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Volumn 32, Issue 7, 2004, Pages 2223-2230

Unusual 2-aminopurine fluorescence from a complex of DNA and the EcoKI methyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINOPURINE; ADENINE; CYTOSINE; DNA; GUANIDINE; METHYLTRANSFERASE; NUCLEOTIDE; S ADENOSYLMETHIONINE; THYMINE; TYPE II SITE SPECIFIC DEOXYRIBONUCLEASE; DNA BINDING PROTEIN; DNA MODIFICATION METHYLASE ECOKI; SITE SPECIFIC DNA METHYLTRANSFERASE (ADENINE SPECIFIC);

EID: 2342479085     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh531     Document Type: Article
Times cited : (28)

References (51)
  • 1
    • 0014669561 scopus 로고
    • Fluorescence studies of nucleotides and polynucleotides. I. Formycin, 2-aminopurine riboside, 2,6-diaminopurine riboside and their derivatives
    • Ward,D.C., Reich,E. and Stryer,L. (1969) Fluorescence studies of nucleotides and polynucleotides. I. Formycin, 2-aminopurine riboside, 2,6-diaminopurine riboside and their derivatives. J. Biol. Chem., 244, 1228-1237.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1228-1237
    • Ward, D.C.1    Reich, E.2    Stryer, L.3
  • 2
    • 0031011001 scopus 로고    scopus 로고
    • Electronic transition moments of 2-aminopurine
    • Holmen,A., Norden,B. and Albinsson,B. (1997) Electronic transition moments of 2-aminopurine. J. Am. Chem. Soc., 119, 3114-3121.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3114-3121
    • Holmen, A.1    Norden, B.2    Albinsson, B.3
  • 3
    • 0000182297 scopus 로고    scopus 로고
    • Theoretical study of the excited state properties and transitions of 2-aminopurine in the gas phase and in solution
    • Jean,J.M. and Hall,K.B. (2000) Theoretical study of the excited state properties and transitions of 2-aminopurine in the gas phase and in solution. J. Phys. Chem. A, 104, 1930-1937.
    • (2000) J. Phys. Chem. A , vol.104 , pp. 1930-1937
    • Jean, J.M.1    Hall, K.B.2
  • 4
    • 0035969959 scopus 로고    scopus 로고
    • Probing structure and dynamics of DNA with 2-aminopurine: Effects of local environment on fluorescence
    • Rachofsky,E.L., Osman,R. and Ross,J.B. (2001) Probing structure and dynamics of DNA with 2-aminopurine: effects of local environment on fluorescence. Biochemistry, 40, 946-956.
    • (2001) Biochemistry , vol.40 , pp. 946-956
    • Rachofsky, E.L.1    Osman, R.2    Ross, J.B.3
  • 6
    • 0033555454 scopus 로고    scopus 로고
    • Electron transfer between bases in double helical DNA
    • Kelley,S.O. and Barton,J.K. (1999) Electron transfer between bases in double helical DNA. Science, 283, 375-381.
    • (1999) Science , vol.283 , pp. 375-381
    • Kelley, S.O.1    Barton, J.K.2
  • 8
    • 0035793105 scopus 로고    scopus 로고
    • 2-Aminopurine fluorescence quenching and lifetimes: Role of base stacking
    • Jean,J.M. and Hall,K.B. (2001) 2-Aminopurine fluorescence quenching and lifetimes: Role of base stacking. Proc. Natl Acad. Sci. USA, 98, 37-41.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 37-41
    • Jean, J.M.1    Hall, K.B.2
  • 9
    • 0037168485 scopus 로고    scopus 로고
    • Effects of strand and directional asymmetry on base-base coupling and charge transfer in double-helical DNA
    • O'Neill,M.A. and Barton,J.K. (2002) Effects of strand and directional asymmetry on base-base coupling and charge transfer in double-helical DNA. Proc. Natl Acad. Sci. USA, 99, 16543-16550.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16543-16550
    • O'Neill, M.A.1    Barton, J.K.2
  • 10
    • 0023651409 scopus 로고
    • Base pair opening dynamics of a 2-aminopurine substituted EcoRI restriction sequence and its unsubstituted counterpart in oligonucleotides
    • Lycksell,P.O., Graslund,A., Claesens,F., McLaughlin,L.W., Larsson,U. and Rigler,R. (1987) Base pair opening dynamics of a 2-aminopurine substituted EcoRI restriction sequence and its unsubstituted counterpart in oligonucleotides. Nucleic Acids Res., 15, 9011-9025.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 9011-9025
    • Lycksell, P.O.1    Graslund, A.2    Claesens, F.3    McLaughlin, L.W.4    Larsson, U.5    Rigler, R.6
  • 11
    • 0028128641 scopus 로고
    • Melting and premelting transitions of an oligomer measured by DNA base fluorescence and absorption
    • Xu,D., Evans,K.O. and Nordlund,T.M. (1994) Melting and premelting transitions of an oligomer measured by DNA base fluorescence and absorption. Biochemistry, 33, 9592-9599.
    • (1994) Biochemistry , vol.33 , pp. 9592-9599
    • Xu, D.1    Evans, K.O.2    Nordlund, T.M.3
  • 12
    • 0029758746 scopus 로고    scopus 로고
    • Spectroscopic and calorimetric characterizations of DNA duplexes containing 2-aminopurine
    • Law,S.M., Eritja,R., Goodman,M.F. and Breslauer,K.J. (1996) Spectroscopic and calorimetric characterizations of DNA duplexes containing 2-aminopurine. Biochemistry, 35, 12329-12337.
    • (1996) Biochemistry , vol.35 , pp. 12329-12337
    • Law, S.M.1    Eritja, R.2    Goodman, M.F.3    Breslauer, K.J.4
  • 13
    • 0030448581 scopus 로고    scopus 로고
    • Targeted base stacking disruption by the EcoRI DNA methyltransferase
    • Allan,B.W. and Reich,N.O. (1996) Targeted base stacking disruption by the EcoRI DNA methyltransferase. Biochemistry, 35, 14757-14762.
    • (1996) Biochemistry , vol.35 , pp. 14757-14762
    • Allan, B.W.1    Reich, N.O.2
  • 14
    • 0030766474 scopus 로고    scopus 로고
    • The role of base flipping in damage recognition and catalysis by T4 endonuclease V
    • McCullough,A.K., Dodson,M.L., Scharer,O.D. and Lloyd,R.S. (1997) The role of base flipping in damage recognition and catalysis by T4 endonuclease V. J. Biol. Chem., 272, 27210-27217.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27210-27217
    • McCullough, A.K.1    Dodson, M.L.2    Scharer, O.D.3    Lloyd, R.S.4
  • 15
    • 0032516443 scopus 로고    scopus 로고
    • Exonuclease-polymerase active site partitioning of primer-template DNA strands and equilibrium Mg2+ binding properties of bacteriophage T4 DNA polymerase
    • Beechem,J.M., Otto,M.R., Bloom,L.B., Eritja,R., Reha-Krantz,L.J. and Goodman,M.F. (1998) Exonuclease-polymerase active site partitioning of primer-template DNA strands and equilibrium Mg2+ binding properties of bacteriophage T4 DNA polymerase. Biochemistry, 37, 10144-10155.
    • (1998) Biochemistry , vol.37 , pp. 10144-10155
    • Beechem, J.M.1    Otto, M.R.2    Bloom, L.B.3    Eritja, R.4    Reha-Krantz, L.J.5    Goodman, M.F.6
  • 16
    • 0032519379 scopus 로고    scopus 로고
    • 2-Aminopurine as a fluorescent probe for DNA base flipping by methyltransferases
    • Holz,B., Klimasauskas,S., Serva,S. and Weinhold,E. (1998) 2-Aminopurine as a fluorescent probe for DNA base flipping by methyltransferases. Nucleic Acids Res., 26, 1076-1083.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1076-1083
    • Holz, B.1    Klimasauskas, S.2    Serva, S.3    Weinhold, E.4
  • 17
    • 0032529485 scopus 로고    scopus 로고
    • 2-Aminopurine fluorescence studies of base stacking interactions at abasic sites in DNA: Metal-ion and base sequence effects
    • Stivers,J.T. (1998) 2-Aminopurine fluorescence studies of base stacking interactions at abasic sites in DNA: metal-ion and base sequence effects. Nucleic Acids Res., 26, 3837-3844.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3837-3844
    • Stivers, J.T.1
  • 18
    • 0033609041 scopus 로고    scopus 로고
    • Measurement of the absolute temporal coupling between DNA binding and base flipping
    • Allan,B.W., Reich,N.O. and Beechem,J.M. (1999) Measurement of the absolute temporal coupling between DNA binding and base flipping. Biochemistry, 38, 5308-5314.
    • (1999) Biochemistry , vol.38 , pp. 5308-5314
    • Allan, B.W.1    Reich, N.O.2    Beechem, J.M.3
  • 19
    • 0033514427 scopus 로고    scopus 로고
    • Functional roles of the conserved aromatic amino acid residues at position 108 (Motif IV) and position 196 (Motif VIII) in base flipping and catalysis by the N6-adenine DNA methyltransferase from Thermus aquaticus
    • Pues,H., Bleimling,N., Holz,B., Wolcke,J. and Weinhold,E. (1999) Functional roles of the conserved aromatic amino acid residues at position 108 (Motif IV) and position 196 (Motif VIII) in base flipping and catalysis by the N6-adenine DNA methyltransferase from Thermus aquaticus. Biochemistry, 38, 1426-1434.
    • (1999) Biochemistry , vol.38 , pp. 1426-1434
    • Pues, H.1    Bleimling, N.2    Holz, B.3    Wolcke, J.4    Weinhold, E.5
  • 20
    • 0033579953 scopus 로고    scopus 로고
    • Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase
    • Stivers,J.T., Pankiewicz,K.W. and Watanabe,K.A. (1999) Kinetic mechanism of damage site recognition and uracil flipping by Escherichia coli uracil DNA glycosylase. Biochemistry, 38, 952-963.
    • (1999) Biochemistry , vol.38 , pp. 952-963
    • Stivers, J.T.1    Pankiewicz, K.W.2    Watanabe, K.A.3
  • 21
    • 0034644729 scopus 로고    scopus 로고
    • Molecular enzymology of the EcoRV DNA-(Adenine-N (6))-methyltransferase: Kinetics of DNA binding and bending, kinetic mechanism and linear diffusion of the enzyme on DNA
    • Gowher,H. and Jeltsch,A. (2000) Molecular enzymology of the EcoRV DNA-(Adenine-N (6))-methyltransferase: kinetics of DNA binding and bending, kinetic mechanism and linear diffusion of the enzyme on DNA. J. Mol. Biol., 303, 93-110.
    • (2000) J. Mol. Biol. , vol.303 , pp. 93-110
    • Gowher, H.1    Jeltsch, A.2
  • 22
    • 0034326920 scopus 로고    scopus 로고
    • Pre-steady state kinetics of bacteriophage T4 dam DNA-[N(6)-adenine] methyltransferase: Interaction with native (GATC) or modified sites
    • Malygin,E.G., Lindstrom,W.M.,Jr, Schlagman,S.L., Hattman,S. and Reich,N.O. (2000) Pre-steady state kinetics of bacteriophage T4 dam DNA-[N(6)-adenine] methyltransferase: interaction with native (GATC) or modified sites. Nucleic Acids Res., 28, 4207-4211.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4207-4211
    • Malygin, E.G.1    Lindstrom Jr., W.M.2    Schlagman, S.L.3    Hattman, S.4    Reich, N.O.5
  • 23
    • 0034640127 scopus 로고    scopus 로고
    • Binding of EcoP151 DNA methyltransferase to DNA reveals a large structural distortion within the recognition sequence
    • Reddy,Y.V. and Rao,D.N. (2000) Binding of EcoP151 DNA methyltransferase to DNA reveals a large structural distortion within the recognition sequence. J. Mol. Biol., 298, 597-610.
    • (2000) J. Mol. Biol. , vol.298 , pp. 597-610
    • Reddy, Y.V.1    Rao, D.N.2
  • 24
    • 0034667760 scopus 로고    scopus 로고
    • Substrate binding in vitro and kinetics of RsrI [N6-adenine] DNA methyltransferase
    • Szegedi,S.S., Reich,N.O. and Gumport,R.I. (2000) Substrate binding in vitro and kinetics of RsrI [N6-adenine] DNA methyltransferase. Nucleic Acids Res., 28, 3962-3971.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3962-3971
    • Szegedi, S.S.1    Reich, N.O.2    Gumport, R.I.3
  • 25
    • 0034624023 scopus 로고    scopus 로고
    • Functional roles of the conserved threonine 250 in the target recognition domain of HhaI DNA methyltransferase
    • Vilkaitis,G., Dong,A., Weinhold,E., Cheng,X. and Klimasauskas,S. (2000) Functional roles of the conserved threonine 250 in the target recognition domain of HhaI DNA methyltransferase. J. Biol. Chem., 275, 38722-38730.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38722-38730
    • Vilkaitis, G.1    Dong, A.2    Weinhold, E.3    Cheng, X.4    Klimasauskas, S.5
  • 26
    • 0347752416 scopus 로고    scopus 로고
    • Peculiar 2-aminopurine fluorescence monitors the dynamics of open complex formation by bacteriophage T7 RNA polymerase
    • Bandwar,R.P. and Patel,S.S. (2001) Peculiar 2-aminopurine fluorescence monitors the dynamics of open complex formation by bacteriophage T7 RNA polymerase. J. Biol. Chem., 276, 14075-14082.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14075-14082
    • Bandwar, R.P.1    Patel, S.S.2
  • 27
    • 0035969981 scopus 로고    scopus 로고
    • Conformation and dynamics of abasic sites in DNA investigated by time-resolved fluorescence of 2-aminopurine
    • Rachofsky,E.L., Seibert,E., Stivers,J.T., Osman,R. and Ross,J.B. (2001) Conformation and dynamics of abasic sites in DNA investigated by time-resolved fluorescence of 2-aminopurine. Biochemistry, 40, 957-967.
    • (2001) Biochemistry , vol.40 , pp. 957-967
    • Rachofsky, E.L.1    Seibert, E.2    Stivers, J.T.3    Osman, R.4    Ross, J.B.5
  • 28
    • 0037016053 scopus 로고    scopus 로고
    • Probing the DNA interface of the EcoRV DNA-(adenine-N6)-methyltransferase by site-directed mutagenesis, fluorescence spectroscopy and UV cross-linking
    • Beck,C. and Jeltsch,A. (2002) Probing the DNA interface of the EcoRV DNA-(adenine-N6)-methyltransferase by site-directed mutagenesis, fluorescence spectroscopy and UV cross-linking. Biochemistry, 41, 14103-14110.
    • (2002) Biochemistry , vol.41 , pp. 14103-14110
    • Beck, C.1    Jeltsch, A.2
  • 29
    • 0037080166 scopus 로고    scopus 로고
    • Direct measurement of single-stranded DNA translocation by PcrA helicase using the fluorescent base analogue 2-aminopurine
    • Dillingham,M.S., Wigley,D.B. and Webb,M.R. (2002) Direct measurement of single-stranded DNA translocation by PcrA helicase using the fluorescent base analogue 2-aminopurine. Biochemistry, 41, 643-651.
    • (2002) Biochemistry , vol.41 , pp. 643-651
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 30
    • 0037006992 scopus 로고    scopus 로고
    • Using 2-aminopurine fluorescence to detect base unstacking in the template strand during nucleotide incorporation by the bacteriophage T4 DNA polymerase
    • Mandal,S.S., Fidalgo da Silva,E. and Reha-Krantz,L.J. (2002) Using 2-aminopurine fluorescence to detect base unstacking in the template strand during nucleotide incorporation by the bacteriophage T4 DNA polymerase. Biochemistry, 41, 4399-4406.
    • (2002) Biochemistry , vol.41 , pp. 4399-4406
    • Mandal, S.S.1    Fidalgo da Silva, E.2    Reha-Krantz, L.J.3
  • 31
    • 0000010735 scopus 로고    scopus 로고
    • Bacterial DNA methyltransferases
    • Cheng,X. and Blumenthal,R.M. (eds), World Scientific Publishing, Singapore
    • Dryden,D.T.F. (1999) Bacterial DNA methyltransferases. In Cheng,X. and Blumenthal,R.M. (eds), S-Adenosylmethionine-dependent Methyltransferases: Structures and Functions. World Scientific Publishing, Singapore, pp. 283-340.
    • (1999) S-Adenosylmethionine-dependent Methyltransferases: Structures and Functions , pp. 283-340
    • Dryden, D.T.F.1
  • 32
    • 0035883736 scopus 로고    scopus 로고
    • AdoMet-dependent methylation, DNA methyltransferases and base flipping
    • Cheng,X. and Roberts,R.J. (2001) AdoMet-dependent methylation, DNA methyltransferases and base flipping. Nucleic Acids Res., 29, 3784-3795.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3784-3795
    • Cheng, X.1    Roberts, R.J.2
  • 33
    • 0028010888 scopus 로고
    • Hhal methyltransferase flips its target base out of the DNA helix
    • Klimasauskas,S., Kumar,S., Roberts,R.J. and Cheng,X. (1994) Hhal methyltransferase flips its target base out of the DNA helix. Cell, 76, 357-369.
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 34
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • Savva,R., McAuley-Hecht,K., Brown,T. and Pearl,L. (1995) The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature, 373, 487-493.
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 35
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • Slupphaug,G., Mol,C.D., Kavli,B., Arvai,A.S., Krokan,H.E. and Tainer,J.A. (1996) A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature, 384, 87-92.
    • (1996) Nature , vol.384 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavli, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 36
    • 0034746572 scopus 로고    scopus 로고
    • Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with DNA and a cofactor analog
    • Goedecke,K., Pignot,M., Goody,R.S., Scheidig,A.J. and Weinhold,E. (2001) Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with DNA and a cofactor analog. Nat. Struct. Biol., 8, 121-125.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 121-125
    • Goedecke, K.1    Pignot, M.2    Goody, R.S.3    Scheidig, A.J.4    Weinhold, E.5
  • 37
    • 0034130457 scopus 로고    scopus 로고
    • Type I restriction systems: Sophisticated molecular machines
    • Murray,N.E. (2000) Type I restriction systems: sophisticated molecular machines. Microbiol. Mol. Biol. Rev., 64, 412-434.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 412-434
    • Murray, N.E.1
  • 38
    • 0035883536 scopus 로고    scopus 로고
    • Nucleoside triphosphate-dependent restriction enzymes
    • Dryden,D.T., Murray,N.E. and Rao,D.N. (2001) Nucleoside triphosphate-dependent restriction enzymes. Nucleic Acids Res., 29, 3728-3741.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3728-3741
    • Dryden, D.T.1    Murray, N.E.2    Rao, D.N.3
  • 39
    • 0347519281 scopus 로고    scopus 로고
    • Tracking EcoKI and DNA fifty years on: A golden story full of surprises
    • Loenen,W.A. (2003) Tracking EcoKI and DNA fifty years on: a golden story full of surprises. Nucleic Acids Res., 31, 7059-7069.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 7059-7069
    • Loenen, W.A.1
  • 40
    • 0025886886 scopus 로고
    • Mutations that confer de novo activity upon a maintenance methyltransferase
    • Kelleher,J.E., Daniel,A.S. and Murray,N.E. (1991) Mutations that confer de novo activity upon a maintenance methyltransferase. J. Mol. Biol., 221, 431-440.
    • (1991) J. Mol. Biol. , vol.221 , pp. 431-440
    • Kelleher, J.E.1    Daniel, A.S.2    Murray, N.E.3
  • 41
    • 0029353607 scopus 로고
    • Structural modelling of a type I DNA methyltransferase
    • Dryden,D.T.F., Sturrock,S.S. and Winter,M. (1995) Structural modelling of a type I DNA methyltransferase. Nat. Struct. Biol., 2, 632-635.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 632-635
    • Dryden, D.T.F.1    Sturrock, S.S.2    Winter, M.3
  • 42
    • 0028074254 scopus 로고
    • A mutational analysis of the two motifs common to adenine methyltransferases
    • Willcock,D.F., Dryden,D.T.F. and Murray,N.E. (1994) A mutational analysis of the two motifs common to adenine methyltransferases. EMBO J., 13, 3902-3908.
    • (1994) EMBO J. , vol.13 , pp. 3902-3908
    • Willcock, D.F.1    Dryden, D.T.F.2    Murray, N.E.3
  • 43
    • 0030457882 scopus 로고    scopus 로고
    • High resolution footprinting of a type I methyltransferase reveals a large structural distortion within the DNA recognition site
    • Mernagh,D.R. and Kneale,G.G. (1996) High resolution footprinting of a type I methyltransferase reveals a large structural distortion within the DNA recognition site. Nucleic Acids Res., 24, 4853-4858.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4853-4858
    • Mernagh, D.R.1    Kneale, G.G.2
  • 44
    • 0032535247 scopus 로고    scopus 로고
    • Interaction of the type I methyltransferase M.EcoR124I with modified DNA substrates: Sequence discrimination and base flipping
    • Mernagh,D.R., Taylor,I.A. and Kneale,G.G. (1998) Interaction of the type I methyltransferase M.EcoR124I with modified DNA substrates: sequence discrimination and base flipping. Biochem. J., 336, 719-725.
    • (1998) Biochem. J. , vol.336 , pp. 719-725
    • Mernagh, D.R.1    Taylor, I.A.2    Kneale, G.G.3
  • 45
    • 0027497325 scopus 로고
    • Purification and characterization of the methyltransferase from the type 1 restriction and modification system of Escherichia coli K12
    • Dryden,D.T.F., Cooper,L.P. and Murray,N.E. (1993) Purification and characterization of the methyltransferase from the type 1 restriction and modification system of Escherichia coli K12. J. Biol. Chem., 268, 13228-13236.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13228-13236
    • Dryden, D.T.F.1    Cooper, L.P.2    Murray, N.E.3
  • 46
    • 0031049939 scopus 로고    scopus 로고
    • The in vitro assembly of the EcoKI type I DNA restriction/modification enzyme and its in vivo implications
    • Dryden,D.T.F., Cooper,L.P., Thorpe,P.H. and Byron,O. (1997) The in vitro assembly of the EcoKI type I DNA restriction/modification enzyme and its in vivo implications. Biochemistry, 36, 1065-1076.
    • (1997) Biochemistry , vol.36 , pp. 1065-1076
    • Dryden, D.T.F.1    Cooper, L.P.2    Thorpe, P.H.3    Byron, O.4
  • 47
    • 0034112434 scopus 로고    scopus 로고
    • Biotin-avidin microplate assay for the quantitative analysis of enzymatic methylation of DNA by DNA methyltransferases
    • Roth,M. and Jeltsch,A. (2000) Biotin-avidin microplate assay for the quantitative analysis of enzymatic methylation of DNA by DNA methyltransferases. Biol. Chem., 381, 269-272.
    • (2000) Biol. Chem. , vol.381 , pp. 269-272
    • Roth, M.1    Jeltsch, A.2
  • 48
    • 0035970296 scopus 로고    scopus 로고
    • Target recognition by EcoKI: The recognition domain is robust and restriction-deficiency commonly results from the proteolytic control of enzyme activity
    • O'Neill,M., Powell,L.M. and Murray,N.E. (2001) Target recognition by EcoKI: the recognition domain is robust and restriction-deficiency commonly results from the proteolytic control of enzyme activity. J. Mol. Biol., 307, 951-963.
    • (2001) J. Mol. Biol. , vol.307 , pp. 951-963
    • O'Neill, M.1    Powell, L.M.2    Murray, N.E.3
  • 49
    • 0029968248 scopus 로고    scopus 로고
    • The type I restriction endonuclease R.EcoR124I: Over-production and biochemical properties
    • Janscak,P., Abadjieva,A. and Firman,K. (1996) The type I restriction endonuclease R.EcoR124I: over-production and biochemical properties. J. Mol. Biol., 257, 977-991.
    • (1996) J. Mol. Biol. , vol.257 , pp. 977-991
    • Janscak, P.1    Abadjieva, A.2    Firman, K.3
  • 50
    • 0030851906 scopus 로고    scopus 로고
    • A prediction of the amino acids and structures involved in DNA recognition by type I DNA restriction and modification enzymes
    • Sturrock,S.S. and Dryden,D.T.F. (1997) A prediction of the amino acids and structures involved in DNA recognition by type I DNA restriction and modification enzymes. Nucleic Acids Res., 25, 3408-3414.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3408-3414
    • Sturrock, S.S.1    Dryden, D.T.F.2
  • 51
    • 84962407600 scopus 로고    scopus 로고
    • Ab initio MP2 and DFT calculations of geometry and solution tautomerism of purine and some purine derivatives
    • Broo,A. and Holmén,A. (1996) Ab initio MP2 and DFT calculations of geometry and solution tautomerism of purine and some purine derivatives. Chem. Phys. 211, 147-161.
    • (1996) Chem. Phys. , vol.211 , pp. 147-161
    • Broo, A.1    Holmén, A.2


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