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Volumn 31, Issue 11, 2003, Pages 2803-2810

Purification and characterisation of a novel DNA methyltransferase, M.AhdI

Author keywords

[No Author keywords available]

Indexed keywords

DNA METHYLTRANSFERASE; DOUBLE STRANDED DNA; DNA; PROTEIN SUBUNIT;

EID: 0038268065     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg399     Document Type: Article
Times cited : (23)

References (23)
  • 1
    • 0000010735 scopus 로고    scopus 로고
    • Bacterial DNA methyltransferases
    • Cheng,X. and Blumenthal,R.M. (eds), World Scientific Publishing, New York, NY
    • Dryden,D.T.F. (1999) Bacterial DNA methyltransferases. In Cheng,X. and Blumenthal,R.M. (eds), S-adenosyl Methionine Dependent Methyltransferases: Structure and Function. World Scientific Publishing, New York, NY, pp. 283-340.
    • (1999) S-adenosyl Methionine Dependent Methyltransferases: Structure and Function , pp. 283-340
    • Dryden, D.T.F.1
  • 2
    • 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., 24, 412-434.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.24 , pp. 412-434
    • Murray, N.E.1
  • 4
    • 0026503940 scopus 로고
    • Purification and biochemical characterisation of the EcoR124 type I modification methylase
    • Taylor,I., Patel,J., Firman,K. and Kneale,G.G. (1992) Purification and biochemical characterisation of the EcoR124 type I modification methylase. Nucleic Acids Res., 20, 179-186.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 179-186
    • Taylor, I.1    Patel, J.2    Firman, K.3    Kneale, G.G.4
  • 5
    • 0027497325 scopus 로고
    • Purification and characterization of the methyltransferase from the Type-1 restriction and modification system of E.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 E.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
  • 6
    • 0028099459 scopus 로고
    • A symmetrical model for the domain structure of Type I DNA methyltransferases
    • Kneale,G.G. (1994) A symmetrical model for the domain structure of Type I DNA methyltransferases. J. Mol. Biol., 243, 1-5.
    • (1994) J. Mol. Biol. , vol.243 , pp. 1-5
    • Kneale, G.G.1
  • 7
    • 0031969570 scopus 로고    scopus 로고
    • Protein-protein and protein-DNA interactions in the Type I restriction endonuclease R.EcoR124I
    • Mernagh,D.R., Janscak,P., Firman,K. and Kneale,G.G. (1998) Protein-protein and protein-DNA interactions in the Type I restriction endonuclease R.EcoR124I. Biol. Chem., 379, 497-504.
    • (1998) Biol. Chem. , vol.379 , pp. 497-504
    • Mernagh, D.R.1    Janscak, P.2    Firman, K.3    Kneale, G.G.4
  • 8
    • 0032190284 scopus 로고    scopus 로고
    • Analysis of the subunit assembly of the type IC restriction-modification enzyme EcoR124I
    • Janscak,P., Dryden,D.T.F. and Firman,K. (1998) Analysis of the subunit assembly of the type IC restriction-modification enzyme EcoR124I. Nucleic Acids Res., 26, 4439-4445.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4439-4445
    • Janscak, P.1    Dryden, D.T.F.2    Firman, K.3
  • 9
    • 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., 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.1    Cooper, L.P.2    Thorpe, P.H.3    Byron, O.4
  • 10
    • 0024968186 scopus 로고
    • Conservation of complex recognition domains between families of restriction enzymes
    • Cowan,G.M., Gann,A.A.F. and Murray,N.E. (1989) Conservation of complex recognition domains between families of restriction enzymes. Cell, 56, 103-109.
    • (1989) Cell , vol.56 , pp. 103-109
    • Cowan, G.M.1    Gann, A.A.F.2    Murray, N.E.3
  • 11
    • 0026540803 scopus 로고
    • Recombination of constant and variable modules alters DNA sequence recognition by Type IC restriction-modification enzymes
    • Gubler,M., Braguglia,D., Meyer,J. Piekarowitz,A. and Bickle,T.A. (1992) Recombination of constant and variable modules alters DNA sequence recognition by Type IC restriction-modification enzymes. EMBO J., 11, 233-240.
    • (1992) EMBO J. , vol.11 , pp. 233-240
    • Gubler, M.1    Braguglia, D.2    Meyer, J.3    Piekarowitz, A.4    Bickle, T.A.5
  • 13
    • 0344843379 scopus 로고    scopus 로고
    • Cloning expression and characterisation of the novel DNA methyltransferase
    • M.AhdI. PhD thesis, University of Portsmouth, Portsmouth, UK
    • Marks,P. (2001) Cloning expression and characterisation of the novel DNA methyltransferase, M.AhdI. PhD thesis, University of Portsmouth, Portsmouth, UK.
    • (2001)
    • Marks, P.1
  • 14
    • 0030854741 scopus 로고    scopus 로고
    • DNA binding and subunit interactions in the type I methyltransferase M.EcoR124I
    • Mernagh,D.R., Reynolds,L.A. and Kneale,G.G. (1997) DNA binding and subunit interactions in the type I methyltransferase M.EcoR124I. Nucleic Acids Res., 25, 987-991.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 987-991
    • Mernagh, D.R.1    Reynolds, L.A.2    Kneale, G.G.3
  • 15
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • Philo,J.S. (2000) A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Anal. Biochem., 279, 151-163.
    • (2000) Anal. Biochem. , vol.279 , pp. 151-163
    • Philo, J.S.1
  • 16
    • 0027432916 scopus 로고
    • A deletion mutant of the type 1C restriction endonuclease EcoR124I expressing a novel DNA specificty
    • Abadjieva,A., Patel,J., Webb,M., Zinkevich,V. and Firman,K. (1993) A deletion mutant of the type 1C restriction endonuclease EcoR124I expressing a novel DNA specificty. Nucleic Acids Res., 21, 4435-4443.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4435-4443
    • Abadjieva, A.1    Patel, J.2    Webb, M.3    Zinkevich, V.4    Firman, K.5
  • 17
    • 0027501321 scopus 로고
    • Macroevolution by transposition: Drastic modification of DNA recognition by a type I restriction enzyme following Tn5 transposition
    • Meister,J., MacWilliams,M., Hubner,P., Jutte,H., Skrzypek,E., Piekarowicz,A. and Bickle,T.A. (1993) Macroevolution by transposition: drastic modification of DNA recognition by a type I restriction enzyme following Tn5 transposition. EMBO J., 12, 4585-4591.
    • (1993) EMBO J. , vol.12 , pp. 4585-4591
    • Meister, J.1    MacWilliams, M.2    Hubner, P.3    Jutte, H.4    Skrzypek, E.5    Piekarowicz, A.6    Bickle, T.A.7
  • 18
    • 0031971082 scopus 로고    scopus 로고
    • Expression and characterisation of the N-terminal fragment of the HsdS subunit of M.EcoR124I
    • Smith,M.A., Mernagh,D.R. and Kneale,G.G. (1998) Expression and characterisation of the N-terminal fragment of the HsdS subunit of M.EcoR124I. Biol. Chem., 379, 505-510.
    • (1998) Biol. Chem. , vol.379 , pp. 505-510
    • Smith, M.A.1    Mernagh, D.R.2    Kneale, G.G.3
  • 19
    • 0035900560 scopus 로고    scopus 로고
    • Domain structure and subunit interactions in the type I DNA methyltransferase M.EcoR124I
    • Smith,M., Read,C.M. and Kneale,G.G. (2001) Domain structure and subunit interactions in the type I DNA methyltransferase M.EcoR124I. J. Mol. Biol., 314, 41-50.
    • (2001) J. Mol. Biol. , vol.314 , pp. 41-50
    • Smith, M.1    Read, C.M.2    Kneale, G.G.3
  • 20
    • 0017730133 scopus 로고
    • EcoRI methylase: Physical and catalytic properties of the homogenous enzyme
    • Rubin,R.A. and Modrich,P. (1977) EcoRI methylase: physical and catalytic properties of the homogenous enzyme. J. Biol. Chem., 252, 7265-7272.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7265-7272
    • Rubin, R.A.1    Modrich, P.2
  • 21
    • 0025772075 scopus 로고
    • Kinetic mechanism of EcoRI DNA methyltransferase
    • Reich,N.O. and Mashhoon,N. (1991) Kinetic mechanism of EcoRI DNA methyltransferase. Biochemistry, 30, 2933-2929.
    • (1991) Biochemistry , vol.30 , pp. 2929-2933
    • Reich, N.O.1    Mashhoon, N.2
  • 22
    • 0028327426 scopus 로고
    • The domains of a type I DNA methyltransferase: Interactions and role in recognition of DNA methylation
    • Cooper,L.P. and Dryden,D.T.F. (1994) The domains of a type I DNA methyltransferase: interactions and role in recognition of DNA methylation. J. Mol. Biol., 236, 1011-1021.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1011-1021
    • Cooper, L.P.1    Dryden, D.T.F.2
  • 23
    • 0032509099 scopus 로고    scopus 로고
    • The DNA recognition subunit of the type IB restriction-modification enzyme EcoAI tolerates circular permutations of its polypeptide chain
    • Janscak,P. and Bickle,T.A. (1998) The DNA recognition subunit of the type IB restriction-modification enzyme EcoAI tolerates circular permutations of its polypeptide chain. J. Mol. Biol., 284, 937-948.
    • (1998) J. Mol. Biol. , vol.284 , pp. 937-948
    • Janscak, P.1    Bickle, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.