메뉴 건너뛰기




Volumn 251, Issue 3, 1998, Pages 899-906

The Flavobacterium okeanokoites adenine-N6-specific DNA- methyltransferase M.FokI is a tandem enzyme of two independent domains with very different kinetic properties

Author keywords

DNA modification; N6 methyladenine; Protein nucleic acid interaction; Restriction modification system; Specificity

Indexed keywords

DNA METHYLTRANSFERASE;

EID: 0032006084     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2510899.x     Document Type: Article
Times cited : (22)

References (21)
  • 1
    • 0028946713 scopus 로고
    • DNA modification by methyltransferases
    • Cheng, X. (1995a) DNA modification by methyltransferases, Curr. Opin. Struct. Biol. 5, 4-10.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 4-10
    • Cheng, X.1
  • 2
    • 0029163078 scopus 로고
    • Structure and function of DNA methyltransferases
    • Cheng, X. (1995b) 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
  • 3
    • 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. 15, 57-108.
    • (1993) Genet. Eng. , vol.15 , pp. 57-108
    • Heitman, J.1
  • 4
    • 0029904146 scopus 로고    scopus 로고
    • Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison with known structures of methyltransferases and isolation of catalytically inactive single mutants
    • Jeltsch, A., Sobotta, T. & Pingoud, A. (1996) Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison with 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
  • 6
    • 0024440974 scopus 로고
    • Nucleotide sequence of the FokI restriction-modification system: Separate strand-specificity domains in the methyltransferase
    • Looney, M. C., Moran, L. S., Jack, W. E., Fehery, G. R., Benner, J. S., Slatko, B. E. & Wilson, G. G. (1989) Nucleotide sequence of the FokI restriction-modification system: separate strand-specificity domains in the methyltransferase, Gene 80, 193-208.
    • (1989) Gene , vol.80 , pp. 193-208
    • Looney, M.C.1    Moran, L.S.2    Jack, W.E.3    Fehery, G.R.4    Benner, J.S.5    Slatko, B.E.6    Wilson, G.G.7
  • 7
    • 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
  • 9
    • 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
  • 10
    • 0030911133 scopus 로고    scopus 로고
    • Recognition and cleavage of DNA by type-II restriction endonucleases
    • Pingoud, A. & Jeltsch, A. (1997) Recognition and cleavage of DNA by 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
  • 12
    • 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
  • 13
    • 0002598414 scopus 로고
    • Type II restriction enzymes
    • Linn, S. M., Lloyd, R. S. & Roberts, R. J., eds Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY
    • Roberts, R. J. & Halford, S. E. (1993) Type II 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 NY.
    • (1993) Nucleases , pp. 35-88
    • Roberts, R.J.1    Halford, S.E.2
  • 14
    • 0019768975 scopus 로고
    • New restriction endonucleases from Flavobacterium okeanokoites (FokI) and Micrococcus luteus (MluI)
    • Sugisaki, H. & Kanazawa, S. (1981) New restriction endonucleases from Flavobacterium okeanokoites (FokI) and Micrococcus luteus (MluI). Gene 16, 73-78.
    • (1981) Gene , vol.16 , pp. 73-78
    • Sugisaki, H.1    Kanazawa, S.2
  • 15
    • 0024544014 scopus 로고
    • The FokI restriction-modification system. II. 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. II. 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
  • 16
    • 0025797325 scopus 로고
    • Class-IIS restriction enzymes - A review
    • Szybalski, W., Kim, S. C., Hasan, N. & Podhajska, A. J. (1991) Class-IIS restriction enzymes - a review, Gene 100, 13-26.
    • (1991) Gene , vol.100 , pp. 13-26
    • Szybalski, W.1    Kim, S.C.2    Hasan, N.3    Podhajska, A.J.4
  • 17
    • 0026481991 scopus 로고
    • High plasticity of multispecific DNA methyltransferases in the region carrying DNA target recognizing enzyme modules
    • Walter, J., Trautner, T. A. & Noyer-Weidner, M. (1992) High plasticity of multispecific DNA methyltransferases in the region carrying DNA target recognizing enzyme modules, EMBO J. 11, 4445-4450.
    • (1992) EMBO J. , vol.11 , pp. 4445-4450
    • Walter, J.1    Trautner, T.A.2    Noyer-Weidner, M.3
  • 18
    • 0028180206 scopus 로고
    • A novel class of FokI restriction endonuclease mutants that cleave hemi-methylated substrates
    • Waugh, D. S. & Sauer, R. T. (1994) A novel class of FokI restriction endonuclease mutants that cleave hemi-methylated substrates, J. Biol. Chem. 269, 12298-12303.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12298-12303
    • Waugh, D.S.1    Sauer, R.T.2
  • 19
    • 0029858708 scopus 로고    scopus 로고
    • The production and characterization of artificial heterodimers of the restriction endonuclease EcoRV
    • Wende, W., Stahl, F. & Pingoud, A. (1996) The production and characterization of artificial heterodimers of the restriction endonuclease EcoRV, Biol. Chem. Hoppe-Seyler 377, 625-632.
    • (1996) Biol. Chem. Hoppe-Seyler , vol.377 , pp. 625-632
    • Wende, W.1    Stahl, F.2    Pingoud, A.3
  • 21
    • 0020338572 scopus 로고
    • Enhanced expression of cro-beta-galactosidase fusion proteins under the control of the PR promoter of bacteriophage lambda
    • Zabeau, M. & Stanley, K. K. (1982) Enhanced expression of cro-beta-galactosidase fusion proteins under the control of the PR promoter of bacteriophage lambda, EMBO J. 1, 1217-1224.
    • (1982) EMBO J. , vol.1 , pp. 1217-1224
    • Zabeau, M.1    Stanley, K.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.