  • 44
    • 0032985826 scopus 로고    scopus 로고
    • Dna repair mechanisms for the recognition and removal of damaged dna bases
    • Mol CD, Parikh SS, Putnam CD et al DNA repair mechanisms for the recognition and removal of damaged DNA bases. Annu Rev Bioph Biom 1999; 28:101-128.
    • (1999) Annu Rev Bioph Biom , vol.28 , pp. 101-128
    • Mol, C.D.1    Parikh, S.S.2    Putnam, C.D.3
  • 45
    • 0030046809 scopus 로고    scopus 로고
    • Intercalation, dna kinking and the control of transcription
    • Werner MH, Gronenbom AM, Clore GM. Intercalation, DNA kinking and the control of transcription. Science 1996; 271(5250):778-784.
    • (1996) Science , vol.271 , Issue.5250 , pp. 778-784
    • Werner, M.H.1    Gronenbom, A.M.2    Clore, G.M.3
  • 46
    • 33646088737 scopus 로고    scopus 로고
    • Structure and substrate recognition of the escherichia coli dna adenine methyltransferase
    • Horton JR, Lieben K, Bekcs M et al. Structure and substrate recognition of the Escherichia coli DNA adenine methyltransferase. J Mol Biol 2006; 358(2):559-570.
    • (2006) J Mol Biol , vol.358 , Issue.2 , pp. 559-570
    • Horton, J.R.1    Lieben, K.2    Bekcs, M.3
  • 47
    • 44349170102 scopus 로고    scopus 로고
    • Differential stabilization of reaction intermediates: Specificity checkpoints for m-ecori revealed by transient fluorescence and fluorescence lifetime studies
    • Youngblood B, Bonnist E, Drydcn DTF et al. Differential stabilization of reaction intermediates: Specificity checkpoints for M-EcoRI revealed by transient fluorescence and fluorescence lifetime studies. Nudeic Acids Res 2008; 36(9):2917-2925.
    • (2008) Nudeic Acids Res , vol.36 , Issue.9 , pp. 2917-2925
    • Youngblood, B.1    Bonnist, E.2    Drydcn, D.3
  • 48
    • 55549109430 scopus 로고    scopus 로고
    • Role of induced fit in enzyme specificity: A molecular forward/reverse switch
    • Johnson KA. Role of induced fit in enzyme specificity: A molecular forward/reverse switch. J Biol Chem2008; 283(39):26297-26301.
    • (2008) J Biol Chem , vol.283 , Issue.39 , pp. 26297-26301
    • Johnson, K.A.1
  • 49
    • 0023273532 scopus 로고
    • Cloning, sequencing, invivo promoter mapping and expression in escherichia-coli of the gene for the hhal methyltransferase
    • Caserta M, Zacharias W, Nwankwo D et al Cloning, sequencing, invivo promoter mapping and expression in Escherichia-coli of the gene for the Hhal methyltransferase. J Biol Chem 1987; 262(10):4770-4777.
    • (1987) J Biol Chem , vol.262 , Issue.10 , pp. 4770-4777
    • Caserta, M.1    Zacharias, W.2    Nwankwo, D.3
  • 50
    • 0028010888 scopus 로고
    • Hhal methyltransferase flips its target base out of the dna helix
    • Klimasauskas S, Kumar S, Roberts RJ et al. Hhal methyltransferase flips its target base out of the DNA helix. Cell 1994; 76(2):357-369.
    • (1994) Cell , vol.76 , Issue.2 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3
  • 51
    • 0031667109 scopus 로고    scopus 로고
    • Structures of hhal methyltransferase complexed with substrates containing mismatches at the target base
    • O’Gara M, Horton JR, Roberts RJ et al Structures of Hhal methyltransferase complexed with substrates containing mismatches at the target base. Nat Struct Biol 1998; 5(10):872-877.
    • (1998) Nat Struct Biol , vol.5 , Issue.10 , pp. 872-877
    • O’Gara, M.1    Horton, J.R.2    Roberts, R.J.3
  • 52
    • 0030575782 scopus 로고    scopus 로고
    • A structural basis for the preferential binding of hcmimcthylated dna by hhal dna methyltransferasc
    • O’Gara M, Roberts RJ, Cheng XD. A structural basis for the preferential binding of hcmimcthylated DNA by Hhal DNA methyltransferasc. J Mol Biol 1996; 263(4):597-606.
    • (1996) J Mol Biol , vol.263 , Issue.4 , pp. 597-606
    • O’Gara, M.1    Roberts, R.J.2    Cheng, X.D.3
  • 53
    • 0030572656 scopus 로고    scopus 로고
    • Enzymatic c5-cytosine méthylation of dna: Mechanistic implications of new crystal structures for hhal methyltransfcrase-dna-adohey complexes
    • O’Gara M, Klimasauskas S, Roberts RJ et al. Enzymatic C5-cytosine méthylation of DNA: Mechanistic implications of new crystal structures for Hhal methyltransfcrase-DNA-AdoHey complexes. J Mol Biol1996; 261(5):634-645.
    • (1996) J Mol Biol , vol.261 , Issue.5 , pp. 634-645
    • O’Gara, M.1    Klimasauskas, S.2    Roberts, R.J.3
  • 54
    • 2942706016 scopus 로고    scopus 로고
    • Structure of the q23/w mutant of hhal dna methyltransferase: An insight into protein-protein interactions
    • Dong AP, Zhou L, Zhang X et al. Structure of the Q23/W mutant of Hhal DNA methyltransferase: an insight into protein-protein interactions. Biol Chem 2004; 385(5):373-379.
    • (2004) Biol Chem , vol.385 , Issue.5 , pp. 373-379
    • Dong, A.P.1    Zhou, L.2    Zhang, X.3
  • 55
    • 31144473532 scopus 로고    scopus 로고
    • Time-resolved fluorescence of 2-aminopurine as a probe of base flipping in m-hhal-dna complexes
    • Neely RK, Daujotyte D, Grazulis S et al Time-resolved fluorescence of 2-aminopurine as a probe of base flipping in M-Hhal-DNA complexes. Nucleic Acids Res 2005; 33(22):6953-6960.
    • (2005) Nucleic Acids Res , vol.33 , Issue.22 , pp. 6953-6960
    • Neely, R.K.1    Daujotyte, D.2
  • 56
    • 33748113136 scopus 로고    scopus 로고
    • The role of arg165 towards base flipping, base stabilization and catalysis in m-hhai
    • Shieh FK, Youngblood B. Reich NO. The role of Arg165 towards base flipping, base stabilization and catalysis in M-HhaI. J Mol Biol 2006; 362(3):516-527.
    • (2006) J Mol Biol , vol.362 , Issue.3 , pp. 516-527
    • Shieh, F.K.1    Youngblood, B.2    Reich, N.O.3
  • 57
    • 35148870830 scopus 로고    scopus 로고
    • Adomet-dependent methyl-transfer: Glu (119) is essential for dna c5-cytosine methyltransferase m-hhai
    • Shieh FK, Reich NO. AdoMet-dependent methyl-transfer: Glu (119) is essential for DNA C5-cytosine methyltransferase M-HhaI. J Mol Biol 2007; 373(5):1157-1168.
    • (2007) J Mol Biol , vol.373 , Issue.5 , pp. 1157-1168
    • Shieh, F.K.1    Reich, N.O.2
  • 58
    • 0034624023 scopus 로고    scopus 로고
    • Functional roles of the conserved threonine 250 in the target recognition domain of hhal dna methyltransferase
    • Vilkaitis G, Dong AP, Weinhold E et al Functional roles of the conserved threonine 250 in the target recognition domain of Hhal DNA methyltransferase. J Biol Chem 2000; 275(49):38722-38730.
    • (2000) J Biol Chem , vol.275 , Issue.49 , pp. 38722-38730
    • Vilkaitis, G.1    Dong, A.P.2    Weinhold, E.3
  • 59
    • 34547618276 scopus 로고    scopus 로고
    • S-adenosyl-l-methionine-dependent methyl transfer: Observable precatalytic intermediates during dna cytosine méthylation
    • Youngblood B, Shieh FK, Buller F et al. S-Adenosyl-L-methionine-dependent methyl transfer: Observable precatalytic intermediates during DNA cytosine méthylation. Biochemistry 2007; 46(30):8766-8775.
    • (2007) Biochemistry , vol.46 , Issue.30 , pp. 8766-8775
    • Youngblood, B.1    Shieh, F.K.2    Buller, F.3
  • 60
    • 3242714355 scopus 로고    scopus 로고
    • Caught in the act: Visualization of an intermediate in the dna base-flipping pathway induced by hhal methyltransferase
    • Horton JR, Ratncr G, Banavali NK et al Caught in the act: visualization of an intermediate in the DNA base-flipping pathway induced by Hhal methyltransferase. Nucleic Acids Res 2004; 32(13):3877-3886.
    • (2004) Nucleic Acids Res , vol.32 , Issue.13 , pp. 3877-3886
    • Horton, J.R.1    Ratncr, G.2    Banavali, N.K.3
  • 61
    • 33845971526 scopus 로고    scopus 로고
    • Observing an induced-fit mechanism during sequence-specific dna méthylation
    • Estabrook RA, Reich N. Observing an induced-fit mechanism during sequence-specific DNA méthylation. J Biol Chem 2006; 281(48):37205-37214.
    • (2006) J Biol Chem , vol.281 , Issue.48 , pp. 37205-37214
    • Estabrook, R.A.1    Reich, N.2
  • 62
    • 0032519379 scopus 로고    scopus 로고
    • 2-aminopurinc as a fluorescent probe for dna base flipping by methyl transferases
    • Holz B, Klimasauskas S, Serva S et al 2-Aminopurinc as a fluorescent probe for DNA base flipping by methyl transferases. Nucleic Acids Res 1998; 26(4): 1076-1083.
    • (1998) Nucleic Acids Res , vol.26 , Issue.4 , pp. 1076-1083
    • Holz, B.1    Klimasauskas, S.2
  • 63
    • 0033569621 scopus 로고    scopus 로고
    • Active site dynamics of the hhal methylt ransferase: Insights from computer simulation
    • Lau EY, Bruicc TC. Active site dynamics of the Hhal methylt ransferase: Insights from computer simulation. J Mol Biol 1999; 293(1):9-18.
    • (1999) J Mol Biol , vol.293 , Issue.1 , pp. 9-18
    • Lau, E.Y.1    Bruicc, T.C.2
  • 64
    • 14844364378 scopus 로고    scopus 로고
    • Residues distal from the active site that alter enzyme function in m-hhai. Dna cytosine methyltransferase
    • Sharma V, Youngblood B, Reich N. Residues distal from the active site that alter enzyme function in M-HhaI. DNA cytosine methyltransferase. J Biomol Struc and Dyn 2005; 22(5):533-543.
    • (2005) J Biomol Struc and Dyn , vol.22 , Issue.5 , pp. 533-543
    • Sharma, V.1    Youngblood, B.2    Reich, N.3
  • 65
    • 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 RA, Lipson R, Hopkins B et al The coupling of tight DNA binding and base flipping—identification of a conserved structural motif in base flipping enzymes. J Biol Chem 2004; 279(30):31419-31428.
    • (2004) J Biol Chem , vol.279 , Issue.30 , pp. 31419-31428
    • Estabrook, R.A.1    Lipson, R.2    Hopkins, B.3
  • 66
    • 0033605827 scopus 로고    scopus 로고
    • Structure of a binary complex of hhal methyltransferasc with s-adenosyl-l-methionine formed in the presence of a short nonspecific dna oligonucleotide
    • O’Gara M, Zhang X, Roberts RJ et al. Structure of a binary complex of Hhal methyltransferasc with S-adenosyl-L-methionine formed in the presence of a short nonspecific DNA oligonucleotide. J Mol Biol1999; 287(2):201-209.
    • (1999) J Mol Biol , vol.287 , Issue.2 , pp. 201-209
    • O’Gara, M.1    Zhang, X.2    Roberts, R.J.3
  • 68
    • 12844268072 scopus 로고    scopus 로고
    • Statistical co-evolution analysis and molecular dynamics: Identification of amino acid pairs essential for catalysis
    • Estabrook RA, Luo J, Purdy MM et al Statistical co-evolution analysis and molecular dynamics: Identification of amino acid pairs essential for catalysis. Natl Acad Sci USA 2005; 102(4):994-999.
    • (2005) Natl Acad Sci USA , vol.102 , Issue.4 , pp. 994-999
    • Estabrook, R.A.1    Luo, J.2    Purdy, M.M.3
  • 69
    • 34250839422 scopus 로고    scopus 로고
    • Long-range structural and dynamical changes induced by cofactor binding in dna methyltransferasc m-hhai
    • Zhou HJ, Shatz W, Purdy MM et al Long-range structural and dynamical changes induced by cofactor binding in DNA methyltransferasc M-HhaI. Biochemistry 2007; 46(24):7261-7268.
    • (2007) Biochemistry , vol.46 , Issue.24 , pp. 7261-7268
    • Zhou, H.J.1    Shatz, W.2    Purdy, M.M.3
  • 70
    • 0038576427 scopus 로고    scopus 로고
    • Solubility engineering of the hhal methyltransferase
    • Daujotyte D, Vilkaitis G, Manelyte L et al Solubility engineering of the Hhal methyltransferase. Protein Eng 2003; 16(4):295-301.
    • (2003) Protein Eng , vol.16 , Issue.4 , pp. 295-301
    • Daujotyte, D.1    Vilkaitis, G.2    Manelyte, L.3
  • 71
    • 0842313326 scopus 로고    scopus 로고
    • Altering the sequence specificity of haelq methyltransferase by directed evolution using in vitro compartmcntalization
    • Cohen HM, Tawfik DS, Griffiths AD. Altering the sequence specificity of HaelQ methyltransferase by directed evolution using in vitro compartmcntalization. Protein Engineering Design and Selection 2004; 17(1):3-11.
    • (2004) Protein Engineering Design and Selection , vol.17 , Issue.1 , pp. 3-11
    • Cohen, H.M.1    Tawfik, D.S.2    Griffiths, A.D.3
  • 72
    • 0036714679 scopus 로고    scopus 로고
    • Promiscuous méthylation of noncanonical dna sites by haciii methyltransferase
    • Cohen HM, Tawfik DS, Griffiths AD. Promiscuous méthylation of noncanonical DNA sites by HacIII methyltransferase. Nucleic Adds Res 2002; 30(17):3880-3885.
    • (2002) Nucleic Adds Res , vol.30 , Issue.17 , pp. 3880-3885
    • Cohen, H.M.1    Tawfik, D.S.2    Griffiths, A.D.3
  • 73
    • 0032510667 scopus 로고    scopus 로고
    • Directed evolution of an aspartate aminotransferase with new substrate specificities
    • Yano T, Ouc S, Kagamiyama H. Directed evolution of an aspartate aminotransferase with new substrate specificities. Nad Acad Sci USA 1998; 95(10):5511-5515.
    • (1998) Nad Acad Sci USA , vol.95 , Issue.10 , pp. 5511-5515
    • Yano, T.1    Ouc, S.2    Kagamiyama, H.3
  • 74
    • 33745278855 scopus 로고    scopus 로고
    • Computational redesign of endonuclease dna binding and cleavage specificity
    • Ashworth J, Havranek JJ, Duarte CM et al Computational redesign of endonuclease DNA binding and cleavage specificity. Nature 2006; 441(7093):656-659.
    • (2006) Nature , vol.441 , Issue.7093 , pp. 656-659
    • Ashworth, J.1    Havranek, J.J.2    Duarte, C.M.3
  • 75
    • 4544260271 scopus 로고    scopus 로고
    • Sequence-specific mcthyltransferase-induced labeling of dna (Smiling dna)
    • Pljevaljcic G, Schmidt F, Weinhold E. Sequence-specific mcthyltransferase-induced labeling of DNA (SMILing DNA). Chembiochem 2004; 5(3):265-269.
    • (2004) Chembiochem , vol.5 , Issue.3 , pp. 265-269
    • Pljevaljcic, G.1    Schmidt, F.2    Weinhold, E.3
  • 76
    • 4644330069 scopus 로고    scopus 로고
    • Sequence-specific dna labeling using mcthyltransferascs
    • Pljevaljcic G, Schmidt F, Peschlow A et al. Sequence-specific DNA labeling using mcthyltransferascs. Method Mol Biol 2004; 283:145-161.
    • (2004) Method Mol Biol , vol.283 , pp. 145-161
    • Pljevaljcic, G.1    Schmidt, F.2    Peschlow, A.3
  • 77
    • 39749156358 scopus 로고    scopus 로고
    • Molecular scale architecture: Engineered three- and four-way junctions
    • Wilkinson S, Diechtierow M, Estabrook RA et al Molecular scale architecture: Engineered three- and four-way junctions. Bioconjugate Chem 2008; 19(2):470-475.
    • (2008) Bioconjugate Chem , vol.19 , Issue.2 , pp. 470-475
    • Wilkinson, S.1    Diechtierow, M.2    Estabrook, R.A.3
  • 78
    • 39749171718 scopus 로고    scopus 로고
    • Enzyme-directed positioning of nanoparticles on large dna templates
    • Braun G, Dicchrierow M, Wilkinson S et al Enzyme-directed positioning of nanoparticles on large DNA templates. Bioconjugate Chem 2008; 19(2):476-479.
    • (2008) Bioconjugate Chem , vol.19 , Issue.2 , pp. 476-479
    • Braun, G.1    Dicchrierow, M.2    Wilkinson, S.3
  • 79
    • 56149090684 scopus 로고    scopus 로고
    • Epi-drugs to fight cancer: From chemistry to cancer treatment, the toad ahead
    • Mai A, Altucci L. Epi-drugs to fight cancer: from chemistry to cancer treatment, the toad ahead The International J Biochem Cell Biol 2008; doi:10.1016/j.biocel.2008.08.020.
    • (2008) The International J Biochem Cell Biol
    • Mai, A.1    Altucci, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.