메뉴 건너뛰기




Volumn 17, Issue 22, 1998, Pages 6757-6766

Crosslinking the EcoRV restriction endonuclease across the DNA-binding site reveals transient intermediates and conformational changes of the enzyme during DNA binding and catalytic turnover

Author keywords

Protein DNA association; Protein DNA interaction; Restriction endonuclease; Restriction modification system; Specificity

Indexed keywords

BACTERIAL DNA; CIRCULAR DNA; RESTRICTION ENDONUCLEASE;

EID: 0032538889     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.22.6757     Document Type: Article
Times cited : (15)

References (22)
  • 1
    • 0030002197 scopus 로고    scopus 로고
    • A helical arch allowing single-stranded DNA to thread through T5 5′-exonuclease
    • Ceska, T.A., Sayers, J.R., Stier, G. and Suck, D. (1996) A helical arch allowing single-stranded DNA to thread through T5 5′-exonuclease. Nature, 382, 90-93.
    • (1996) Nature , vol.382 , pp. 90-93
    • Ceska, T.A.1    Sayers, J.R.2    Stier, G.3    Suck, D.4
  • 2
    • 0030985132 scopus 로고    scopus 로고
    • Rapid-reaction analysis of plasmid DNA cleavage by the EcoRV restriction endonuclease
    • Erskine, S.G., Baldwin, G.S. and 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
  • 3
    • 0344682577 scopus 로고    scopus 로고
    • Synthesis and biochemical characterization of obligatory dimers of the sugar non-specific nuclease from Serratia marcescens using specifically designed bismaleimidoalkanes as SH-specific crosslinking reagents
    • in press
    • Franke, I. and Pingoud, A. (1998) Synthesis and biochemical characterization of obligatory dimers of the sugar non-specific nuclease from Serratia marcescens using specifically designed bismaleimidoalkanes as SH-specific crosslinking reagents. J. Prot. Chem., in press.
    • (1998) J. Prot. Chem.
    • Franke, I.1    Pingoud, A.2
  • 4
    • 0022504314 scopus 로고
    • Relaxed specificity of the EcoRV restriction endonuclease
    • Halford, S.E., Lovelady, B.M. and McCallum, S.A. (1986) Relaxed specificity of the EcoRV restriction endonuclease. Gene, 41, 173-181.
    • (1986) Gene , vol.41 , pp. 173-181
    • Halford, S.E.1    Lovelady, B.M.2    McCallum, S.A.3
  • 5
    • 0032562139 scopus 로고    scopus 로고
    • Kinetic characterization of linear diffusion of the restriction endonuclease EcoRV on DNA
    • Jeltsch, A. and Pingoud, A. (1998) Kinetic characterization of linear diffusion of the restriction endonuclease EcoRV on DNA. Biochemistry, 37, 2160-2169.
    • (1998) Biochemistry , vol.37 , pp. 2160-2169
    • Jeltsch, A.1    Pingoud, A.2
  • 7
    • 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. and 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
  • 8
    • 0028988416 scopus 로고
    • 2+ binding to the active site of EcoRV endonuclease: A crystallographic study of complexes with substrate and product DNA at 2 Å resolution
    • 2+ binding to the active site of 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
  • 9
    • 0029616338 scopus 로고
    • Calf 5′ to 3′ exo/ endonuclease must slide from a 5′ end of the substrate to perform structure-specific cleavage
    • Murante, R.S., Rust, L. and Bambara, R.A. (1995) Calf 5′ to 3′ exo/ endonuclease must slide from a 5′ end of the substrate to perform structure-specific cleavage. J. Biol. Chem., 270, 30377-30383.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30377-30383
    • Murante, R.S.1    Rust, L.2    Bambara, R.A.3
  • 10
    • 0031576347 scopus 로고    scopus 로고
    • Conformational transition and structural deformability of EcoRV endonuclease revealed by crystallographic analysis
    • Perona, J.J. and Martin, A.M. (1997) Conformational transition and structural deformability of EcoRV endonuclease revealed by crystallographic analysis. J. Mol. Biol., 273, 207-225.
    • (1997) J. Mol. Biol. , vol.273 , pp. 207-225
    • Perona, J.J.1    Martin, A.M.2
  • 11
    • 0030911133 scopus 로고    scopus 로고
    • Recognition and cleavage of DNA by type-II restriction endonucleases
    • Pingoud, A. and 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
    • 0002598414 scopus 로고
    • Type II restriction enzymes
    • Linn, S.M. Lloyd, R.S. and Roberts, R.J. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Roberts, R.J. and Halford, S.E. (1993) Type II restriction enzymes. In Linn, S.M. Lloyd, R.S. and Roberts, R.J. (eds), Nucleases. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 35-88.
    • (1993) Nucleases , pp. 35-88
    • Roberts, R.J.1    Halford, S.E.2
  • 14
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R.S. and Record, M.T., Jr (1994) Coupling of local folding to site-specific binding of proteins to DNA. Science, 263, 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 15
    • 0029994359 scopus 로고    scopus 로고
    • Introduction of asymmetry in the naturally symmetric restriction endonuclease EcoRV to investigate intersubunit communication in the homodimeric protein
    • Stahl, F., Wende, W., Jeltsch, A. and Pingoud, A. (1996) Introduction of asymmetry in the naturally symmetric restriction endonuclease EcoRV to investigate intersubunit communication in the homodimeric protein. Proc. Natl Acad. Sci. USA, 93, 6175-6180.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6175-6180
    • Stahl, F.1    Wende, W.2    Jeltsch, A.3    Pingoud, A.4
  • 16
    • 0025889005 scopus 로고
    • EcoRV restriction endonuclease binds all DNA sequences with equal affinity
    • Taylor, J.D., Badcoe, I.G., Clarke, A.R. and 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
  • 17
    • 0025819774 scopus 로고
    • Site-directed mutagenesis studies with EcoRV restriction endonuclease to identify regions involved in recognition and catalysis
    • Thielking, V., Selent, U., Köhler, E., Wolfes, H., Pieper, U., Geiger, R., Urbanke, C., Winkler, F.K. and Pingoud, A. (1991) Site-directed mutagenesis studies with EcoRV restriction endonuclease to identify regions involved in recognition and catalysis. Biochemistry, 30, 6416-6422.
    • (1991) Biochemistry , vol.30 , pp. 6416-6422
    • Thielking, V.1    Selent, U.2    Köhler, E.3    Wolfes, H.4    Pieper, U.5    Geiger, R.6    Urbanke, C.7    Winkler, F.K.8    Pingoud, A.9
  • 18
    • 0028934112 scopus 로고
    • Specific DNA recognition by EcoRV restriction endonuclease induced by calcium ions
    • Vipond, I.B. and Halford, S.E. (1995) Specific DNA recognition by EcoRV restriction endonuclease induced by calcium ions. Biochemistry, 34, 1113-1119.
    • (1995) Biochemistry , vol.34 , pp. 1113-1119
    • Vipond, I.B.1    Halford, S.E.2
  • 19
    • 0029858708 scopus 로고    scopus 로고
    • The production and characterization of artificial heterodimers of the restriction endonuclease EcoRV
    • Wende, W., Stahl, F. and Pingoud A. (1996) The production and characterization of artificial heterodimers of the restriction endonuclease EcoRV. Biol. Chem., 377, 625-632.
    • (1996) Biol. Chem. , vol.377 , pp. 625-632
    • Wende, W.1    Stahl, F.2    Pingoud, A.3
  • 20
    • 0028023146 scopus 로고
    • Protein engineering of the restriction endonuclease EcoRV: Replacement of an amino acid residue in the DNA binding site leads to an altered selectivity towards unmodified and modified substrates
    • Wenz, C. Selent, U., Wende, W., Jeltsch, A., Wolfes, H. and Pingoud, A. (1994) Protein engineering of the restriction endonuclease EcoRV: replacement of an amino acid residue in the DNA binding site leads to an altered selectivity towards unmodified and modified substrates. Biochim. Biophys. Acta, 1219, 73-80.
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 73-80
    • Wenz, C.1    Selent, U.2    Wende, W.3    Jeltsch, A.4    Wolfes, H.5    Pingoud, A.6
  • 21
    • 0029975922 scopus 로고    scopus 로고
    • Probing the indirect readout of the restriction enzyme EcoRV
    • Wenz, C., Jeltsch, A. and Pingoud, A. (1996) Probing the indirect readout of the restriction enzyme EcoRV. J. Biol. Chem., 271, 5565-5573.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5565-5573
    • Wenz, C.1    Jeltsch, A.2    Pingoud, A.3
  • 22
    • 0027159254 scopus 로고
    • The crystal structure of EcoRV endonuclease and of its complexes with cognate and non-cognate DNA fragments
    • Winkler, F.K. et al. (1993) The crystal structure of EcoRV endonuclease and of its complexes with cognate and non-cognate DNA fragments. EMBO J., 12, 1781-1795.
    • (1993) EMBO J. , vol.12 , pp. 1781-1795
    • Winkler, F.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.