메뉴 건너뛰기




Volumn 275, Issue 5, 1998, Pages 747-758

Kinetics of methylation and binding of DNA by the EcoRV adenine-n6 methyltransferase

Author keywords

Conformational change; Enzyme mechanism; Protein nucleic acid interaction; Restriction modification system; Specific DNA binding

Indexed keywords

ADENINE; DNA; DNA METHYLTRANSFERASE; THYMIDINE;

EID: 0032488961     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1492     Document Type: Article
Times cited : (44)

References (50)
  • 1
    • 0028143223 scopus 로고
    • Interaction of EcoP15I DNA methyltransferase with oligonucleotides containing the asymmetric sequence 5′-CAGCAG-3′
    • Ahmad, I. & Rao, D. N. (1994). Interaction of EcoP15I DNA methyltransferase with oligonucleotides containing the asymmetric sequence 5′-CAGCAG-3′. J. Mol. Biol. 242, 378-388.
    • (1994) J. Mol. Biol. , vol.242 , pp. 378-388
    • Ahmad, I.1    Rao, D.N.2
  • 2
    • 0024594761 scopus 로고
    • Preferential site-specific hemimethylation of GATC sites in pBR322 DNA by dam methyltransferase from Escherichia coli
    • Bergerat, A., Kriebardis, A. & Guschlbauer, W. (1989). Preferential site-specific hemimethylation of GATC sites in pBR322 DNA by dam methyltransferase from Escherichia coli. J. Biol. Chem. 264, 4064-4070.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4064-4070
    • Bergerat, A.1    Kriebardis, A.2    Guschlbauer, W.3
  • 3
    • 0021770483 scopus 로고
    • Characterization of the genes coding for the EcoRV restriction and modification system of Escherichia coli
    • Bougueleret, L., Schwarzstein, M., Tsugita, A. & Zabeau, M. (1984). Characterization of the genes coding for the EcoRV restriction and modification system of Escherichia coli. Nucl. Acids Res. 12, 3659-3677.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 3659-3677
    • Bougueleret, L.1    Schwarzstein, M.2    Tsugita, A.3    Zabeau, M.4
  • 5
    • 0030059614 scopus 로고    scopus 로고
    • The EcoRV modification methylase causes considerable binding of DNA upon binding to its recognition sequence GATATC
    • Cal, S. & Connolly, B. A. (1996). The EcoRV modification methylase causes considerable binding of DNA upon binding to its recognition sequence GATATC. J. Biol. Chem. 271, 1008-1015.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1008-1015
    • Cal, S.1    Connolly, B.A.2
  • 6
    • 0031036523 scopus 로고    scopus 로고
    • DNA distortion and base flipping by the EcoRV DNA methyltransferase
    • Cal, S. & Connolly, B. A. (1997). DNA distortion and base flipping by the EcoRV DNA methyltransferase. J. Biol. Chem. 272, 490-496.
    • (1997) J. Biol. Chem. , vol.272 , pp. 490-496
    • Cal, S.1    Connolly, B.A.2
  • 7
    • 0344731165 scopus 로고
    • W. H. Freeman & Co., San Francisco, USA
    • Cantor, C. R. & Schimmel, P. (1980). Biophysical Chemistry, Part III, W. H. Freeman & Co., San Francisco, USA.
    • (1980) Biophysical Chemistry , Issue.3 PART
    • Cantor, C.R.1    Schimmel, P.2
  • 8
    • 0029163078 scopus 로고
    • Structure and function of DNA methyltransferases
    • Cheng, X. (1995). Structure and function of DNA methyltransferases. Annu. Rev. Biophys. Biomol. Struct. 24, 293-318.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 293-318
    • Cheng, X.1
  • 10
    • 0029556128 scopus 로고
    • Kinetic studies of MvaI DNA methyltransferase interaction with modified oligonucleotide duplexes
    • Gromova, E. S., Oretskaya, T. S., Eritja, R. & Guschlbauer, W. (1995). Kinetic studies of MvaI DNA methyltransferase interaction with modified oligonucleotide duplexes. Biochem. Mol. Biol. Int. 36, 247-255.
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , pp. 247-255
    • Gromova, E.S.1    Oretskaya, T.S.2    Eritja, R.3    Guschlbauer, W.4
  • 11
    • 0027422635 scopus 로고
    • On the origins, structures and functions of restriction-modification enzymes
    • (Setlow, J. K., ed.) Plenum Press, New York
    • Heitman, J. (1993). On the origins, structures and functions of restriction-modification enzymes. In Genetic Engineering (Setlow, J. K., ed.) 15, pp. 57-108, Plenum Press, New York.
    • (1993) Genetic Engineering , vol.15 , pp. 57-108
    • Heitman, J.1
  • 12
    • 0020160863 scopus 로고
    • Involvement of outside DNA sequences in the major kinetic path by which EcoRI endonuclease locates and leaves its recognition sequence
    • Jack, W. E., Terry, B. J. & Modrich, P. (1982). Involvement of outside DNA sequences in the major kinetic path by which EcoRI endonuclease locates and leaves its recognition sequence. Proc. Natl Acad. Sci. USA, 79, 4010-4014.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 4010-4014
    • Jack, W.E.1    Terry, B.J.2    Modrich, P.3
  • 13
    • 0029940857 scopus 로고    scopus 로고
    • Horizontal gene transfer contributes to the wide distribution and evolution of type II restriction-modification systems
    • Jeltsch, A. & Pingoud, A. (1996). Horizontal gene transfer contributes to the wide distribution and evolution of type II restriction-modification systems. J. Mol. Evol. 42, 91-96.
    • (1996) J. Mol. Evol. , vol.42 , pp. 91-96
    • Jeltsch, A.1    Pingoud, A.2
  • 14
    • 0028782732 scopus 로고
    • Pausing of the restriction endonuclease EcoRI during linear diffusion on DNA
    • Jeltsch, A., Alves, J., Wolfes, H., Maass, G. & Pingoud, A. (1994). Pausing of the restriction endonuclease EcoRI during linear diffusion on DNA. biochemistry, 33, 1025-10219.
    • (1994) Biochemistry , vol.33 , pp. 1025-10219
    • Jeltsch, A.1    Alves, J.2    Wolfes, H.3    Maass, G.4    Pingoud, A.5
  • 16
    • 0029904146 scopus 로고    scopus 로고
    • Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison to known structures of methyltransferases and isolation of catalytically inactive single mutants
    • Jeltsch, A., Sobotta, T. & Pingoud, A. (1996a). Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison to known structures of methyltransferases and isolation of catalytically inactive single mutants. Protein Eng. 9, 413-423.
    • (1996) Protein Eng. , vol.9 , pp. 413-423
    • Jeltsch, A.1    Sobotta, T.2    Pingoud, A.3
  • 17
    • 0029790522 scopus 로고    scopus 로고
    • Linear diffusion of the restriction endonuclease EcoRV on DNA is essential for the in vivo function of the enzyme
    • Jeltsch, A., Wenz, C., Stahl, F. & Pingoud, A. (1996b). Linear diffusion of the restriction endonuclease EcoRV on DNA is essential for the in vivo function of the enzyme. EMBO J. 15, 5104-5111.
    • (1996) EMBO J. , vol.15 , pp. 5104-5111
    • Jeltsch, A.1    Wenz, C.2    Stahl, F.3    Pingoud, A.4
  • 18
    • 0028990179 scopus 로고
    • M.HhaI binds tightly to substrates containing mismatches at the target base
    • Klimasauskas, S. & Roberts, R. J. (1995). M.HhaI binds tightly to substrates containing mismatches at the target base. Nucl. Acids Res. 23, 1388-1395.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 1388-1395
    • Klimasauskas, S.1    Roberts, R.J.2
  • 19
    • 0028010888 scopus 로고
    • HhaI methyltransferase flips its target base out of the DNA helix
    • Klimasauskas, S., Kumar, S., Roberts, R. J. & Cheng, X. (1994). HhaI 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
  • 20
    • 0027946731 scopus 로고
    • Three-dimensional structure of the adenine-specific DNA methyltransferase M.TaqI in complex with the cofactor S-adenosylmethionine
    • Labahn, J., Granzin, J., Schluckebier, G., Robinson, D. P., Jack, W. E., Schildkraut, I. & Saenger, W. (1994). Three-dimensional structure of the adenine-specific DNA methyltransferase M.TaqI in complex with the cofactor S-adenosylmethionine. Proc. Natl Acad. Sci. USA, 91, 10957-10961.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10957-10961
    • Labahn, J.1    Granzin, J.2    Schluckebier, G.3    Robinson, D.P.4    Jack, W.E.5    Schildkraut, I.6    Saenger, W.7
  • 21
    • 0023649944 scopus 로고
    • The GATATC-modification enzyme EcoRV is closely related to the GATC-recognizing methyltransferases DpnII and dam from E.coli and phage T4
    • Lauster, R., Kriebardis, A. & Guschlbauer, W. (1987). The GATATC-modification enzyme EcoRV is closely related to the GATC-recognizing methyltransferases DpnII and dam from E.coli and phage T4. FEBS Letters, 220, 167-176.
    • (1987) FEBS Letters , vol.220 , pp. 167-176
    • Lauster, R.1    Kriebardis, A.2    Guschlbauer, W.3
  • 22
    • 0029091789 scopus 로고
    • Substrate-length-dependent activities of human immunodeficiency virus type 1 integrase in vitro: Differential DNA binding affinities associated with different lengths of substrates
    • Lee, P. S., Censullo, M. I., Kim, H. G. & Han, M. K. (1995). Substrate-length-dependent activities of human immunodeficiency virus type 1 integrase in vitro: differential DNA binding affinities associated with different lengths of substrates. Biochemistry, 34, 10215-10223.
    • (1995) Biochemistry , vol.34 , pp. 10215-10223
    • Lee, P.S.1    Censullo, M.I.2    Kim, H.G.3    Han, M.K.4
  • 23
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNa amino-methyl-transferases, and suggests a catalytic mechanism for these enzymes
    • Malone, T., Blumenthal, R. M. & Cheng, X. (1995). Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyl-transferases, and suggests a catalytic mechanism for these enzymes. J. Mol. Biol. 253, 618-632.
    • (1995) J. Mol. Biol. , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.M.2    Cheng, X.3
  • 24
    • 0029099018 scopus 로고
    • Dam methylase from Escherichia coli: Kinetic studies using modified DNA oligomers: hemimethylated substrates
    • Marzabel, S., DuBois, S., Thielking, V., Cano, A., Eritja, R. & Guschlbauer, W. (1995). Dam methylase from Escherichia coli: kinetic studies using modified DNA oligomers: hemimethylated substrates. Nucl. Acids Res. 23, 3648-3655.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 3648-3655
    • Marzabel, S.1    DuBois, S.2    Thielking, V.3    Cano, A.4    Eritja, R.5    Guschlbauer, W.6
  • 25
    • 0028305060 scopus 로고
    • Investigation of ionizable residues critical for sequence-specific enzymatic DNA modification: Protein modification and steady-state and pre-steady-state kinetic analyses of EcoRI DNA methyltransferase
    • Mashhoon, N. & Reich, N. O. (1994). Investigation of ionizable residues critical for sequence-specific enzymatic DNA modification: protein modification and steady-state and pre-steady-state kinetic analyses of EcoRI DNA methyltransferase. Biochemistry, 33, 7113-7119.
    • (1994) Biochemistry , vol.33 , pp. 7113-7119
    • Mashhoon, N.1    Reich, N.O.2
  • 26
    • 0029758242 scopus 로고    scopus 로고
    • The paradoxical influence of thymine analogues an restriction endonuclease cleavage of oligonucleotides
    • Mazurek, M. & Sowers, L. C. (1996). The paradoxical influence of thymine analogues an restriction endonuclease cleavage of oligonucleotides. Biochemistry, 35, 11522-11528.
    • (1996) Biochemistry , vol.35 , pp. 11522-11528
    • Mazurek, M.1    Sowers, L.C.2
  • 27
    • 0028901038 scopus 로고
    • Selfish behavior of restriction-modification systems
    • Naito, T., Kusano, K. & Kobayashi, I. (1995). Selfish behavior of restriction-modification systems. Science, 267, 897-899.
    • (1995) Science , vol.267 , pp. 897-899
    • Naito, T.1    Kusano, K.2    Kobayashi, I.3
  • 28
    • 0025151421 scopus 로고
    • Incorporation of a complete set of deoxyadenosine and thymidine analogues suitable for the study of protein nucleic acid interactions into oligodeoxynucleotides. Application to the EcoRV restriction endonuclease and modification methylase
    • Newman, P. C., Nwosu, V. U., Williams, D. M., Cosstick, R., Seela, F. & Connolly, B. A. (1990). Incorporation of a complete set of deoxyadenosine and thymidine analogues suitable for the study of protein nucleic acid interactions into oligodeoxynucleotides. Application to the EcoRV restriction endonuclease and modification methylase. Biochemistry, 29, 9891-9901.
    • (1990) Biochemistry , vol.29 , pp. 9891-9901
    • Newman, P.C.1    Nwosu, V.U.2    Williams, D.M.3    Cosstick, R.4    Seela, F.5    Connolly, B.A.6
  • 30
    • 0024284344 scopus 로고
    • The cloning, purification and characterization of the EcoRV modification methylase
    • Nwosu, V. U., Connolly, B. A., Halford, S. E. & Garnett, J. (1988). The cloning, purification and characterization of the EcoRV modification methylase. Nucl. Acids Res. 16, 3705-3720.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 3705-3720
    • Nwosu, V.U.1    Connolly, B.A.2    Halford, S.E.3    Garnett, J.4
  • 31
    • 0030572656 scopus 로고    scopus 로고
    • Enzymatic C5-cytosine methylation of DNA: Mechanistic implications of new crystal structures for HhaI methyltransferase-DNA-AdoHcy complexes
    • O'Gara, M., Klimasauskas, S., Roberts, R. J. & Cheng, X. (1996a). Enzymatic C5-cytosine methylation of DNA: mechanistic implications of new crystal structures for HhaI methyltransferase-DNA-AdoHcy complexes. J. Mol. Biol. 261, 634-645.
    • (1996) J. Mol. Biol. , vol.261 , pp. 634-645
    • O'Gara, M.1    Klimasauskas, S.2    Roberts, R.J.3    Cheng, X.4
  • 32
    • 0030575782 scopus 로고    scopus 로고
    • A structural basis for the preferential binding of hemimethylated DNA by HhaI DNA methyltransferase
    • O'Gara, M., Roberts, R. J. & Cheng, X. (1996b). A structural basis for the preferential binding of hemimethylated DNA by HhaI DNA methyltransferase. J. Mol. Biol. 263, 597-606.
    • (1996) J. Mol. Biol. , vol.263 , pp. 597-606
    • O'Gara, M.1    Roberts, R.J.2    Cheng, X.3
  • 33
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G. & Gray, T. (1995). How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 34
    • 0030911133 scopus 로고    scopus 로고
    • Recognition and cleavage of DNA of type-II restriction endonucleases
    • Pingoud, A. & Jeltsch, A. (1997). Recognition and cleavage of DNA of type-II restriction endonucleases. Eur. J. Biochem. 246, 1-22.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 1-22
    • Pingoud, A.1    Jeltsch, A.2
  • 35
    • 0025772075 scopus 로고
    • Kinetic mechanism of the EcoRI DNA methyltransferase
    • Reich, N. O. & Mashhoon, N. (1991). Kinetic mechanism of the EcoRI DNA methyltransferase. Biochemistry, 30, 2929-2933.
    • (1991) Biochemistry , vol.30 , pp. 2929-2933
    • Reich, N.O.1    Mashhoon, N.2
  • 36
    • 0027222612 scopus 로고
    • Presteady state of kinetics of an S-adenosylmethionine-dependent enzyme
    • Reich, N. O. & Mashhoon, N. (1993). Presteady state of kinetics of an S-adenosylmethionine-dependent enzyme. J. Biol. Chem. 268, 9191-9193.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9191-9193
    • Reich, N.O.1    Mashhoon, N.2
  • 37
    • 0029068629 scopus 로고
    • The crystal structure of HaeIII methyltransferase covalently complexed to DNA: An extrahelical cytosine and rearranged base pairing
    • Reinisch, K. M., Chen, L., Verdine, G. L. & Lipscomb, W. N. (1995). The crystal structure of HaeIII methyltransferase covalently complexed to DNA: an extrahelical cytosine and rearranged base pairing. Cell, 82, 143-153.
    • (1995) Cell , vol.82 , pp. 143-153
    • Reinisch, K.M.1    Chen, L.2    Verdine, G.L.3    Lipscomb, W.N.4
  • 38
    • 0002598414 scopus 로고
    • The restriction enzymes
    • (Linn, S. M., Lloyd, R. S. & Roberts, R. J., eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Roberts, R. J. & Halford, S. E. (1993). The restriction enzymes. In Nucleases (Linn, S. M., Lloyd, R. S. & Roberts, R. J., eds), pp. 35-88, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1993) Nucleases , pp. 35-88
    • Roberts, R.J.1    Halford, S.E.2
  • 39
    • 0028956315 scopus 로고
    • Universal catalytic domain structure of AdoMet-dependent methyltransferase
    • Schluckebier, G., O'Gara, M., Saenger, W. & Cheng, X. (1995a). Universal catalytic domain structure of AdoMet-dependent methyltransferase. J. Mol. Biol. 247, 16-20.
    • (1995) J. Mol. Biol. , vol.247 , pp. 16-20
    • Schluckebier, G.1    O'Gara, M.2    Saenger, W.3    Cheng, X.4
  • 40
    • 0029053631 scopus 로고
    • A model for DNA binding and enzyme action derived from cristallographic studies of the TaqI N6-adenine-methyltransferase
    • Schluckebier, G., Labahn, J., Granzin, J., Schildkraut, I. & Saenger, W. (1995b). A model for DNA binding and enzyme action derived from cristallographic studies of the TaqI N6-adenine-methyltransferase. Gene, 157, 131-134.
    • (1995) Gene , vol.157 , pp. 131-134
    • Schluckebier, G.1    Labahn, J.2    Granzin, J.3    Schildkraut, I.4    Saenger, W.5
  • 41
    • 0031561804 scopus 로고    scopus 로고
    • Differential binding of S-adenosylmethionine, S-adenosylhomocysteine and sinefungin to the adenine-specific DNA methyltransferase M.TaqI
    • Schluckebier, G., Kozak, M., Bleiming, N., Weinhold, E. & Saenger, W. (1997). Differential binding of S-adenosylmethionine, S-adenosylhomocysteine and sinefungin to the adenine-specific DNA methyltransferase M.TaqI. J. Mol. Biol. 265, 56-67.
    • (1997) J. Mol. Biol. , vol.265 , pp. 56-67
    • Schluckebier, G.1    Kozak, M.2    Bleiming, N.3    Weinhold, E.4    Saenger, W.5
  • 42
    • 0030045741 scopus 로고    scopus 로고
    • Contribution of facilitated diffusion and processive catalysis to enzyme efficiency: Implications for the EcoRI restriction-modification system
    • Surby, M. A. & Reich, N. O. (1996). Contribution of facilitated diffusion and processive catalysis to enzyme efficiency: implications for the EcoRI restriction-modification system. Biochemistry, 35, 2201-2208.
    • (1996) Biochemistry , vol.35 , pp. 2201-2208
    • Surby, M.A.1    Reich, N.O.2
  • 43
    • 0029157302 scopus 로고
    • Sequence-specific binding of DNA by the EcoRV restriction and modification enzymes with nucleic acid and cofactor analogues
    • Szcselkun, M. D. & Connolly, B. A. (1995). Sequence-specific binding of DNA by the EcoRV restriction and modification enzymes with nucleic acid and cofactor analogues. Biochemistry, 34, 10724-10733.
    • (1995) Biochemistry , vol.34 , pp. 10724-10733
    • Szcselkun, M.D.1    Connolly, B.A.2
  • 44
    • 0029095895 scopus 로고
    • Probing the protein-DNA interface of the EcoRV modification methyltransferase bound to its recognition sequence, GATATC
    • Szcselkun, M. D., Jones, H. & Connolly, B. A. (1995). Probing the protein-DNA interface of the EcoRV modification methyltransferase bound to its recognition sequence, GATATC. Biochemistry, 34, 10734-10743.
    • (1995) Biochemistry , vol.34 , pp. 10734-10743
    • Szcselkun, M.D.1    Jones, H.2    Connolly, B.A.3
  • 45
    • 0025609630 scopus 로고
    • Fidelity of DNA recognition by the EcoRV restriction/modification system in vivo
    • Taylor, J. D., Goodall, A. J., Vermote, C. L. & Halford, S. E. (1990). Fidelity of DNA recognition by the EcoRV restriction/modification system in vivo. Biochemistry, 29, 10727-10733.
    • (1990) Biochemistry , vol.29 , pp. 10727-10733
    • Taylor, J.D.1    Goodall, A.J.2    Vermote, C.L.3    Halford, S.E.4
  • 46
    • 0022381905 scopus 로고
    • Facilitated diffusion during catalysis by EcoRI endonuclease: Nonspecific interactions in EcoRI catalysis
    • Terry, B. J., Jack, W. E. & Modrich, P. (1985). Facilitated diffusion during catalysis by EcoRI endonuclease: nonspecific interactions in EcoRI catalysis. J. Biol. Chem. 260, 13130-13137.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13130-13137
    • Terry, B.J.1    Jack, W.E.2    Modrich, P.3
  • 47
    • 0026512375 scopus 로고
    • Influence of enzyme-substrate contacts located outside the EcoRI recognition site on cleavage of duplex oligodeoxyribonucleotide substrates by EcoRI endonuclease
    • Van cleve, M. D. & Gumport, R. I. (1992). Influence of enzyme-substrate contacts located outside the EcoRI recognition site on cleavage of duplex oligodeoxyribonucleotide substrates by EcoRI endonuclease. Biochemistry, 31, 334-339.
    • (1992) Biochemistry , vol.31 , pp. 334-339
    • Van Cleve, M.D.1    Gumport, R.I.2
  • 48
    • 0027172789 scopus 로고
    • A double filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interaction
    • Wong, I. & Lohman, T. M. (1993). A double filter method for nitrocellulose-filter binding: application to protein-nucleic acid interaction. Proc. Natl Acad. Sci. USA, 90, 5428-5432.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5428-5432
    • Wong, I.1    Lohman, T.M.2
  • 49
    • 0029050606 scopus 로고
    • HhaI and HpaII DNA methyltransferases bind DNA mismatches, methylate uracil and block DNA repair
    • Yang, A. S., Shen, J.-C., Zingg, J.-M., Mi, S. & Jones, P. A. (1995). HhaI and HpaII DNA methyltransferases bind DNA mismatches, methylate uracil and block DNA repair. Nucl. Acids Res. 23, 1380-1387.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 1380-1387
    • Yang, A.S.1    Shen, J.-C.2    Zingg, J.-M.3    Mi, S.4    Jones, P.A.5
  • 50
    • 0029864013 scopus 로고    scopus 로고
    • Large electrostatic differences in the binding thermodynamics of a cationic peptide to oligomeric and polymeric DNA
    • Zhang, W., Bond, J. P., Anderson, C. F., Lohman, T. M. & Record, M. T., Jr. (1996). Large electrostatic differences in the binding thermodynamics of a cationic peptide to oligomeric and polymeric DNA. Proc. Natl Acad. Sci. USA, 93, 2511-2516.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2511-2516
    • Zhang, W.1    Bond, J.P.2    Anderson, C.F.3    Lohman, T.M.4    Record M.T., Jr.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.