메뉴 건너뛰기




Volumn 275, Issue 5, 1998, Pages 759-772

Reactions of the EcoRV restriction endonuclease with fluorescent oligodeoxynucleotides: Identical equilibrium constants for binding to specific and non-specific DNA

Author keywords

DNA recognition; DNA protein interaction; Fluorescence depolarization; Fluorescence resonance energy transfer; Restriction modification

Indexed keywords

DANSYL CHLORIDE; EOSIN; MAGNESIUM ION; OLIGODEOXYNUCLEOTIDE; RESTRICTION ENDONUCLEASE; DNA; ENDODEOXYRIBONUCLEASE ECORV; FLUORESCENT DYE; OLIGODEOXYRIBONUCLEOTIDE; TYPE II SITE SPECIFIC DEOXYRIBONUCLEASE;

EID: 0032488670     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1517     Document Type: Article
Times cited : (44)

References (65)
  • 1
    • 0028932881 scopus 로고
    • Structure and function of restriction endonucleases
    • Aggarwal, A. K. (1995). Structure and function of restriction endonucleases. Curr. Opin. Struct. Biol. 5, 11-19.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 11-19
    • Aggarwal, A.K.1
  • 2
    • 0029097035 scopus 로고
    • Accuracy of the EcoRV restriction endonuclease: Binding and cleavage studies with oligonucleotide substrates
    • Alves, J., Selent, U. & Wolfes, H. (1995). Accuracy of the EcoRV restriction endonuclease: binding and cleavage studies with oligonucleotide substrates. Biochemistry, 34, 11191-11197.
    • (1995) Biochemistry , vol.34 , pp. 11191-11197
    • Alves, J.1    Selent, U.2    Wolfes, H.3
  • 3
    • 0028936107 scopus 로고
    • Rapid reaction analysis of the catalytic cycle of the EcoRV restriction endonuclease
    • Baldwin, G. S., Vipond, I. B. & Halford, S. E. (1995). Rapid reaction analysis of the catalytic cycle of the EcoRV restriction endonuclease. Biochemistry, 34, 705-714.
    • (1995) Biochemistry , vol.34 , pp. 705-714
    • Baldwin, G.S.1    Vipond, I.B.2    Halford, S.E.3
  • 4
    • 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, 3659-3678.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 3659-3678
    • Bougueleret, L.1    Schwarzstein, M.2    Tsugita, A.3    Zabeau, M.4
  • 5
  • 6
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin reaction cycle
    • Burston, S. G., Ransom, N. A. & Clarke, A. R. (1995). The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol. 249, 138-152.
    • (1995) J. Mol. Biol. , vol.249 , pp. 138-152
    • Burston, S.G.1    Ransom, N.A.2    Clarke, A.R.3
  • 7
    • 0030059614 scopus 로고    scopus 로고
    • The EcoRV modification methylase causes considerable bending of DNA upon binding to its recognition site GATATC
    • Cal, S. & Connolly, B. A. (1996). The EcoRV modification methylase causes considerable bending of DNA upon binding to its recognition site GATATC. J. Biol. Chem. 271, 1008-1015.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1008-1015
    • Cal, S.1    Connolly, B.A.2
  • 8
    • 0345593506 scopus 로고
    • Genetic and spectroscopic characterisation of structural changes in dehydrogenase enzymes and their substrates during enzyme catalysis
    • Clarke, A. R., Cortes, A., Halsall, D. J., Hart, K. W. & Holbrook, J. J. (1991). Genetic and spectroscopic characterisation of structural changes in dehydrogenase enzymes and their substrates during enzyme catalysis. Spec. Publ. Roy. Soc. Chem. 94, 223-226.
    • (1991) Spec. Publ. Roy. Soc. Chem. , vol.94 , pp. 223-226
    • Clarke, A.R.1    Cortes, A.2    Halsall, D.J.3    Hart, K.W.4    Holbrook, J.J.5
  • 9
    • 0027394243 scopus 로고
    • Observing the helical geometry of double-stranded DNA in solution by fluorescence resonance energy transfer
    • Clegg, R. M., Murchie, A. I. H., Zechel, A. & Lilley, D. M. J. (1993). Observing the helical geometry of double-stranded DNA in solution by fluorescence resonance energy transfer. Proc. Natl Acad. Sci. USA, 90, 2994-2998.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2994-2998
    • Clegg, R.M.1    Murchie, A.I.H.2    Zechel, A.3    Lilley, D.M.J.4
  • 10
    • 0023649588 scopus 로고
    • The synthesis of oligonucleotides containing a primary amino group at the 5′-terminus
    • Connolly, B. A. (1987). The synthesis of oligonucleotides containing a primary amino group at the 5′-terminus. Nucl. Acids Res. 15, 3131-3139.
    • (1987) Nucl. Acids Res. , vol.15 , pp. 3131-3139
    • Connolly, B.A.1
  • 11
    • 0021993083 scopus 로고
    • Purification and crystallization of the EcoRV restriction endonuclease
    • D'Arcy, A., Brown, R. S., Zabeau, M., van Resandt, R. W. & Winkler, F. K. (1985). Purification and crystallization of the EcoRV restriction endonuclease. J. Biol. Chem. 260, 1987-1990.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1987-1990
    • D'Arcy, A.1    Brown, R.S.2    Zabeau, M.3    Van Resandt, R.W.4    Winkler, F.K.5
  • 12
    • 0031591392 scopus 로고    scopus 로고
    • Specific binding by EcoRV endonuclease to its DNA recognition site GATATC
    • Engler, L. E., Welch, K. K. & Jen-Jacobson, L. (1997). Specific binding by EcoRV endonuclease to its DNA recognition site GATATC. J. Mol. Biol. 269, 82-101.
    • (1997) J. Mol. Biol. , vol.269 , pp. 82-101
    • Engler, L.E.1    Welch, K.K.2    Jen-Jacobson, L.3
  • 13
    • 0029071725 scopus 로고
    • Interactions of the EcoRV restriction endonuclease with fluorescent oligodeoxynucleotides
    • Erskine, S. G. & Halford, S. E. (1995). Interactions of the EcoRV restriction endonuclease with fluorescent oligodeoxynucleotides. Gene, 157, 153-156.
    • (1995) Gene , vol.157 , pp. 153-156
    • Erskine, S.G.1    Halford, S.E.2
  • 14
    • 0030985132 scopus 로고    scopus 로고
    • Rapid reaction analysis of plasmid DNA cleavage by the EcoRV restriction endonuclease
    • Erskine, S. G., Baldwin, G. S. & Halford, S. E. (1997). Rapid reaction analysis of plasmid DNA cleavage by the EcoRV restriction endonuclease. Biochemistry, 36, 7567-7576.
    • (1997) Biochemistry , vol.36 , pp. 7567-7576
    • Erskine, S.G.1    Baldwin, G.S.2    Halford, S.E.3
  • 15
    • 0025790430 scopus 로고
    • Interaction of DNA with the Klenow fragment of DNA polymerase I studied by time-resolved fluorescence spectroscopy
    • Guest, C. R., Hochstrasser, R. A., Dupuy, C. G., Allen, D. J., Benkovic, S. J. & Millar, D. P. (1991). Interaction of DNA with the Klenow fragment of DNA polymerase I studied by time-resolved fluorescence spectroscopy. Biochemistry, 30, 8759-8770.
    • (1991) Biochemistry , vol.30 , pp. 8759-8770
    • Guest, C.R.1    Hochstrasser, R.A.2    Dupuy, C.G.3    Allen, D.J.4    Benkovic, S.J.5    Millar, D.P.6
  • 17
    • 0016806339 scopus 로고
    • Stopped-flow fluorescence studies on saccharide binding to lysozyme
    • Halford, S. E. (1975). Stopped-flow fluorescence studies on saccharide binding to lysozyme. Biochem. J. 149, 411-422.
    • (1975) Biochem. J. , vol.149 , pp. 411-422
    • Halford, S.E.1
  • 18
    • 0024281289 scopus 로고
    • Modes of DNA cleavage by the EcoRV restriction endonuclease
    • Halford, S. E. & Goodall, A. J. (1988). Modes of DNA cleavage by the EcoRV restriction endonuclease. Biochemistry, 27, 1771-1777.
    • (1988) Biochemistry , vol.27 , pp. 1771-1777
    • Halford, S.E.1    Goodall, A.J.2
  • 19
    • 0019186907 scopus 로고
    • The EcoRI restriction endonuclease with bacteriophage DNA: Equilibrium binding studies
    • Halford, S. E. & Johnson, N. P. (1980). The EcoRI restriction endonuclease with bacteriophage (DNA: equilibrium binding studies. Biochem. J. 191, 593-604.
    • (1980) Biochem. J. , vol.191 , pp. 593-604
    • Halford, S.E.1    Johnson, N.P.2
  • 20
    • 0022504314 scopus 로고
    • Relaxed specificity of the EcoRV restriction endonuclease
    • Halford, S. E., Lovelady, B. M. & McCallum, S. A. (1986). Relaxed specificity of the EcoRV restriction endonuclease. Gene, 41, 173-185.
    • (1986) Gene , vol.41 , pp. 173-185
    • Halford, S.E.1    Lovelady, B.M.2    McCallum, S.A.3
  • 21
    • 0011185190 scopus 로고
    • Mechanism of action of restriction endonuclease EcoRV
    • (Eckstein, F. & Lilley, D. M. J., eds), Springer, Berlin, Germany
    • Halford, S. E., Taylor, J. D., Vermote, C. L. M. & Vipond, I. B. (1993). Mechanism of action of restriction endonuclease EcoRV. In Nucleic Acids and Molecular Biology (Eckstein, F. & Lilley, D. M. J., eds), vol. 7, pp. 47-69, Springer, Berlin, Germany.
    • (1993) Nucleic Acids and Molecular Biology , vol.7 , pp. 47-69
    • Halford, S.E.1    Taylor, J.D.2    Vermote, C.L.M.3    Vipond, I.B.4
  • 22
    • 0030900407 scopus 로고    scopus 로고
    • Kinetic analysis of a mutational hot-spot in the EcoRV restriction endonuclease
    • Hancox, E. L. & Halford, S. E. (1997). Kinetic analysis of a mutational hot-spot in the EcoRV restriction endonuclease. Biochemistry, 36, 7577-7585.
    • (1997) Biochemistry , vol.36 , pp. 7577-7585
    • Hancox, E.L.1    Halford, S.E.2
  • 24
    • 0025261344 scopus 로고
    • Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction
    • Heyduk, T. & Lee, J. C. (1990). Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction. Proc. Natl Acad. Sci. USA, 87, 1744-1748.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1744-1748
    • Heyduk, T.1    Lee, J.C.2
  • 26
    • 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. (1996). 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
  • 27
    • 0016624901 scopus 로고
    • Binding energy, specificity and enzymic catalysis: The Circe effect
    • Jencks, W. P. (1975). Binding energy, specificity and enzymic catalysis: the Circe effect. Adv. Enzymol. Relat. Areas Mol. Biol. 43, 219-410.
    • (1975) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.43 , pp. 219-410
    • Jencks, W.P.1
  • 29
    • 0028988416 scopus 로고
    • 2+ binding to the active site of the EcoRV endonuclease: A crystallographic study of complexes with substrate and product DNA at 2 Å resolution
    • 2+ binding to the active site of the EcoRV endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 Å resolution. Biochemistry, 34, 683-696.
    • (1995) Biochemistry , vol.34 , pp. 683-696
    • Kostrewa, D.1    Winkler, F.K.2
  • 30
    • 0030885532 scopus 로고    scopus 로고
    • DNA binding specificity of MunI restriction endonuclease is controlled by pH and calcium ions: Involvement of active site carboxylate residues
    • Lagunavicius, A., Grazulis, S., Balciunaite, E., Vainius, D. & Siksnys, V. (1997). DNA binding specificity of MunI restriction endonuclease is controlled by pH and calcium ions: involvement of active site carboxylate residues. Biochemistry, 36, 11093-11099.
    • (1997) Biochemistry , vol.36 , pp. 11093-11099
    • Lagunavicius, A.1    Grazulis, S.2    Balciunaite, E.3    Vainius, D.4    Siksnys, V.5
  • 33
    • 0028036709 scopus 로고
    • Interactions of TaqI endonuclease with the phosphate backbone
    • Mayer, A. N. & Barany, F. (1994). Interactions of TaqI endonuclease with the phosphate backbone. J. Biol. Chem. 269, 29067-29076.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29067-29076
    • Mayer, A.N.1    Barany, F.2
  • 34
    • 0025165469 scopus 로고
    • Interaction of the EcoRV restriction endonuclease with the deoxyadenosine and thymidine bases in its recognition hexamer d(GATATC)
    • Newman, P. C., Williams, D. M., Cosstick, R., Seela, F. & Connolly, B. A. (1990). Interaction of the EcoRV restriction endonuclease with the deoxyadenosine and thymidine bases in its recognition hexamer d(GATATC). Biochemistry, 29, 9902-9910.
    • (1990) Biochemistry , vol.29 , pp. 9902-9910
    • Newman, P.C.1    Williams, D.M.2    Cosstick, R.3    Seela, F.4    Connolly, B.A.5
  • 35
    • 0027453423 scopus 로고
    • DNA recognition by the EcoK methyltransferase: The influence of DNA methylation and the cofactor S-adenosyl methionine
    • Powell, L. M., Dryden, D. T. F., Willcock, D. F., Pain, R. H. & Murray, N. E. (1993). DNA recognition by the EcoK methyltransferase: the influence of DNA methylation and the cofactor S-adenosyl 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
  • 36
    • 0002598414 scopus 로고
    • Type II restriction endonucleases
    • (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 endonucleases. 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
  • 37
    • 0021152929 scopus 로고
    • The recognition sequence for EcoRV is GAT/ATC
    • Schildkraut, I., Banner, C. D. B., Rhodes, C. S. & Parekh, S. (1984). The recognition sequence for EcoRV is GAT/ATC. Gene, 27, 327-329.
    • (1984) Gene , vol.27 , pp. 327-329
    • Schildkraut, I.1    Banner, C.D.B.2    Rhodes, C.S.3    Parekh, S.4
  • 38
    • 0026696177 scopus 로고
    • A site-directed mutagenesis study to identify amino acid residues involved in the catalytic function of the restriction endonuclease EcoRV
    • Selent, U., Ruter, T., Köhler, E., Liedtke, M., Thielking, V., Alves, J., Oelgeschläger, T., Wolfes, H., Peters, F. & Pingoud, A. (1992). A site-directed mutagenesis study to identify amino acid residues involved in the catalytic function of the restriction endonuclease EcoRV. Biochemistry, 31, 4808-4815.
    • (1992) Biochemistry , vol.31 , pp. 4808-4815
    • Selent, U.1    Ruter, T.2    Köhler, E.3    Liedtke, M.4    Thielking, V.5    Alves, J.6    Oelgeschläger, T.7    Wolfes, H.8    Peters, F.9    Pingoud, A.10
  • 39
    • 0027420804 scopus 로고
    • Catalytic and binding properties of restriction endonuclease Cfr9I
    • Siksnys, V. & Pleckaityte, M. (1993). Catalytic and binding properties of restriction endonuclease Cfr9I. Eur. J. Biochem. 217, 411-419.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 411-419
    • Siksnys, V.1    Pleckaityte, M.2
  • 40
    • 0028043346 scopus 로고
    • Genetic recombination in E. coli: RuvC protein cleaves Holliday junctions at resolution hotspots in vitro
    • Shah, R., Bennett, R. J. & West, S. C. (1994). Genetic recombination in E. coli: RuvC protein cleaves Holliday junctions at resolution hotspots in vitro. Cell, 79, 853-864.
    • (1994) Cell , vol.79 , pp. 853-864
    • Shah, R.1    Bennett, R.J.2    West, S.C.3
  • 41
    • 0030936839 scopus 로고    scopus 로고
    • The RuvC dimer resolves Holliday junctions by a dual incision mechanism that involves base-specific contacts
    • Shah, R., Cosstick, R. & West, S. C. (1997). The RuvC dimer resolves Holliday junctions by a dual incision mechanism that involves base-specific contacts. EMBO J. 16, 1464-1472.
    • (1997) EMBO J. , vol.16 , pp. 1464-1472
    • Shah, R.1    Cosstick, R.2    West, S.C.3
  • 43
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer, L. (1978). Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47, 819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 44
    • 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
  • 45
    • 0029978713 scopus 로고    scopus 로고
    • Recombination by resolvase to analyse DNA communications by the SfiI restriction endonuclease
    • Szczelkun, M. D. & Halford, S. E. (1996). Recombination by resolvase to analyse DNA communications by the SfiI restriction endonuclease. EMBO J. 15, 1460-1469.
    • (1996) EMBO J. , vol.15 , pp. 1460-1469
    • Szczelkun, M.D.1    Halford, S.E.2
  • 46
    • 0024322164 scopus 로고
    • Discrimination between DNA sequences by the EcoRV restriction endonuclease
    • Taylor, J. D. & Halford, S. E. (1989). Discrimination between DNA sequences by the EcoRV restriction endonuclease. Biochemistry, 28, 6198-6207.
    • (1989) Biochemistry , vol.28 , pp. 6198-6207
    • Taylor, J.D.1    Halford, S.E.2
  • 47
    • 0026569359 scopus 로고
    • The activity of the EcoRV restriction endonuclease is influenced by flanking DNA sequences both inside and outside the DNA-protein complex
    • Taylor, J. D. & Halford, S. E. (1992). The activity of the EcoRV restriction endonuclease is influenced by flanking DNA sequences both inside and outside the DNA-protein complex. Biochemistry, 31, 90-97.
    • (1992) Biochemistry , vol.31 , pp. 90-97
    • Taylor, J.D.1    Halford, S.E.2
  • 48
    • 0025889005 scopus 로고
    • EcoRV restriction endonuclease binds all DNA sequences with equal affinity
    • Taylor, J. D., Badcoe, I. G., Clarke, A. R. & Halford, S. E. (1991). EcoRV restriction endonuclease binds all DNA sequences with equal affinity. Biochemistry, 30, 8743-8753.
    • (1991) Biochemistry , vol.30 , pp. 8743-8753
    • Taylor, J.D.1    Badcoe, I.G.2    Clarke, A.R.3    Halford, S.E.4
  • 49
    • 0021112461 scopus 로고
    • Thermodynamic parameters governing interaction of EcoRI endonuclease with specific and nonspecific DNA sequences
    • Terry, B. J., Jack, W. E. & Modrich, P. (1983). Thermodynamic parameters governing interaction of EcoRI endonuclease with specific and nonspecific DNA sequences. J. Biol. Chem. 258, 9820-9825.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9820-9825
    • Terry, B.J.1    Jack, W.E.2    Modrich, P.3
  • 50
    • 0022381905 scopus 로고
    • Facilitated diffusion during catalysis by EcoRI endonuclease
    • Terry, B. J., Jack, W. E. & Modrich, P. (1985). Facilitated diffusion during catalysis by EcoRI endonuclease. 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
  • 52
    • 0029991992 scopus 로고    scopus 로고
    • Influence of the phosphate backbone on the recognition and hydrolysis of DNA by the EcoRV restriction endonuclease - A study using oligodeoxy-nucleotide phosphorothioates
    • Thorogood, H., Grasby, J. A. & Connolly, B. A. (1996a). Influence of the phosphate backbone on the recognition and hydrolysis of DNA by the EcoRV restriction endonuclease - a study using oligodeoxy-nucleotide phosphorothioates. J. Biol. Chem. 271, 8855-8862.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8855-8862
    • Thorogood, H.1    Grasby, J.A.2    Connolly, B.A.3
  • 53
    • 0029984146 scopus 로고    scopus 로고
    • Resonance raman spectroscopy of 4-thiothymidine and oligodeoxy-nucleotides containing this base both free in solution and bound to the restriction endonuclease EcoRV
    • Thorogood, H., Waters, T. R., Parker, A. W., Wharton, C. W. & Connolly, B. A. (1996b). Resonance raman spectroscopy of 4-thiothymidine and oligodeoxy-nucleotides containing this base both free in solution and bound to the restriction endonuclease EcoRV. Biochemistry, 35, 8723-8733.
    • (1996) Biochemistry , vol.35 , pp. 8723-8733
    • Thorogood, H.1    Waters, T.R.2    Parker, A.W.3    Wharton, C.W.4    Connolly, B.A.5
  • 54
    • 0026755152 scopus 로고
    • EcoRV restriction endonuclease: Communication between DNA recognition and catalysis
    • Vermote, C. L. M., Vipond, I. B. & Halford, S. E. (1992). EcoRV restriction endonuclease: communication between DNA recognition and catalysis. Biochemistry, 31, 6089-6097.
    • (1992) Biochemistry , vol.31 , pp. 6089-6097
    • Vermote, C.L.M.1    Vipond, I.B.2    Halford, S.E.3
  • 56
    • 0030053257 scopus 로고    scopus 로고
    • An isoleucine-to-leucine mutation that switches the cofactor requirement of the EcoRV restriction endonuclease from magnesium to manganese
    • Vipond, I. B., Moon, B-J. & Halford, S. E. (1996). An isoleucine-to-leucine mutation that switches the cofactor requirement of the EcoRV restriction endonuclease from magnesium to manganese. Biochemistry, 35, 1712-1721.
    • (1996) Biochemistry , vol.35 , pp. 1712-1721
    • Vipond, I.B.1    Moon, B.-J.2    Halford, S.E.3
  • 57
    • 0030790696 scopus 로고    scopus 로고
    • Structure of the multi-modular endonuclease FokI bound to DNA
    • Wah, D. A., Hirsch, J. A., Dorner, L. F., Schildkraut, I. & Aggarwal, A. K. (1997). Structure of the multi-modular endonuclease FokI bound to DNA. Nature, 388, 97-100.
    • (1997) Nature , vol.388 , pp. 97-100
    • Wah, D.A.1    Hirsch, J.A.2    Dorner, L.F.3    Schildkraut, I.4    Aggarwal, A.K.5
  • 58
    • 0026627728 scopus 로고
    • Continuous spectrophotometric assay for endonucleases using synthetic oligodeoxynucleotides and based on the hyperchromic effect
    • Waters, T. R. & Connolly, B. A. (1992). Continuous spectrophotometric assay for endonucleases using synthetic oligodeoxynucleotides and based on the hyperchromic effect. Anal. Biochem. 204, 204-209.
    • (1992) Anal. Biochem. , vol.204 , pp. 204-209
    • Waters, T.R.1    Connolly, B.A.2
  • 59
    • 0028354227 scopus 로고
    • Interaction of restriction endonuclease EcoRV with the deoxyguanosine and deoxycytidine bases in its recognition sequence
    • Waters, T. R. & Connolly, B. A. (1994). Interaction of restriction endonuclease EcoRV with the deoxyguanosine and deoxycytidine bases in its recognition sequence. Biochemistry, 34, 1812-1819.
    • (1994) Biochemistry , vol.34 , pp. 1812-1819
    • Waters, T.R.1    Connolly, B.A.2
  • 60
    • 0029975922 scopus 로고    scopus 로고
    • Probing the indirect readout of the restriction endonuclease EcoRV
    • Wenz, C., Jeltsch, A. & Pingoud, A. (1996). Probing the indirect readout of the restriction endonuclease EcoRV. J. Biol. Chem. 211, 5565-5573.
    • (1996) J. Biol. Chem. , vol.211 , pp. 5565-5573
    • Wenz, C.1    Jeltsch, A.2    Pingoud, A.3
  • 62
    • 0028967016 scopus 로고
    • Sequence-specific DNA recognition by the SmaI endonuclease
    • Withers, B. E. & Dunbar, J. C. (1995). Sequence-specific DNA recognition by the SmaI endonuclease. J. Biol. Chem. 270, 6496-6504.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6496-6504
    • Withers, B.E.1    Dunbar, J.C.2
  • 63
    • 0025865885 scopus 로고
    • Isolation of BamHI variants with reduced cleavage activities
    • Xu, S.-Y. & Schildkraut, I. (1991). Isolation of BamHI variants with reduced cleavage activities. J. Biol. Chem. 266, 4425-4429.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4425-4429
    • Xu, S.-Y.1    Schildkraut, I.2
  • 64
    • 0026722915 scopus 로고
    • Characterization of steady-state, single-turnover and binding kinetics of the TaqI restriction endonuclease
    • Zebala, J. F., Choi, J. & Barany, F. (1992a). Characterization of steady-state, single-turnover and binding kinetics of the TaqI restriction endonuclease. J. Biol. Chem. 267, 8097-8105.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8097-8105
    • Zebala, J.F.1    Choi, J.2    Barany, F.3
  • 65
    • 0026744561 scopus 로고
    • DNA recognition of base analogue and chemically modified substrates by the TaqI restriction endonuclease
    • Zebala, J. F., Choi, J., Trainor, J. & Barany, F. (1992b). DNA recognition of base analogue and chemically modified substrates by the TaqI restriction endonuclease. J. Biol. Chem. 267, 8106-8116.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8106-8116
    • Zebala, J.F.1    Choi, J.2    Trainor, J.3    Barany, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.