메뉴 건너뛰기




Volumn 18, Issue 21, 1999, Pages 6177-6188

Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11

Author keywords

DNA binding protein; Spo11; Topoisomerase

Indexed keywords

BACTERIAL ENZYME; DIMER; DNA BINDING PROTEIN; DNA TOPOISOMERASE; MONOMER;

EID: 0033229826     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.21.6177     Document Type: Article
Times cited : (142)

References (61)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J.P. and Leslie, A.G.W. (1996) Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr., D52, 30-42.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 2
    • 0032530488 scopus 로고    scopus 로고
    • Toprim - A conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins
    • Aravind, L., Leipe, D. and Koonin, E. (1998) Toprim - a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. Nucleic Acids Res., 26, 4205-4213.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4205-4213
    • Aravind, L.1    Leipe, D.2    Koonin, E.3
  • 4
    • 0030045003 scopus 로고    scopus 로고
    • Structure and mechanism of DNA topoisomerase II
    • Berger, J.M., Gamblin, S.J., Harrison, S.C. and Wang, J.C. (1996) Structure and mechanism of DNA topoisomerase II. Nature, 379, 225-232.
    • (1996) Nature , vol.379 , pp. 225-232
    • Berger, J.M.1    Gamblin, S.J.2    Harrison, S.C.3    Wang, J.C.4
  • 5
    • 0032493293 scopus 로고    scopus 로고
    • Structural similarities between topoisomerases that cleave one or both DNA strands
    • Berger, J.M., Fass, D., Wang, J.C. and Harrison, S.C. (1998) Structural similarities between topoisomerases that cleave one or both DNA strands. Proc. Natl Acad. Sci. USA. 95, 7876-7881.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7876-7881
    • Berger, J.M.1    Fass, D.2    Wang, J.C.3    Harrison, S.C.4
  • 6
    • 0027960665 scopus 로고
    • Purification of a DNA topoisomerase II from the hyperthermophilic archaeon Sulfolobus shibatae
    • Bergerat, A., Gadelle, D. and Forterre, P. (1994) Purification of a DNA topoisomerase II from the hyperthermophilic archaeon Sulfolobus shibatae. J. Biol. Chem., 269, 27663-27669.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27663-27669
    • Bergerat, A.1    Gadelle, D.2    Forterre, P.3
  • 7
    • 0030987132 scopus 로고    scopus 로고
    • An atypical topoisomerase II from archaea with implications for meiotic recombination
    • Bergerat, A., de Massy, B., Gadelle, D., Varoutas, P.-C., Nicolas, A. and Forterre, P. (1997) An atypical topoisomerase II from archaea with implications for meiotic recombination. Nature, 386, 414-416.
    • (1997) Nature , vol.386 , pp. 414-416
    • Bergerat, A.1    De Massy, B.2    Gadelle, D.3    Varoutas, P.-C.4    Nicolas, A.5    Forterre, P.6
  • 9
    • 0000800913 scopus 로고
    • Catenation and knotting of duplex DNA by type I topoisomerases: A mechanistic parallel with type II topoisomerases
    • Brown, P.O. and Cozzarelli, N.R. (1981) Catenation and knotting of duplex DNA by type I topoisomerases: a mechanistic parallel with type II topoisomerases. Proc. Natl Acad. Sci. USA, 78, 843-847.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 843-847
    • Brown, P.O.1    Cozzarelli, N.R.2
  • 10
    • 0032533417 scopus 로고    scopus 로고
    • Reconstitution of DNA topoisomerase VI of the thermophilic archaeon Sulfolohus shibatae from subunits separately overexpressed in Escherichia coli
    • Buhler, C., Gadelle, D., Forterre, P., Wang, J. and Bergerat, A. (1998) Reconstitution of DNA topoisomerase VI of the thermophilic archaeon Sulfolohus shibatae from subunits separately overexpressed in Escherichia coli. Nucleic Acids Res., 26, 5157-5162.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5157-5162
    • Buhler, C.1    Gadelle, D.2    Forterre, P.3    Wang, J.4    Bergerat, A.5
  • 12
    • 0002591057 scopus 로고
    • DNA topoisomerases as targets of therapeutics: A structural overview
    • Andoh, T., Ikeda, H. and Oguro, M. (eds). CRC Press
    • Caron, P.C. and Wang, J.C. (1993) DNA topoisomerases as targets of therapeutics: a structural overview. In Andoh, T., Ikeda, H. and Oguro, M. (eds), Molecular Biology of DNA Topoisomerases. CRC Press, pp. 1-18.
    • (1993) Molecular Biology of DNA Topoisomerases , pp. 1-18
    • Caron, P.C.1    Wang, J.C.2
  • 13
    • 0028678214 scopus 로고
    • Alignment of primary sequences of DNA topoisomerases
    • Liu, L.F. (ed.). Academic Press
    • Caron, P. and Wang, J.C. (1994) Alignment of primary sequences of DNA topoisomerases. In Liu, L.F. (ed.), Advances in Pharmacology. Academic Press, pp. 271-291.
    • (1994) Advances in Pharmacology , pp. 271-291
    • Caron, P.1    Wang, J.C.2
  • 15
    • 0032513296 scopus 로고    scopus 로고
    • Identification of active-site residues in the Escherichia coli DNA topoisomerase I
    • Chen, S.-J. and Wang, J.C. (1998) Identification of active-site residues in the Escherichia coli DNA topoisomerase I. J. Biol. Chem., 273, 6050-6056.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6050-6056
    • Chen, S.-J.1    Wang, J.C.2
  • 16
    • 0032549763 scopus 로고    scopus 로고
    • Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases
    • Cheng, C., Kussie, P., Pavletich, N. and Shuman, S. (1998) Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases. Cell, 92, 841-850.
    • (1998) Cell , vol.92 , pp. 841-850
    • Cheng, C.1    Kussie, P.2    Pavletich, N.3    Shuman, S.4
  • 17
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 18
    • 0029111419 scopus 로고
    • The nucleotide mapping of DNA double-strand breaks at the CYS3 initiation site of meiotic recombination in Saccharomyces cerevisiae
    • de Massy, B., Rocco, V. and Nicolas, A. (1995) The nucleotide mapping of DNA double-strand breaks at the CYS3 initiation site of meiotic recombination in Saccharomyces cerevisiae. EMBO J., 14, 4589-4598.
    • (1995) EMBO J. , vol.14 , pp. 4589-4598
    • De Massy, B.1    Rocco, V.2    Nicolas, A.3
  • 19
    • 0032493878 scopus 로고    scopus 로고
    • Meiotic recombination in C.elegans initiates by a conserved mechanism and is dispensable for homologous chromosome synapsis
    • Dernburg, A.F., McDonald, K., Moulder, G., Barstead, R., Dresser, M. and Villeneuve, A.M. (1998) Meiotic recombination in C.elegans initiates by a conserved mechanism and is dispensable for homologous chromosome synapsis. Cell, 94, 387-398.
    • (1998) Cell , vol.94 , pp. 387-398
    • Dernburg, A.F.1    McDonald, K.2    Moulder, G.3    Barstead, R.4    Dresser, M.5    Villeneuve, A.M.6
  • 20
    • 0025770051 scopus 로고
    • Mechanistic studies on E.coli DNA topoisomerase I: Divalent ion effects
    • Domanico, P.L. and Tse-Dinh, Y.-C. (1991) Mechanistic studies on E.coli DNA topoisomerase I: divalent ion effects. J. Inorg. Biochem., 42, 87-96.
    • (1991) J. Inorg. Biochem. , vol.42 , pp. 87-96
    • Domanico, P.L.1    Tse-Dinh, Y.-C.2
  • 21
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry, 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 22
    • 0032947158 scopus 로고    scopus 로고
    • Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands
    • Fass, D., Bogden, C.E. and Berger, J.M. (1999) Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands. Nature Struct. Biol., 6, 322-326.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 322-326
    • Fass, D.1    Bogden, C.E.2    Berger, J.M.3
  • 23
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • Fortelle, E.d.-L. and Bricogne, G. (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol., 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • Fortelle, E.D.-L.1    Bricogne, G.2
  • 24
    • 0021235437 scopus 로고
    • The purification and characterization of DNA topoisomerases 1 and II of the yeast Saccharomyces cerevisiae
    • Goto, T., Laipis, P. and Wang, J.C. (1984) The purification and characterization of DNA topoisomerases 1 and II of the yeast Saccharomyces cerevisiae. J. Biol. Chem., 16, 10422-10429.
    • (1984) J. Biol. Chem. , vol.16 , pp. 10422-10429
    • Goto, T.1    Laipis, P.2    Wang, J.C.3
  • 25
    • 0030970690 scopus 로고    scopus 로고
    • A super new twist on the initiation of meiotic recombination
    • Haber, J.E. (1997) A super new twist on the initiation of meiotic recombination. Cell, 89, 163-166.
    • (1997) Cell , vol.89 , pp. 163-166
    • Haber, J.E.1
  • 26
    • 0025995844 scopus 로고
    • A structural taxonomy of DNA-binding domains
    • Harrison, S.C. (1991) A structural taxonomy of DNA-binding domains. Nature, 353, 715-719.
    • (1991) Nature , vol.353 , pp. 715-719
    • Harrison, S.C.1
  • 27
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 28
    • 0032475933 scopus 로고    scopus 로고
    • Structure of the DNA repair and replication endonuclease and exonuclease FEN-1 : Coupling DNA and PCNA binding to FEN-1 activity
    • Hosfield, D., Mol, C., Shen, B. and Tainer, J. (1998) Structure of the DNA repair and replication endonuclease and exonuclease FEN-1 : coupling DNA and PCNA binding to FEN-1 activity. Cell, 95, 135-146.
    • (1998) Cell , vol.95 , pp. 135-146
    • Hosfield, D.1    Mol, C.2    Shen, B.3    Tainer, J.4
  • 30
    • 0028789631 scopus 로고
    • Covalent protein-DNA complexes at the 5′ strand termini of meiosis-specific double-strand breaks in yeast
    • Keeney, S. and Kleckner, N. (1995) Covalent protein-DNA complexes at the 5′ strand termini of meiosis-specific double-strand breaks in yeast. Proc. Natl Acad. Sci. USA, 92, 11274-11278.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11274-11278
    • Keeney, S.1    Kleckner, N.2
  • 31
    • 0030893115 scopus 로고    scopus 로고
    • Meiosis-specific DNA double-strand breaks are catalyzed by Spo11, a member of a widely conserved protein family
    • Keeney, S., Giroux, G.N. and Kleckner, N. (1997) Meiosis-specific DNA double-strand breaks are catalyzed by Spo11, a member of a widely conserved protein family. Cell, 88, 375-384.
    • (1997) Cell , vol.88 , pp. 375-384
    • Keeney, S.1    Giroux, G.N.2    Kleckner, N.3
  • 33
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 34
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. and Wilson, K.S. (1993) Automated refinement of protein models. Acta Crystallogr., D49, 129-147.
    • (1993) Acta Crystallogr. , vol.D49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R., MacArthur, M., Moss, D. and Thornton, J. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 36
    • 0028115776 scopus 로고
    • Three-dimensional structure of the 67K N-terminal fragment of E.coli DNA topoisomerase I
    • Lima, C.D., Wang, J.C. and Mondragón, A. (1994) Three-dimensional structure of the 67K N-terminal fragment of E.coli DNA topoisomerase I. Nature, 367, 138-146.
    • (1994) Nature , vol.367 , pp. 138-146
    • Lima, C.D.1    Wang, J.C.2    Mondragón, A.3
  • 37
    • 0029145136 scopus 로고
    • The location and structure of double-strand DNA breaks induced during yeast meiosis: Evidence for a covalently linked DNA-protein intermediate
    • Liu, J., Wu, T.-C. and Lichten, M. (1995) The location and structure of double-strand DNA breaks induced during yeast meiosis: evidence for a covalently linked DNA-protein intermediate. EMBO J., 14, 4599-4608.
    • (1995) EMBO J. , vol.14 , pp. 4599-4608
    • Liu, J.1    Wu, T.-C.2    Lichten, M.3
  • 38
    • 0032493748 scopus 로고    scopus 로고
    • Identification of active-site residues in the 'GyrA' half of yeast DNA topoisomerase II
    • Liu, Q. and Wang, J. (1998) Identification of active-site residues in the 'GyrA' half of yeast DNA topoisomerase II. J. Biol. Chem., 273, 20252-20260.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20252-20260
    • Liu, Q.1    Wang, J.2
  • 39
    • 0033514360 scopus 로고    scopus 로고
    • Similarity in the catalysis of DNA breakage and rejoining by type IA and IIA DNA topoisomerases
    • Liu, Q. and Wang, J. (1999) Similarity in the catalysis of DNA breakage and rejoining by type IA and IIA DNA topoisomerases. Proc. Natl Acad. Sci. USA, 96, 881-886.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 881-886
    • Liu, Q.1    Wang, J.2
  • 40
    • 0032530197 scopus 로고    scopus 로고
    • mei-W68 in Drosophila melanogaster encodes a Spo11 homolog: Evidence that the mechanism for initiating meiotic recombination is conserved
    • McKim, K.S. and Hayashi-Hagihara, A. (1998) mei-W68 in Drosophila melanogaster encodes a Spo11 homolog: evidence that the mechanism for initiating meiotic recombination is conserved. Genes Dev., 12, 2932-2942.
    • (1998) Genes Dev. , vol.12 , pp. 2932-2942
    • McKim, K.S.1    Hayashi-Hagihara, A.2
  • 41
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt, E. and Murphy, M. (1994) Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr., D50, 869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.1    Murphy, M.2
  • 42
    • 2142860722 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 RNase H, a 5′ to 3′ RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic proteins
    • Mueser, T., Nossal, N. and Hyde, C. (1996) Structure of bacteriophage T4 RNase H, a 5′ to 3′ RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic proteins. Cell, 85, 1101-1112.
    • (1996) Cell , vol.85 , pp. 1101-1112
    • Mueser, T.1    Nossal, N.2    Hyde, C.3
  • 43
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A. and Dodson, E.J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr., D53, 240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 45
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet., 11, 281-296.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 46
    • 0023646699 scopus 로고
    • Role of the divalent cation in topoisomerase II-mediated reactions
    • Osheroff, N. (1987) Role of the divalent cation in topoisomerase II-mediated reactions. Biochemistry, 26, 6402-6406.
    • (1987) Biochemistry , vol.26 , pp. 6402-6406
    • Osheroff, N.1
  • 47
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • Otwinowski, Z.1    Minor, W.2
  • 48
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo, C. and Sauer, R.T. (1992) Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem., 61, 1053-1095.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.1    Sauer, R.T.2
  • 49
    • 0032489634 scopus 로고    scopus 로고
    • Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA
    • Redinbo, M.R., Stewart, L., Kuhn, P., Champoux, J.J. and Hol, W.G.J. (1998) Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science, 279, 1504-1513.
    • (1998) Science , vol.279 , pp. 1504-1513
    • Redinbo, M.R.1    Stewart, L.2    Kuhn, P.3    Champoux, J.J.4    Hol, W.G.J.5
  • 50
    • 0028334718 scopus 로고
    • DNA transport by a type II DNA topoisomerase: Evidence in favor of a two-gate mechanism
    • Roca, J. and Wang, J.C. (1994) DNA transport by a type II DNA topoisomerase: evidence in favor of a two-gate mechanism. Cell, 77, 609-616.
    • (1994) Cell , vol.77 , pp. 609-616
    • Roca, J.1    Wang, J.C.2
  • 51
    • 0029961651 scopus 로고    scopus 로고
    • DNA transport by a type II DNA topoisomerase: Direct evidence for a two-gate mechanism
    • Roca, J.R., Berger, J.M., Harrison, S.C. and Wang, J.C. (1996) DNA transport by a type II DNA topoisomerase: direct evidence for a two-gate mechanism. Proc. Natl Acad. Sci. USA, 93, 4057-4062.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4057-4062
    • Roca, J.R.1    Berger, J.M.2    Harrison, S.C.3    Wang, J.C.4
  • 52
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90 degrees
    • Schultz, S.C., Shields, G.C. and Steitz, T.A. (1991) Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees. Science, 253, 1001-1007.
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 53
    • 0032540265 scopus 로고    scopus 로고
    • Conserved themes but novel activities in recombinases and topoisomerases
    • Sherrat, D. and Wigley, D. (1998) Conserved themes but novel activities in recombinases and topoisomerases. Cell, 93, 149-152.
    • (1998) Cell , vol.93 , pp. 149-152
    • Sherrat, D.1    Wigley, D.2
  • 54
    • 0027788051 scopus 로고
    • Structure of the Mg (2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis
    • Stock, A.M., Martinez-Hackert, E., Rasmussen, B.F., West, A.H., Stock, J.B., Ringe, D. and Petsko, G.A. (1993) Structure of the Mg (2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry, 32, 13375-13380.
    • (1993) Biochemistry , vol.32 , pp. 13375-13380
    • Stock, A.M.1    Martinez-Hackert, E.2    Rasmussen, B.F.3    West, A.H.4    Stock, J.B.5    Ringe, D.6    Petsko, G.A.7
  • 55
    • 0030991897 scopus 로고    scopus 로고
    • Type II DNA topoisomerase from Saccharomyces cerevisiae is a stable dimer
    • Tennyson, R.B. and Lindsley, J.E. (1997) Type II DNA topoisomerase from Saccharomyces cerevisiae is a stable dimer. Biochemistry, 36, 6107-6114.
    • (1997) Biochemistry , vol.36 , pp. 6107-6114
    • Tennyson, R.B.1    Lindsley, J.E.2
  • 56
    • 0019332581 scopus 로고
    • Covalent bonds between protein and DNA: Formation of phosphotyrosine linkage between certain DNA topoisomerases and DNA
    • Tse, Y.-C. Kirkegaard, K. and Wang, J.C. (1980) Covalent bonds between protein and DNA: formation of phosphotyrosine linkage between certain DNA topoisomerases and DNA. J. Biol. Chem., 255, 5560-5565.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5560-5565
    • Tse, Y.-C.1    Kirkegaard, K.2    Wang, J.C.3
  • 57
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne, G.D., Standaert, R.F., Karplus, A.P., Schreiber, S.L. and Clardy, J. (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol., 229, 105-124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, A.P.3    Schreiber, S.L.4    Clardy, J.5
  • 58
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • Wang, J.C. (1996) DNA topoisomerases. Annu. Rev. Biochem., 65, 635-692.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 635-692
    • Wang, J.C.1
  • 59
    • 0026428621 scopus 로고
    • Crystal structure of an N-terminal fragment of the DNA gyrase B protein
    • Wigley, D.B., Davies, G.J., Dodson, E.J., Maxwell, A. and Dodson, G. (1991) Crystal structure of an N-terminal fragment of the DNA gyrase B protein Nature, 351, 624-629.
    • (1991) Nature , vol.351 , pp. 624-629
    • Wigley, D.B.1    Davies, G.J.2    Dodson, E.J.3    Maxwell, A.4    Dodson, G.5
  • 61
    • 0032502767 scopus 로고    scopus 로고
    • Site-directed mutagenesis of conserved aspartates, glutamates and arginines in the active-site region of Escherichia coli DNA topoisomerase I
    • Zhu, C.-X., Roche, C., Papanicolaou, N., DiPietrantonio, A. and Tse-Dinh, Y.-C. (1998) Site-directed mutagenesis of conserved aspartates, glutamates and arginines in the active-site region of Escherichia coli DNA topoisomerase I. J. Biol. Chem., 273, 8783-8789.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8783-8789
    • Zhu, C.-X.1    Roche, C.2    Papanicolaou, N.3    DiPietrantonio, A.4    Tse-Dinh, Y.-C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.