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Volumn 259, Issue 2, 1996, Pages 229-240

Functional analysis of conserved motifs in EcoP15I DNA methyltransferase

Author keywords

DNA protein crosslinking; Sinefungin; Site directed mutagenesis; Type III restriction modification system

Indexed keywords

ADENINE; ARGININE; DNA METHYLTRANSFERASE; GLYCINE; METHYL GROUP; SERINE; TRYPTOPHAN; TYROSINE;

EID: 0029967388     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0315     Document Type: Article
Times cited : (35)

References (38)
  • 1
    • 0025017245 scopus 로고
    • DNA methylation. The effect of minor bases on DNA-protein interactions
    • Adams, R. L. P. (1990). DNA methylation. The effect of minor bases on DNA-protein interactions. Biochem. J. 265, 309-320.
    • (1990) Biochem. J. , vol.265 , pp. 309-320
    • Adams, R.L.P.1
  • 2
    • 0028220511 scopus 로고
    • Photolabeling of the EcoP15I DNA methyltransferase with S-adenosyl-L-methionine
    • Ahmad, I. & Rao, D. N. (1994a). Photolabeling of the EcoP15I DNA methyltransferase with S-adenosyl-L-methionine. Gene, 142, 67-71.
    • (1994) Gene , vol.142 , pp. 67-71
    • Ahmad, I.1    Rao, D.N.2
  • 3
    • 0028143223 scopus 로고
    • Interaction of EcoP15I DNA methyltransferase with oligonucleotides containing the asymmetric sequence 5'-CAGCAG-3'
    • Ahmad, I. & Rao, D. N. (1994b). 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
  • 4
    • 0029035548 scopus 로고
    • DNA recognition by the EcoP15I and EcoPI modification methyltransferases
    • Ahmad, I., Krishnamurthy V. & Rao, D. N. (1995). DNA recognition by the EcoP15I and EcoPI modification methyltransferases. Gene, 157, 143-147.
    • (1995) Gene , vol.157 , pp. 143-147
    • Ahmad, I.1    Krishnamurthy, V.2    Rao, D.N.3
  • 5
    • 0001952059 scopus 로고
    • The ATP-dependent restriction enzymes
    • Linn, S. M., Lloyd, R. S. & Robert, R. J., eds
    • Bickle, T. A. (1993). The ATP-dependent restriction enzymes. In Nucleuses (Linn, S. M., Lloyd, R. S. & Robert, R. J., eds), pp. 89-109.
    • (1993) Nucleuses , pp. 89-109
    • Bickle, T.A.1
  • 6
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C. & Doly, J. (1979). A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucl. Acids Res. 7, 1513-1523.
    • (1979) Nucl. Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0027338134 scopus 로고
    • Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine
    • Cheng, X., Kumar, S., Posfai, J. & Roberts, R. J. (1993). Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine. Cell, 74, 299-307.
    • (1993) Cell , vol.74 , pp. 299-307
    • Cheng, X.1    Kumar, S.2    Posfai, J.3    Roberts, R.J.4
  • 9
    • 0014817347 scopus 로고
    • Use of dimethyl suberimidate, a crosslinking reagent, in studying the subunit structure of oligomeric proteins
    • Davies, G. E. & Stark, G. R. (1970). Use of dimethyl suberimidate, a crosslinking reagent, in studying the subunit structure of oligomeric proteins. Proc. Natl Acad. Sci. USA, 66, 651-656.
    • (1970) Proc. Natl Acad. Sci. USA , vol.66 , pp. 651-656
    • Davies, G.E.1    Stark, G.R.2
  • 10
    • 0029353607 scopus 로고
    • Structural modelling of a type I DNA methyltransferase
    • Dryden, D. T. F., Sturrock, S. S. & Winter, M. (1995). Structural modelling of a type I DNA methyltransferase. Nature Struct. Biol. 2, 632-635.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 632-635
    • Dryden, D.T.F.1    Sturrock, S.S.2    Winter, M.3
  • 11
    • 0027328486 scopus 로고
    • The role of the preserved sequences of Dam methylase
    • Guyot, J. B., Grassi, J., Hahn, U. & Guschlbauer, W. (1993). The role of the preserved sequences of Dam methylase. Nucl. Acids Res. 21, 3183-3190.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 3183-3190
    • Guyot, J.B.1    Grassi, J.2    Hahn, U.3    Guschlbauer, W.4
  • 12
    • 0024278335 scopus 로고
    • Type III DNA restriction and modification systems EcoPI and EcoP15I. Nucleotide sequence of the EcoPI operon, the EcoP15I mod gene and some EcoPI mod mutants
    • Hümbelin, M., Suri, B., Rao, D. N., Hornby D. P., Eberle, H., Pripfl, T., Kenel, S. & Bickle, T. A. (1988). Type III DNA restriction and modification systems EcoPI and EcoP15I. Nucleotide sequence of the EcoPI operon, the EcoP15I mod gene and some EcoPI mod mutants. J. Mol. Biol. 200, 23-29.
    • (1988) J. Mol. Biol. , vol.200 , pp. 23-29
    • Hümbelin, M.1    Suri, B.2    Rao, D.N.3    Hornby, D.P.4    Eberle, H.5    Pripfl, T.6    Kenel, S.7    Bickle, T.A.8
  • 13
    • 0024398664 scopus 로고
    • Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes
    • Ingrosso, D., Fowler, A. V., Bleibaum, J. & Clarke, S. (1989). Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. J. Biol. Chem. 264, 20131-20139.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20131-20139
    • Ingrosso, D.1    Fowler, A.V.2    Bleibaum, J.3    Clarke, S.4
  • 14
    • 0024841942 scopus 로고
    • Sequence motifs characteristic of DNA [cytosine-N4] methyltransferases: Similarity to adenine and cytosine-C5-methylases
    • Klimasauskas, S., Timinskas, A., Menkevicius, S., Butkiene, D., Butkus, V. & Janulaitis, A. (1989). Sequence motifs characteristic of DNA [cytosine-N4] methyltransferases: similarity to adenine and cytosine-C5-methylases. Nucl. Acids Res. 17, 9823-9831.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 9823-9831
    • Klimasauskas, S.1    Timinskas, A.2    Menkevicius, S.3    Butkiene, D.4    Butkus, V.5    Janulaitis, A.6
  • 15
    • 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
  • 16
    • 0027185601 scopus 로고
    • Conserved sequence motif DPPY in region IV of the phage T4 Dam DNA-[N6-adenine]-methyltransferase is important for S-adenosyl-L-methionine binding
    • Kossykh, V. G., Schlagaman, S. L. & Hattman, S. (1993). Conserved sequence motif DPPY in region IV of the phage T4 Dam DNA-[N6-adenine]-methyltransferase is important for S-adenosyl-L-methionine binding. Nucl. Acids Res. 21, 3563-3566.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 3563-3566
    • Kossykh, V.G.1    Schlagaman, S.L.2    Hattman, S.3
  • 17
    • 2642699794 scopus 로고
    • Rapid and efficient site-directed mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985). Rapid and efficient site-directed mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA, 82, 488-492.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 18
    • 0027946731 scopus 로고
    • Three-dimensional structure of the adenine-specific DNA methyltransferase M.TaqI in complex with the cofactor S-adenosylmethionine
    • Labahn, J., Grazin, 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    Grazin, J.2    Schluckebier, G.3    Robinson, D.P.4    Jack, W.E.5    Schildkraut, I.6    Saenger, W.7
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0024582758 scopus 로고
    • Cytosine-specific type II DNA methyltransferases; a conserved enzyme core with variable target-recognizing domain
    • Lauster, R., Trautner, T. A. & Noyer-Weidner, M. (1989). Cytosine-specific type II DNA methyltransferases; a conserved enzyme core with variable target-recognizing domain. 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
  • 22
    • 0025767319 scopus 로고
    • M.EcoP15I methylates the second adenine in its recognition sequence
    • Meisel, A., Krüger, D. H. & Bickle, T. A. (1991). M.EcoP15I methylates the second adenine in its recognition sequence. Nucl. Acids Res. 9, 3997.
    • (1991) Nucl. Acids Res. , vol.9 , pp. 3997
    • Meisel, A.1    Krüger, D.H.2    Bickle, T.A.3
  • 23
    • 0028248579 scopus 로고
    • Limited proteolysis of protein-nucleic acid complexes
    • (Kneale, G. G., ed.), Humana Press, Totowa, NJ
    • Plyte, S. E. & Kneale, G. G. (1994). Limited proteolysis of protein-nucleic acid complexes. In Methods in Molecular Biology (Kneale, G. G., ed.), vol. 30, pp. 151-160, Humana Press, Totowa, NJ.
    • (1994) Methods in Molecular Biology , vol.30 , pp. 151-160
    • Plyte, S.E.1    Kneale, G.G.2
  • 24
    • 0024604147 scopus 로고
    • Predictive motifs derived from cytosine methyltransferases
    • Posfai, J., Bhagwat, A. S., Posfai, G. & Roberts, R. J. (1989). Predictive motifs derived from cytosine methyltransferases. Nucl. Acids Res. 17, 2421-2435.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 2421-2435
    • Posfai, J.1    Bhagwat, A.S.2    Posfai, G.3    Roberts, R.J.4
  • 25
    • 0028955417 scopus 로고
    • S-Adenosyl methionine alters the DNA contacts of the EcoKI methyltransferase
    • Powell, L. M. & Murray N. E. (1995). S-Adenosyl methionine alters the DNA contacts of the EcoKI methyltransferase. Nucl. Acids Res. 23, 967-974.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 967-974
    • Powell, L.M.1    Murray, N.E.2
  • 26
    • 0027453423 scopus 로고
    • DNA recognition by the EcoKI methyltransferase; The influence of DNA methylation and the cofactor S-adenosyl-L-methionine
    • Powell, L. M., Dryden, D. T. F., Willcock, D. F., Pain, R. H. & Murray, N. E. (1993). DNA recognition by the EcoKI methyltransferase; The influence of DNA methylation and the cofactor S-adenosyl-L-methionine. J. Mol. Biol. 234, 60-71.
    • (1993) J. Mol. Biol. , vol.234 , pp. 60-71
    • Powell, L.M.1    Dryden, D.T.F.2    Willcock, D.F.3    Pain, R.H.4    Murray, N.E.5
  • 27
    • 0024388203 scopus 로고
    • Cloning, overexpression and the catalytic properties of EcoP15I modification methylase from Escherichia coli
    • Rao, D. N., Page, M. G. & Bickle, T. A. (1989). Cloning, overexpression and the catalytic properties of EcoP15I modification methylase from Escherichia coli. J. Mol. Biol. 209, 599-606.
    • (1989) J. Mol. Biol. , vol.209 , pp. 599-606
    • Rao, D.N.1    Page, M.G.2    Bickle, T.A.3
  • 28
    • 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
  • 29
    • 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
  • 31
    • 0028956315 scopus 로고
    • Universal catalytic domain structure of AdoMet-dependent methyltransferases
    • Schluckebier, G., O'Gara, M. Saenger, W. & Cheng, X. (1995). Universal catalytic domain structure of AdoMet-dependent methyltransferases. J. Mol. Biol. 247, 16-20.
    • (1995) J. Mol. Biol. , vol.247 , pp. 16-20
    • Schluckebier, G.1    O'Gara, M.S.W.2    Cheng, X.3
  • 33
    • 0024544014 scopus 로고
    • The FokI restriction-modification system. Presence of two domains in FokI methylase responsible for modification of different DNA strands
    • Sugisaki, H., Kita, K. & Takanami, M. (1989). The FokI restriction-modification system. Presence of two domains in FokI methylase responsible for modification of different DNA strands. J. Biol. Chem. 264, 5757-5761.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5757-5761
    • Sugisaki, H.1    Kita, K.2    Takanami, M.3
  • 34
    • 0029095895 scopus 로고
    • Probing the Protein-DNA interface of the EcoRV modification methyltransferase bound to its recognition sequence, GATATC
    • Szczelkun, 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
    • Szczelkun, M.D.1    Jones, H.2    Connolly, B.A.3
  • 36
    • 0028074254 scopus 로고
    • A mutational analysis of the two motifs common to adenine methyltransferases
    • Willcock, D. F., Dryden, D. T. F. & 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
  • 37
    • 0026338873 scopus 로고
    • Restriction and modification systems
    • Wilson, G. G. & Murray, N. E. (1991). Restriction and modification systems. Annu. Rev. Genet. 25, 585-627.
    • (1991) Annu. Rev. Genet. , vol.25 , pp. 585-627
    • Wilson, G.G.1    Murray, N.E.2


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