메뉴 건너뛰기




Volumn 377, Issue 10, 1996, Pages 625-632

The production and characterization of artificial heterodimers of the restriction endonuclease EcoRV

Author keywords

Affinity chromatography; DNA cleavage; Protein nucleic acid interaction; Restriction enzyme; Site directed mutagenesis; Subunit

Indexed keywords

DNA; MUTANT PROTEIN; OLIGODEOXYNUCLEOTIDE; PLASMID DNA; RESTRICTION ENDONUCLEASE;

EID: 0029858708     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm3.1996.377.10.625     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 0020371498 scopus 로고
    • Nucleotide sequence and exact localization of the neomycin phosphotransferase gene from transposon T5
    • Beck, E., Ludwig, G., Auerswald, E.A., Reiss, B., and Schaller, H. (1982). Nucleotide sequence and exact localization of the neomycin phosphotransferase gene from transposon T5. Gene 19, 327-336.
    • (1982) Gene , vol.19 , pp. 327-336
    • Beck, E.1    Ludwig, G.2    Auerswald, E.A.3    Reiss, B.4    Schaller, H.5
  • 2
    • 0027144017 scopus 로고
    • Characterization of a novel form of thymidylate synthase: A heterodimer isolated after specific chemical modification of the immobilized native enzyme
    • Bradshaw, T.P., and Dunlap, R.B. (1993). Characterization of a novel form of thymidylate synthase: a heterodimer isolated after specific chemical modification of the immobilized native enzyme. Biochemistry 32, 12774-12781.
    • (1993) Biochemistry , vol.32 , pp. 12774-12781
    • Bradshaw, T.P.1    Dunlap, R.B.2
  • 3
    • 0014635189 scopus 로고
    • 32P-labelled oligonucleotides on thin layers of DEAE-cellulose
    • 32P-labelled oligonucleotides on thin layers of DEAE-cellulose. Eur. J. Biochem. 11, 395-399.
    • (1969) Eur. J. Biochem. , vol.11 , pp. 395-399
    • Brownlee, G.G.1    Sanger, F.2
  • 5
    • 0028355988 scopus 로고
    • Heterodimeric thymidylate syntheses with C-terminal deletion on one subunit
    • Carreras, C.W., Costi, P.M., and Santi, D.V. (1994). Heterodimeric thymidylate syntheses with C-terminal deletion on one subunit. J. Biol. Chem. 269, 12444-12446.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12444-12446
    • Carreras, C.W.1    Costi, P.M.2    Santi, D.V.3
  • 6
    • 0028024850 scopus 로고
    • Structure of Pvull endonuclease with cognate DNA
    • Cheng, X., Balendiran, K., Schildkraut, I., and Anderson, J.E. (1994). Structure of Pvull endonuclease with cognate DNA. EMBO J. 13, 3927-3935.
    • (1994) EMBO J. , vol.13 , pp. 3927-3935
    • Cheng, X.1    Balendiran, K.2    Schildkraut, I.3    Anderson, J.E.4
  • 7
    • 0028861748 scopus 로고
    • Subunit functional studies of NAD(P)H:quinone oxidoreductase with a heterodimer approach
    • Cui, K., Lu, A.Y., and Yang, C.S. (1995). Subunit functional studies of NAD(P)H:quinone oxidoreductase with a heterodimer approach. Proc. Natl. Acad. Sci. USA92, 1043-1047.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1043-1047
    • Cui, K.1    Lu, A.Y.2    Yang, C.S.3
  • 8
    • 0021993083 scopus 로고
    • Purification and crystallization of the EcoRV restriction endonuclease
    • D'Arcy, A., Brown, R.S., Zabeau, M., van Resandt, R.W., and 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
  • 9
    • 0026535482 scopus 로고
    • Engineering surface charge. 2. A method for purifying heterodimers of Escherichia coli glutathione reductase
    • Deonarain, M.P., Scrutton, N.S., and Perham, R.N. (1992). Engineering surface charge. 2. A method for purifying heterodimers of Escherichia coli glutathione reductase. Biochemistry 37, 1498-1504.
    • (1992) Biochemistry , vol.37 , pp. 1498-1504
    • Deonarain, M.P.1    Scrutton, N.S.2    Perham, R.N.3
  • 10
    • 0025271840 scopus 로고
    • Active site of mercuric reductase resides at the subunit interface and requires Cys135 and Cys140 from one subunit and Cys558 and Cys559 from the adjacent subunit: Evidence from in vivo and in vitro heterodimer formation
    • Distefano, M.D., Moore, M.J., and Walsh, C.T. (1990). Active site of mercuric reductase resides at the subunit interface and requires Cys135 and Cys140 from one subunit and Cys558 and Cys559 from the adjacent subunit: evidence from in vivo and in vitro heterodimer formation. Biochemistry 29, 2703-2713.
    • (1990) Biochemistry , vol.29 , pp. 2703-2713
    • Distefano, M.D.1    Moore, M.J.2    Walsh, C.T.3
  • 11
    • 0027482856 scopus 로고
    • Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline
    • Eriani, G., Cavarelli, J., Martin, F., Dirheimer, G., Moras, D., and Gangloff, J. (1993). Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline. Proc. Natl. Acad. Sci. USA 90, 10816-10820.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10816-10820
    • Eriani, G.1    Cavarelli, J.2    Martin, F.3    Dirheimer, G.4    Moras, D.5    Gangloff, J.6
  • 12
    • 0027433504 scopus 로고
    • Catalytically active cross-species heterodimers of thymidylate synthase
    • Greene, P.J., Maley, F., Pedersen Lane, J., and Santi, D.V. (1993). Catalytically active cross-species heterodimers of thymidylate synthase. Biochemistry 32, 10283-10288.
    • (1993) Biochemistry , vol.32 , pp. 10283-10288
    • Greene, P.J.1    Maley, F.2    Pedersen Lane, J.3    Santi, D.V.4
  • 15
    • 10544226758 scopus 로고
    • Studies on the canonical DNA-EcoRI endonuclease complex and the EcoRI kink
    • R.H. Sarma and M.H. Sarma, eds. (Schenectady, NY, USA: Adenine Press)
    • Kim, Y., Choi, J., Grable, J.C., Greene, P., Hager, P., and Rosenberg, J.M. (1994). Studies on the canonical DNA-EcoRI endonuclease complex and the EcoRI kink. In: Structural Biology, Vol. 1, R.H. Sarma and M.H. Sarma, eds. (Schenectady, NY, USA: Adenine Press), pp. 224-246.
    • (1994) Structural Biology , vol.1 , pp. 224-246
    • Kim, Y.1    Choi, J.2    Grable, J.C.3    Greene, P.4    Hager, P.5    Rosenberg, J.M.6
  • 16
    • 25744475786 scopus 로고
    • 2+ induced specific DNA binding
    • R.H. Sarma and M.H. Sarma, eds. (Schenectady, NY, USA: Adenine Press)
    • 2+ induced specific DNA binding. In: Structural Biology, Vol. 1, R.H. Sarma and M.H. Sarma, eds. (Schenectady, NY, USA: Adenine Press), pp. 217-224.
    • (1994) Structural Biology , vol.1 , pp. 217-224
    • Köhler, E.1    Wende, W.2    Pingoud, A.3
  • 17
    • 0028988416 scopus 로고
    • 2+ binding to the active site of EcoRV endonuclease: A crystallographic study of com-plexes with substrate and product DNA at 2 Angstrom resolution
    • 2+ binding to the active site of EcoRV endonuclease: A crystallographic study of com-plexes with substrate and product DNA at 2 Angstrom resolution. Biochemistry 34, 683-696.
    • (1995) Biochemistry , vol.34 , pp. 683-696
    • Kostrewa, D.1    Winkler, F.K.2
  • 18
    • 0023656788 scopus 로고
    • Intersubunit location of the active site of ribulosebisphosphate carboxylase/oxygenase as determined by in vivo hybridization of site-directed mutants
    • Larimer, F.W., Lee, E.H., Mural, R.J., Soper, T.S., and Hartmann, F.C. (1987). Intersubunit location of the active site of ribulosebisphosphate carboxylase/oxygenase as determined by in vivo hybridization of site-directed mutants. J. Biol. Chem. 262, 15327-15329.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15327-15329
    • Larimer, F.W.1    Lee, E.H.2    Mural, R.J.3    Soper, T.S.4    Hartmann, F.C.5
  • 19
    • 0028236355 scopus 로고
    • Determination of the catalytic site of creatine kinase by site-directed mutagenesis
    • Lin, L., Perryman, M.B., Friedman, D., Roberts, R., and Ma, T.S. (1994). Determination of the catalytic site of creatine kinase by site-directed mutagenesis. Biochim. Biophys. Acta 1206, 97-104.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 97-104
    • Lin, L.1    Perryman, M.B.2    Friedman, D.3    Roberts, R.4    Ma, T.S.5
  • 20
    • 0029048413 scopus 로고
    • Structure of BamHI endonuclease bound to DNA: Partial folding and unfolding on DNA binding
    • Newman, M., Strzelecka, T., Dorner, L.F., Schildkraut, I., and Aggarwal, A.K. (1995). Structure of BamHI endonuclease bound to DNA: partial folding and unfolding on DNA binding. Science 269, 656-663.
    • (1995) Science , vol.269 , pp. 656-663
    • Newman, M.1    Strzelecka, T.2    Dorner, L.F.3    Schildkraut, I.4    Aggarwal, A.K.5
  • 21
    • 0028073781 scopus 로고
    • Comparison of N-terminal affinity domains: Effect on expression level and product heterogeneity of recombinant restriction endonuclease EcoRV
    • Oswald, T., Wende, W., Pingoud, A., and Rinas, U. (1994). Comparison of N-terminal affinity domains: effect on expression level and product heterogeneity of recombinant restriction endonuclease EcoRV. Appl. Microbiol. Biotechnol. 42, 73-77.
    • (1994) Appl. Microbiol. Biotechnol. , vol.42 , pp. 73-77
    • Oswald, T.1    Wende, W.2    Pingoud, A.3    Rinas, U.4
  • 22
    • 0029132683 scopus 로고
    • Structure and function of Salmonella typhimurium orotate phosphoribosyltransferase: Protein complementation reveals shared active sites
    • Ozturk, D.H., Dorfman, R.H., Scapin, G., Sacchettini, J.C., and Grubmeyer, C. (1995). Structure and function of Salmonella typhimurium orotate phosphoribosyltransferase: protein complementation reveals shared active sites. Biochemistry 34, 10764-10770.
    • (1995) Biochemistry , vol.34 , pp. 10764-10770
    • Ozturk, D.H.1    Dorfman, R.H.2    Scapin, G.3    Sacchettini, J.C.4    Grubmeyer, C.5
  • 24
    • 0002598414 scopus 로고
    • Type II restriction enzymes
    • S.M. Linn, R.S. Lloyd and R.J. Roberts, eds. (Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press)
    • Roberts, R.J., and Halford, S.E. (1993). Type II restriction enzymes. In: Nucleases, S.M. Linn, R.S. Lloyd and R.J. Roberts, eds. (Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press), pp. 35-88.
    • (1993) Nucleases , pp. 35-88
    • Roberts, R.J.1    Halford, S.E.2
  • 25
    • 0342416705 scopus 로고
    • Regeneration of active enzyme by formation of hybrids from inactive derivatives: Implications for active sites shared between polypeptide chains of aspartate transcarbamoylase
    • Robey, E.A., and Schachman, H.K. (1985). Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase. Proc. Natl. Acad. Sci. USA 82, 361-365.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 361-365
    • Robey, E.A.1    Schachman, H.K.2
  • 26
    • 0021152929 scopus 로고
    • The cleavage site for the restriction endonuclease EcoRV is 5′-GAT̂ATC-3′
    • Schildkraut, I., Banner, C.D.B., Rhodes, C.S., and Parekh, S. (1984). The cleavage site for the restriction endonuclease EcoRV is 5′-GAT̂ATC-3′. 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
  • 27
    • 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., Rüter, T., Köhler, E., Liedtke, M.,Thielking, V., Alves, J., Oelgeschläger, T., Wolfes, H., Peters, F., and 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    Rüter, 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
  • 28
    • 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
  • 30
    • 0024322164 scopus 로고
    • Discrimination between DNA sequences by the EcoRV restriction endonuclease
    • Taylor, J.D., and 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
  • 31
    • 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
  • 32
    • 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
  • 34
    • 0027193354 scopus 로고
    • Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants
    • Tobias, K.E., and Kahana, C. (1993). Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants. Biochemistry 32, 5842-5847.
    • (1993) Biochemistry , vol.32 , pp. 5842-5847
    • Tobias, K.E.1    Kahana, C.2
  • 35
    • 0018831237 scopus 로고
    • Transcomplementable copy-number mutants of plasmid ColE1
    • Twigg, A.J., and Sherratt, D. (1980). Transcomplementable copy-number mutants of plasmid ColE1. Nature 283, 216-218.
    • (1980) Nature , vol.283 , pp. 216-218
    • Twigg, A.J.1    Sherratt, D.2
  • 36
    • 0023008210 scopus 로고
    • Protein engineering of homodimeric tyrosyl-tRNA synthetase to produce active heterodimers
    • Ward, W.H., Jones, D.H., and Fersht, A.R. (1986). Protein engineering of homodimeric tyrosyl-tRNA synthetase to produce active heterodimers. J. Biol. Chem. 261, 9576-9578.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9576-9578
    • Ward, W.H.1    Jones, D.H.2    Fersht, A.R.3
  • 37
    • 0008697435 scopus 로고
    • Shared active sites in oligomeric enzymes: Model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis
    • Wente, S.R., and Schachman, H.K. (1987). Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis. Proc. Natl. Acad. Sci. USA 84, 31-35.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 31-35
    • Wente, S.R.1    Schachman, H.K.2
  • 38
    • 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
  • 39
    • 0029975922 scopus 로고    scopus 로고
    • Probing the indirect readout of the restriction enzyme EcoRV - Mutational analysis of contacts to the DNA backbone
    • Wenz, C., Jeltsch, A., and Pingoud, A. (1996). Probing the indirect readout of the restriction enzyme EcoRV - Mutational analysis of contacts to the DNA backbone. J. Biol. Chem. 277, 5565-5573.
    • (1996) J. Biol. Chem. , vol.277 , pp. 5565-5573
    • Wenz, C.1    Jeltsch, A.2    Pingoud, A.3
  • 41
    • 0020338572 scopus 로고
    • R-promotor of bacteriophage λ
    • R-promotor of bacteriophage λ. 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.