메뉴 건너뛰기




Volumn 37, Issue 2, 2003, Pages 260-272

Prokaryotic DNA Methyltransferases: The Structure and the Mechanism of Interaction with DNA

Author keywords

DNA methyltransferase inhibitors; DNA methyltransferases; Homology; Mechanism of DNA methylation; Prokaryotes; S adenosyl L methionine; Structure; Target base flipping

Indexed keywords

DNA BASE; DNA METHYLTRANSFERASE; DNA METHYLTRANSFERASE INHIBITOR; INITIATION FACTOR; METHYLTRANSFERASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 0037275680     PISSN: 00268933     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023301923025     Document Type: Review
Times cited : (9)

References (96)
  • 1
    • 0037007175 scopus 로고    scopus 로고
    • Beyond Watson and Crick: DNA methylation and molecular enzymology of DNA methyltransferases
    • Jeltsch A. 2002. Beyond Watson and Crick: DNA methylation and molecular enzymology of DNA methyltransferases. Chembiochem. 3, 274-293.
    • (2002) Chembiochem. , vol.3 , pp. 274-293
    • Jeltsch, A.1
  • 2
    • 0032168678 scopus 로고    scopus 로고
    • CpG methylation, chromatin structure and gene silencing-a three-way connection
    • Razin A. 1998. CpG methylation, chromatin structure and gene silencing-a three-way connection. EMBO J. 17, 4905-4908.
    • (1998) EMBO J. , vol.17 , pp. 4905-4908
    • Razin, A.1
  • 3
    • 0034176798 scopus 로고    scopus 로고
    • DNA hypermethylation in tumorigenesis: Epigenetics joins genetics
    • Baylin S.B., Herman J.G. 2000. DNA hypermethylation in tumorigenesis: epigenetics joins genetics. Trends Genet. 16, 168-174.
    • (2000) Trends Genet. , vol.16 , pp. 168-174
    • Baylin, S.B.1    Herman, J.G.2
  • 6
    • 0033579311 scopus 로고    scopus 로고
    • DNA methylation de novo
    • Bird A. 1999. DNA methylation de novo. Science. 286, 2287-2288.
    • (1999) Science , vol.286 , pp. 2287-2288
    • Bird, A.1
  • 7
    • 0025801120 scopus 로고
    • Organization of restriction-modification systems
    • Wilson G.G. 1991. Organization of restriction-modification systems. Nucleic Acids Res. 19, 2539-2566.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2539-2566
    • Wilson, G.G.1
  • 8
    • 0027422635 scopus 로고
    • On the origins, structures and functions of restriction-modification enzymes
    • Heitman J. 1993. On the origins, structures and functions of restriction-modification enzymes. Genet. Eng. (NY). 15, 57-108.
    • (1993) Genet. Eng. (NY) , vol.15 , pp. 57-108
    • Heitman, J.1
  • 9
    • 0030911133 scopus 로고    scopus 로고
    • Recognition and cleavage of DNA type-II restriction endonucleases
    • Pingoud A., Jeltsch A. 1997. Recognition and cleavage of DNA 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
  • 10
    • 0034130457 scopus 로고    scopus 로고
    • Type I restriction systems: Sophisticated molecular machines (a legacy of Bertani and Weigle)
    • Murray N.E. 2000. Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle). Microbiol. Mol. Biol. Rev. 64, 412-434.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 412-434
    • Murray, N.E.1
  • 11
    • 0027536144 scopus 로고
    • Restriction endonucleases and modification methylases
    • Anderson J.E. 1993. Restriction endonucleases and modification methylases. Current Opin. Struct. Biol. 3, 24-30.
    • (1993) Current Opin. Struct. Biol. , vol.3 , pp. 24-30
    • Anderson, J.E.1
  • 13
    • 0036106345 scopus 로고    scopus 로고
    • 5C-DNA methyltransferase MspI is involved in its topoisomerase activity
    • 5C-DNA methyltransferase MspI is involved in its topoisomerase activity. Eur. J. Biochem. 269, 2491-2497.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2491-2497
    • Dubey, A.K.1    Bhattacharya, S.K.2
  • 15
  • 16
    • 0030749234 scopus 로고    scopus 로고
    • The Neisseria gonorrhoeae S.NgoVIII restriction / modification system: A type IIs system homologous to the Haemophilus parahaemolyticus HphI restriction / modification system
    • Gunn J.S., Stein D.C. 1997. The Neisseria gonorrhoeae S.NgoVIII restriction / modification system: a type IIs system homologous to the Haemophilus parahaemolyticus HphI restriction / modification system. Nucleic Acids Res. 25, 4147-4152.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4147-4152
    • Gunn, J.S.1    Stein, D.C.2
  • 17
    • 0034613269 scopus 로고    scopus 로고
    • Novel subtype of type IIs restriction enzymes. BfiI endonuclease exhibits similarities to the EDTA-resistant nuclease Nuc of Salmonella typhimurium
    • Sapranauskas R., Sasnauskas G., Lagunavicius A., Vilkaitis G., Lubys A., Siksnys V. 2000. Novel subtype of type IIs restriction enzymes. BfiI endonuclease exhibits similarities to the EDTA-resistant nuclease Nuc of Salmonella typhimurium. J. Biol. Chem. 275, 30878-30885.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30878-30885
    • Sapranauskas, R.1    Sasnauskas, G.2    Lagunavicius, A.3    Vilkaitis, G.4    Lubys, A.5    Siksnys, V.6
  • 18
    • 0032535109 scopus 로고    scopus 로고
    • Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of Streptococcus pneumoniae bound to S-adenosylmethionine
    • Tran P.H., Korszun Z.R., Cerritelli S., Springhorn S.S., Lacks S.A. 1998. Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of Streptococcus pneumoniae bound to S-adenosylmethionine. Structure. 6, 1563-1575.
    • (1998) Structure , vol.6 , pp. 1563-1575
    • Tran, P.H.1    Korszun, Z.R.2    Cerritelli, S.3    Springhorn, S.S.4    Lacks, S.A.5
  • 19
    • 0035175516 scopus 로고    scopus 로고
    • REBASE-restriction enzymes and methylases
    • Roberts R.J., Macelis D. 2001. REBASE-restriction enzymes and methylases. Nucleic Acids Res. 29, 268-269.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 268-269
    • Roberts, R.J.1    Macelis, D.2
  • 22
    • 0024582758 scopus 로고
    • Cytosine-specific type II DNA methyltransferases. A conserved enzyme core with variable target-recognizing domains
    • Lauster R., Trautner T.A., Noyer-Weidner M. 1989. Cytosine-specific type II DNA methyltransferases. A conserved enzyme core with variable target-recognizing domains. J. Mol. Biol. 206, 305-312.
    • (1989) J. Mol. Biol. , vol.206 , pp. 305-312
    • Lauster, R.1    Trautner, T.A.2    Noyer-Weidner, M.3
  • 23
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, 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-methyltransferases, 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
    • 0033571544 scopus 로고    scopus 로고
    • Molecular evolution of DNA-(cytosine-N4) methyltransferases: Evidence for their polyphyletic origin
    • Bujnicki J.M., Radlinska M. 1999. Molecular evolution of DNA-(cytosine-N4) methyltransferases: evidence for their polyphyletic origin. Nucleic Acids Res. 27, 4501-4509.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4501-4509
    • Bujnicki, J.M.1    Radlinska, M.2
  • 27
    • 0036917154 scopus 로고    scopus 로고
    • DNA duplexes containing photoactive derivatives of 2′-deoxyuridine as photocrosslinking probes for EcoRII DNA methyltransferase-substrate interaction
    • Koudan E.V., Subach O.M., Korshunova G.A., Romanova E.A., Eritja R., Gromova E.S. 2002. DNA duplexes containing photoactive derivatives of 2′-deoxyuridine as photocrosslinking probes for EcoRII DNA methyltransferase-substrate interaction. J. Biomol. Struct. Dyn. 20, 421-428.
    • (2002) J. Biomol. Struct. Dyn. , vol.20 , pp. 421-428
    • Koudan, E.V.1    Subach, O.M.2    Korshunova, G.A.3    Romanova, E.A.4    Eritja, R.5    Gromova, E.S.6
  • 28
    • 0030612472 scopus 로고    scopus 로고
    • Structure of PvuII DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment
    • Gong W., O'Gara M., Blumenthal R.M., Cheng X. 1997. Structure of PvuII DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment. Nucleic Acids Res. 25, 2702-2715.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2702-2715
    • Gong, W.1    O'Gara, M.2    Blumenthal, R.M.3    Cheng, X.4
  • 29
    • 0031422310 scopus 로고    scopus 로고
    • Structural studies of EcoRII methylase: Exploring similarities among methylases
    • Schroeder S.G., Samudzi C.T. 1997. Structural studies of EcoRII methylase: exploring similarities among methylases. Protein Eng. 10, 1385-1393.
    • (1997) Protein Eng. , vol.10 , pp. 1385-1393
    • Schroeder, S.G.1    Samudzi, C.T.2
  • 32
    • 0028104849 scopus 로고
    • DsaV methyltransferase and its isoschizomers contain a conserved segment that is similar to the segment in HhaI methyltransferase that is in contact with DNA bases
    • Gopal J., Yebra M.J., Bhagwat A.S. 1994. DsaV methyltransferase and its isoschizomers contain a conserved segment that is similar to the segment in HhaI methyltransferase that is in contact with DNA bases. Nucleic Acids Res. 22, 4482-4488.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4482-4488
    • Gopal, J.1    Yebra, M.J.2    Bhagwat, A.S.3
  • 33
    • 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., 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
  • 34
    • 0035863850 scopus 로고    scopus 로고
    • Structure of human Dnmt2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA
    • Dong A., Yoder J.A., Zhang X., Zhou L., Bestor T.H., Cheng X. 2001. Structure of human Dnmt2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA. Nucleic Acids Res. 29, 439-448.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 439-448
    • Dong, A.1    Yoder, J.A.2    Zhang, X.3    Zhou, L.4    Bestor, T.H.5    Cheng, X.6
  • 35
    • 0023176797 scopus 로고
    • Kinetic and catalytic mechanism of HhaI methyltransferase
    • Wu J.C., Santi D.V. 1987. Kinetic and catalytic mechanism of HhaI methyltransferase. J. Biol. Chem. 262, 4778-4786.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4778-4786
    • Wu, J.C.1    Santi, D.V.2
  • 36
    • 0001726386 scopus 로고
    • Mutational separation of DNA binding from catalysis in a DNA cytosine methyltransferase
    • Chen L., MacMillan A.M., Verdine G.L. 1993. Mutational separation of DNA binding from catalysis in a DNA cytosine methyltransferase. J. Am. Chem. Soc. 115, 5318-5319.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 5318-5319
    • Chen, L.1    MacMillan, A.M.2    Verdine, G.L.3
  • 37
    • 0035877609 scopus 로고    scopus 로고
    • The mechanism of DNA cytosine-5 methylation. Kinetic and mutational dissection of HhaI methyltransferase
    • Vilkaitis G., Merkiene E., Serva S., Weinhold E., Klimasauskas S. 2001. The mechanism of DNA cytosine-5 methylation. Kinetic and mutational dissection of HhaI methyltransferase. J. Biol. Chem. 276, 20924-20934.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20924-20934
    • Vilkaitis, G.1    Merkiene, E.2    Serva, S.3    Weinhold, E.4    Klimasauskas, S.5
  • 38
    • 0023718544 scopus 로고
    • 5-Fluorocytosine in DNA is a mechanism-based inhibitor of HhaI methylase
    • Osterman D.G., DePillis G.D., Wu J.C., Matsuda A., Santi D.V. 1988. 5-Fluorocytosine in DNA is a mechanism-based inhibitor of HhaI methylase. Biochemistry. 27, 5204-5210.
    • (1988) Biochemistry , vol.27 , pp. 5204-5210
    • Osterman, D.G.1    DePillis, G.D.2    Wu, J.C.3    Matsuda, A.4    Santi, D.V.5
  • 39
    • 0026078020 scopus 로고
    • Stereochemical studies of the C-methylation of deoxycytidine catalyzed by HhaI methylase and the N-methylation of deoxyadenosine catalyzed by EcoRI methylase
    • Ho D.K., Wu J.C., Santi D.V., Floss H.G. 1991. Stereochemical studies of the C-methylation of deoxycytidine catalyzed by HhaI methylase and the N-methylation of deoxyadenosine catalyzed by EcoRI methylase. Arch. Biochem. Biophys. 284, 264-269.
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 264-269
    • Ho, D.K.1    Wu, J.C.2    Santi, D.V.3    Floss, H.G.4
  • 42
    • 0033538456 scopus 로고    scopus 로고
    • On the substrate specificity of DNA methyltransferases. Adenine-N6 DNA methyltransferases also modify cytosine residues at position N4
    • Jeltsch A., Christ F., Fatemi M., Roth M. 1999. On the substrate specificity of DNA methyltransferases. Adenine-N6 DNA methyltransferases also modify cytosine residues at position N4. J. Biol. Chem. 274, 19538-19544.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19538-19544
    • Jeltsch, A.1    Christ, F.2    Fatemi, M.3    Roth, M.4
  • 43
    • 0034743948 scopus 로고    scopus 로고
    • The cytosine N4-methyltransferase M.PvuII also modifies adenine residues
    • Jeltsch A. 2001. The cytosine N4-methyltransferase M.PvuII also modifies adenine residues. Biol. Chem. 382, 707-710.
    • (2001) Biol. Chem. , vol.382 , pp. 707-710
    • Jeltsch, A.1
  • 44
    • 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
  • 45
    • 0029068629 scopus 로고
    • The crystal structure of HaeIII methyltransferase convalently 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 convalently 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
  • 46
    • 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
  • 47
    • 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., Weinhold E. 2001. Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with DNA and a cofactor analog. Nature Struct. Biol. 8, 121-125.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 121-125
    • Goedecke, K.1    Pignot, M.2    Goody, R.S.3    Scheidig, A.J.4    Weinhold, E.5
  • 48
    • 0035883736 scopus 로고    scopus 로고
    • AdoMet-dependent methylation, DNA methyltransferases and base flipping
    • Cheng X., 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
  • 49
    • 0035420651 scopus 로고    scopus 로고
    • Role of DNA minor groove interactions in substrate recognition by the M.SinI and M.EcoRII DNA (cytosine-5) methyltransferases
    • Kiss A., Posfai G., Zsurka G., Rasko T., Venetianer P. 2001. Role of DNA minor groove interactions in substrate recognition by the M.SinI and M.EcoRII DNA (cytosine-5) methyltransferases. Nucleic Acids Res. 29, 3188-3194.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3188-3194
    • Kiss, A.1    Posfai, G.2    Zsurka, G.3    Rasko, T.4    Venetianer, P.5
  • 50
    • 0035909057 scopus 로고    scopus 로고
    • How does a DNA interacting enzyme change its specificity during molecular evolution? A site-directed mutagenesis study at the DNA binding site of the DNA-(adenine-N6)-methyltransferase EcoRV
    • Beck C., Cranz S., Solmaz M., Roth M., Jeltsch A. 2001. How does a DNA interacting enzyme change its specificity during molecular evolution? A site-directed mutagenesis study at the DNA binding site of the DNA-(adenine-N6)-methyltransferase EcoRV. Biochemistry. 40, 10956-10965.
    • (2001) Biochemistry , vol.40 , pp. 10956-10965
    • Beck, C.1    Cranz, S.2    Solmaz, M.3    Roth, M.4    Jeltsch, A.5
  • 52
    • 0032519379 scopus 로고    scopus 로고
    • 2-Aminopurine as a fluorescent probe for DNA base flipping by methyltransferases
    • Holz B., Klimasauskas S., Serva S., 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
  • 53
    • 0030448581 scopus 로고    scopus 로고
    • Targeted base stacking disruption by the EcoRI DNA methyltransferase
    • Allan B.W., 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
  • 55
    • 0034667760 scopus 로고    scopus 로고
    • Substrate binding in vitro and kinetics of RsrI [N6-adenine] DNA methyltransferase
    • Szegedi S.S., Reich N.O., 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
  • 56
    • 0034640127 scopus 로고    scopus 로고
    • Binding of EcoP15I DNA methyltransferase to DNA reveals a large structural distortion within the recognition sequence
    • Reddy V.R., Rao D.N. 2000. Binding of EcoP15I 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, V.R.1    Rao, D.N.2
  • 57
    • 0033593476 scopus 로고    scopus 로고
    • Mutational analysis of target base flipping by the EcoRV adenine-N6 DNA methyltransferase
    • Jeltsch A., Roth M., Friedrich T. 1999. Mutational analysis of target base flipping by the EcoRV adenine-N6 DNA methyltransferase. J. Mol. Biol. 285, 1121-1130.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1121-1130
    • Jeltsch, A.1    Roth, M.2    Friedrich, T.3
  • 58
    • 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. Nucleic Acids Res. 23, 1388-1395.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1388-1395
    • Klimasauskas, S.1    Roberts, R.J.2
  • 59
    • 0032145158 scopus 로고    scopus 로고
    • Chemical display of thymine residues flipped out by DNA methyltransferases
    • Serva S., Weinhold E., Roberts R.J., Klimasauskas S. 1998. Chemical display of thymine residues flipped out by DNA methyltransferases. Nucleic Acids Res. 26, 3473-3479.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3473-3479
    • Serva, S.1    Weinhold, E.2    Roberts, R.J.3    Klimasauskas, S.4
  • 60
    • 0033591334 scopus 로고    scopus 로고
    • Identification of the binding site for the extrahelical target base in N6-adenine DNA methyltransferases by photo-cross-linking with duplex oligodeoxyribonucleotides containing 5-iodouracil at the target position
    • Holz B., Dank N., Eickhoff J.E., Lipps G., Krauss G., Weinhold E. 1999. Identification of the binding site for the extrahelical target base in N6-adenine DNA methyltransferases by photo-cross-linking with duplex oligodeoxyribonucleotides containing 5-iodouracil at the target position. J. Biol. Chem. 274, 15066-15072.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15066-15072
    • Holz, B.1    Dank, N.2    Eickhoff, J.E.3    Lipps, G.4    Krauss, G.5    Weinhold, E.6
  • 61
    • 0037016666 scopus 로고    scopus 로고
    • Bacteriophage T4 Dam DNA-[N6-adenine]methyltransferase. Kinetic evidence for a catalytically essential conformational change in the ternary complex
    • Evdokimov A.A., Zinoviev V.V., Malygin E.G., Schlagman S.L., Hattman S. 2002. Bacteriophage T4 Dam DNA-[N6-adenine]methyltransferase. Kinetic evidence for a catalytically essential conformational change in the ternary complex. J. Biol. Chem. 277, 279-286.
    • (2002) J. Biol. Chem. , vol.277 , pp. 279-286
    • Evdokimov, A.A.1    Zinoviev, V.V.2    Malygin, E.G.3    Schlagman, S.L.4    Hattman, S.5
  • 62
    • 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, 2933-2939.
    • (1991) Biochemistry , vol.30 , pp. 2933-2939
    • Reich, N.O.1    Mashhoon, N.2
  • 63
    • 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., 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
  • 64
    • 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
  • 65
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • von Hippel P.H., Berg O.G. 1989. Facilitated target location in biological systems. J. Biol. Chem. 264, 675-678.
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • Von Hippel, P.H.1    Berg, O.G.2
  • 66
    • 0035883723 scopus 로고    scopus 로고
    • Structure and function of type II restriction endonucleases
    • Pingoud A., Jeltsch A. 2001. Structure and function of type II restriction endonucleases. Nucleic Acids Res. 29, 3705-3727.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3705-3727
    • Pingoud, A.1    Jeltsch, A.2
  • 67
    • 0026647626 scopus 로고
    • Sequence-specific DNA binding by the MspI DNA methyltransferase
    • Dubey A.K., Roberts R.J. 1992. Sequence-specific DNA binding by the MspI DNA methyltransferase. Nucleic Acids Res. 20, 3167-3173.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3167-3173
    • Dubey, A.K.1    Roberts, R.J.2
  • 68
    • 0030711030 scopus 로고    scopus 로고
    • Interaction of the phage T4 Dam DNA-[N6-adenine] methyltransferase with oligonucleotides containing native or modified (defective) recognition sites
    • Malygin E.G., Petrov N.A., Gorbunov Y.A., Kossykh V.G., Hattman S. 1997. Interaction of the phage T4 Dam DNA-[N6-adenine] methyltransferase with oligonucleotides containing native or modified (defective) recognition sites. Nucleic Acids Res. 25, 4393-4399.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4393-4399
    • Malygin, E.G.1    Petrov, N.A.2    Gorbunov, Y.A.3    Kossykh, V.G.4    Hattman, S.5
  • 70
    • 0030059614 scopus 로고    scopus 로고
    • The EcoRV modification methylase causes considerable bending of DNA upon binding to its recognition sequence GATATC
    • Cal S., Connolly B.A. 1996. The EcoRV modification methylase causes considerable bending 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
  • 71
    • 0030842058 scopus 로고    scopus 로고
    • Angle and locus of the bend induced by the MspI DNA methyltransferase in a sequence-specific complex with DNA
    • Dubey A.K., Bhattacharya S.K. 1997. Angle and locus of the bend induced by the MspI DNA methyltransferase in a sequence-specific complex with DNA. Nucleic Acids Res. 25, 2025-2029.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2025-2029
    • Dubey, A.K.1    Bhattacharya, S.K.2
  • 72
    • 0029848936 scopus 로고    scopus 로고
    • Sequence-specific recognition of cytosine C5 and adenine N6 DNA methyltransferases requires different deformations of DNA
    • Garcia R.A., Bustamante C.J., Reich N.O. 1996. Sequence-specific recognition of cytosine C5 and adenine N6 DNA methyltransferases requires different deformations of DNA. Proc. Natl. Acad. Sci. USA. 93, 7618-7622.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7618-7622
    • Garcia, R.A.1    Bustamante, C.J.2    Reich, N.O.3
  • 73
    • 0028908131 scopus 로고
    • Footprint analysis of M.SssI and M.HhaI methyltransferases reveals extensive interactions with the substrate DNA backbone
    • Renbaum P., Razin A. 1995. Footprint analysis of M.SssI and M.HhaI methyltransferases reveals extensive interactions with the substrate DNA backbone. J. Mol. Biol. 248, 19-26.
    • (1995) J. Mol. Biol. , vol.248 , pp. 19-26
    • Renbaum, P.1    Razin, A.2
  • 74
    • 0034663610 scopus 로고    scopus 로고
    • DNA bending induced by DNA (cytosine-5) methyltransferases
    • Rasko T., Finta C., Kiss A. 2000. DNA bending induced by DNA (cytosine-5) methyltransferases. Nucleic Acids Res. 28, 3083-3091.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3083-3091
    • Rasko, T.1    Finta, C.2    Kiss, A.3
  • 75
    • 0030154882 scopus 로고    scopus 로고
    • Base eversion and shuffling by DNA methyltransferases
    • Nelson H.C., Bestor T.H. 1996. Base eversion and shuffling by DNA methyltransferases. Chem. Biol. 3, 419-423.
    • (1996) Chem. Biol. , vol.3 , pp. 419-423
    • Nelson, H.C.1    Bestor, T.H.2
  • 76
    • 0242444679 scopus 로고    scopus 로고
    • Dynamic modes of the flipped-out cytosine during HhaI methyltransferase-DNA interactions in solution
    • Klimasauskas S., Szyperski T., Serva S., Wuthrich K. 1998. Dynamic modes of the flipped-out cytosine during HhaI methyltransferase-DNA interactions in solution. EMBO J. 17, 317-324.
    • (1998) EMBO J. , vol.17 , pp. 317-324
    • Klimasauskas, S.1    Szyperski, T.2    Serva, S.3    Wuthrich, K.4
  • 77
    • 0031941434 scopus 로고    scopus 로고
    • Direct real time observation of base flipping by the EcoRI DNA methyltransferase
    • Allan B.W., Beechem J.M., Lindstrom W.M., Reich N.O. 1998. Direct real time observation of base flipping by the EcoRI DNA methyltransferase. J. Biol. Chem. 273, 2368-2373.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2368-2373
    • Allan, B.W.1    Beechem, J.M.2    Lindstrom, W.M.3    Reich, N.O.4
  • 78
    • 0025031980 scopus 로고
    • The double role of methyl donor and allosteric effector of S-adenosyl-methionine for Dam methylase of E. coli
    • Bergerat A., Guschlbauer W. 1990. The double role of methyl donor and allosteric effector of S-adenosyl-methionine for Dam methylase of E. coli. Nucleic Acids Res. 18, 4369-4375.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4369-4375
    • Bergerat, A.1    Guschlbauer, W.2
  • 79
    • 0033591248 scopus 로고    scopus 로고
    • Kinetic mechanism of cytosine DNA methyltransferase MspI
    • Bhattacharya S.K., Dubey A.K. 1999. Kinetic mechanism of cytosine DNA methyltransferase MspI. J. Biol. Chem. 274, 14743-14749.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14743-14749
    • Bhattacharya, S.K.1    Dubey, A.K.2
  • 80
    • 0029099018 scopus 로고
    • Dam methylase from Escherichia coli: Kinetic studies using modified DNA oligomers: Hemimethylated substrates
    • Marzabal S., DuBoris S., Thielking V., Cano A., Eritja R., Guschlbauer W. 1995. Dam methylase from Escherichia coli: kinetic studies using modified DNA oligomers: hemimethylated substrates. Nucleic Acids Res. 23, 3648-3655.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3648-3655
    • Marzabal, S.1    DuBoris, S.2    Thielking, V.3    Cano, A.4    Eritja, R.5    Guschlbauer, W.6
  • 81
    • 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. 1996. 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
  • 82
    • 0029157302 scopus 로고
    • Sequence-specific binding of DNA by the EcoRV restriction and modification enzymes with nucleic acid and cofactor analogues
    • Szczelkun 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
    • Szczelkun, M.D.1    Connolly, B.A.2
  • 83
    • 0026720055 scopus 로고
    • In vitro specificity of EcoRI DNA methyltransferase
    • Reich N.O., Olsen C., Osti F., Murphy J. 1992. In vitro specificity of EcoRI DNA methyltransferase. J. Biol. Chem. 267, 15802-15807.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15802-15807
    • Reich, N.O.1    Olsen, C.2    Osti, F.3    Murphy, J.4
  • 84
    • 0026323307 scopus 로고
    • Antitumor properties of 2(1H)-pyrimidinone riboside (zebularine) and its fluorinated analogues
    • Driscoll J.S., Marquez V.E., Plowman J., Liu P.S., Kelley J.A., Barchi J.J. Jr. 1991. Antitumor properties of 2(1H)-pyrimidinone riboside (zebularine) and its fluorinated analogues. J. Med. Chem. 34, 3280-3284.
    • (1991) J. Med. Chem. , vol.34 , pp. 3280-3284
    • Driscoll, J.S.1    Marquez, V.E.2    Plowman, J.3    Liu, P.S.4    Kelley, J.A.5    Barchi Jr., J.J.6
  • 85
    • 0029736819 scopus 로고    scopus 로고
    • Methylation inhibitors can increase the rate of cytosine deamination by (cytosine-5)-DNA methyltransferase
    • Zingg J.M., Shen J.C., Yang A.S., Rapoport H., Jones P.A. 1996. Methylation inhibitors can increase the rate of cytosine deamination by (cytosine-5)-DNA methyltransferase. Nucleic Acids Res. 24, 3267-3275.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3267-3275
    • Zingg, J.M.1    Shen, J.C.2    Yang, A.S.3    Rapoport, H.4    Jones, P.A.5
  • 86
    • 0034727638 scopus 로고    scopus 로고
    • Reviving a dead enzyme: Cytosine deaminations promoted by an inactive DNA methyltransferase and an S-adenosyl-methionine analogue
    • Sharath A.N., Weinhold E., Bhagwat A.S. 2000. Reviving a dead enzyme: cytosine deaminations promoted by an inactive DNA methyltransferase and an S-adenosyl-methionine analogue. Biochemistry. 39, 14611-14616.
    • (2000) Biochemistry , vol.39 , pp. 14611-14616
    • Sharath, A.N.1    Weinhold, E.2    Bhagwat, A.S.3
  • 87
    • 0027977001 scopus 로고
    • Cytosine deaminations catalyzed by DNA cytosine methyltransferases are unlikely to be the major cause of mutational hot spots at sites of cytosine methylation in Escherichia coli
    • Wyszynski M., Gabbara S., Bhagwat A.S. 1994. Cytosine deaminations catalyzed by DNA cytosine methyltransferases are unlikely to be the major cause of mutational hot spots at sites of cytosine methylation in Escherichia coli. Proc. Natl. Acad. Sci. USA. 91, 1574-1578.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1574-1578
    • Wyszynski, M.1    Gabbara, S.2    Bhagwat, A.S.3
  • 88
    • 0021830501 scopus 로고
    • The irreversible binding of azacytosine-containing DNA fragments to bacterial DNA(cytosine-5)methyltransferases
    • Friedman S. 1985. The irreversible binding of azacytosine-containing DNA fragments to bacterial DNA(cytosine-5)methyltransferases. J. Biol. Chem. 260, 5698-5705.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5698-5705
    • Friedman, S.1
  • 89
    • 0028920604 scopus 로고
    • The mechanism of inhibition of DNA (cytosine-5-)-methyltransferases by 5-azacytosine is likely to involve methyl transfer to the inhibitor
    • Gabbara S., Bhagwat A.S. 1995. The mechanism of inhibition of DNA (cytosine-5-)-methyltransferases by 5-azacytosine is likely to involve methyl transfer to the inhibitor. Biochem. J. 307, 87-92.
    • (1995) Biochem. J. , vol.307 , pp. 87-92
    • Gabbara, S.1    Bhagwat, A.S.2
  • 91
    • 0027285491 scopus 로고
    • Determination of the order of substrate addition to MspI DNA methyltransferase using a novel mechanism-based inhibitor
    • Taylor C., Ford K., Connolly B.A., Hornby D.P. 1993. Determination of the order of substrate addition to MspI DNA methyltransferase using a novel mechanism-based inhibitor. Biochem. J. 291, 493-504.
    • (1993) Biochem. J. , vol.291 , pp. 493-504
    • Taylor, C.1    Ford, K.2    Connolly, B.A.3    Hornby, D.P.4
  • 93
    • 0036965821 scopus 로고    scopus 로고
    • Zebularine: A novel DNA methylation inhibitor that forms a covalent complex with DNA methyltransferases
    • Zhou L., Cheng X., Connolly B., Dickman M., Hurd P., Hornby D. 2002. Zebularine: a novel DNA methylation inhibitor that forms a covalent complex with DNA methyltransferases. J. Mol. Biol. 321, 591-599.
    • (2002) J. Mol. Biol. , vol.321 , pp. 591-599
    • Zhou, L.1    Cheng, X.2    Connolly, B.3    Dickman, M.4    Hurd, P.5    Hornby, D.6
  • 94
    • 0030789978 scopus 로고    scopus 로고
    • DNA containing 4′-thio-2′-deoxycytidine inhibits methylation by HhaI methyltransferase
    • Kumar S., Horton J.R., Jones G.D., Walker R.T., Roberts R.J., Cheng X. 1997. DNA containing 4′-thio-2′-deoxycytidine inhibits methylation by HhaI methyltransferase. Nucleic Acids Res. 25, 2773-2783.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2773-2783
    • Kumar, S.1    Horton, J.R.2    Jones, G.D.3    Walker, R.T.4    Roberts, R.J.5    Cheng, X.6
  • 95
    • 0028851193 scopus 로고
    • Selective inhibition of cytosine-DNA methylases by polyamines
    • Ruiz-Herrera J., Ruiz-Medrano R., Dominguez A. 1995. Selective inhibition of cytosine-DNA methylases by polyamines. FEBS Lett. 357, 192-196.
    • (1995) FEBS Lett. , vol.357 , pp. 192-196
    • Ruiz-Herrera, J.1    Ruiz-Medrano, R.2    Dominguez, A.3
  • 96
    • 0033532378 scopus 로고    scopus 로고
    • An essential role for DNA adenine methylation in bacterial virulence
    • Heithoff D.M., Sinsheimer R.L., Low D.A., Mahan M.J. 1999. An essential role for DNA adenine methylation in bacterial virulence. Science. 284, 967-970.
    • (1999) Science , vol.284 , pp. 967-970
    • Heithoff, D.M.1    Sinsheimer, R.L.2    Low, D.A.3    Mahan, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.