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Volumn 12, Issue 12, 2011, Pages 827-841

All tangled up: How cells direct, manage and exploit topoisomerase function

Author keywords

[No Author keywords available]

Indexed keywords

DNA TOPOISOMERASE; DNA TOPOISOMERASE (ATP HYDROLYSING) A; DNA TOPOISOMERASE (ATP HYDROLYSING) B; DOUBLE STRANDED DNA; ETOPOSIDE; MOXIFLOXACIN; NOVOBIOCIN; RADICICOL; RECQ HELICASE; REPLICATION FACTOR A; SINGLE STRANDED DNA;

EID: 81855198087     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3228     Document Type: Review
Times cited : (511)

References (211)
  • 2
    • 50649101663 scopus 로고    scopus 로고
    • DNA topoisomerases: Harnessing and constraining energy to govern chromosome topology
    • Schoeffler, A. J. & Berger, J. M. DNA topoisomerases: harnessing and constraining energy to govern chromosome topology. Q. Rev. Biophys. 41, 41-101 (2008).
    • (2008) Q. Rev. Biophys , vol.41 , pp. 41-101
    • Schoeffler, A.J.1    Berger, J.M.2
  • 3
    • 0028115776 scopus 로고
    • Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase i
    • Lima, C. D., Wang, J. C. & Mondragón, A. Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I. Nature 367, 138-146 (1994).
    • (1994) Nature , vol.367 , pp. 138-146
    • Lima, C.D.1    Wang, J.C.2    Mondragón, A.3
  • 4
    • 0019332581 scopus 로고
    • Covalent bonds between protein and DNA. Formation of phosphotyrosine linkage between certain DNA topoisomerases and DNA
    • Tse, Y. C., Kirkegaard, K. & Wang, J. C. Covalent bonds between protein and DNA. Formation of phosphotyrosine linkage between certain DNA topoisomerases and DNA. J. Biol. Chem. 255, 5560-5565 (1980).
    • (1980) J. Biol. Chem , vol.255 , pp. 5560-5565
    • Tse, Y.C.1    Kirkegaard, K.2    Wang, J.C.3
  • 5
    • 0000800913 scopus 로고
    • Catenation and knotting of duplex DNA by type 1 topoisomerases: A mechanistic parallel with type 2 topoisomerases
    • Brown, P. O. & Cozzarelli, N. R. Catenation and knotting of duplex DNA by type 1 topoisomerases: a mechanistic parallel with type 2 topoisomerases. Proc. Natl Acad. Sci. USA 78, 843-847 (1981).
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 843-847
    • Brown, P.O.1    Cozzarelli, N.R.2
  • 6
    • 0015222656 scopus 로고
    • Interaction between DNA and an Escherichia coli protein omega
    • Wang, J. C. Interaction between DNA and an Escherichia coli protein omega. J. Mol. Biol. 55, 523-533 (1971).
    • (1971) J. Mol. Biol , vol.55 , pp. 523-533
    • Wang, J.C.1
  • 7
    • 0027976667 scopus 로고
    • Decatenating activity of Escherichia coli DNA gyrase and topoisomerases i and III during oriC and pBR322 DNA replication in vitro
    • Hiasa, H., DiGate, R. J. & Marians, K. J. Decatenating activity of Escherichia coli DNA gyrase and topoisomerases I and III during oriC and pBR322 DNA replication in vitro. J. Biol. Chem. 269, 2093-2099 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 2093-2099
    • Hiasa, H.1    Digate, R.J.2    Marians, K.J.3
  • 8
    • 0024324482 scopus 로고
    • A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase
    • Wallis, J. W., Chrebet, G., Brodsky, G., Rolfe, M. & Rothstein, R. A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase. Cell 58, 409-419 (1989).
    • (1989) Cell , vol.58 , pp. 409-419
    • Wallis, J.W.1    Chrebet, G.2    Brodsky, G.3    Rolfe, M.4    Rothstein, R.5
  • 9
    • 0033031935 scopus 로고    scopus 로고
    • RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: A conserved mechanism for control of DNA recombination
    • Harmon, F. G., DiGate, R. J. & Kowalczykowski, S. C. RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: a conserved mechanism for control of DNA recombination. Mol. Cell 3, 611-620 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 611-620
    • Harmon, F.G.1    Digate, R.J.2    Kowalczykowski, S.C.3
  • 10
    • 0023712287 scopus 로고
    • Identification of a potent decatenating enzyme from Escherichia coli
    • DiGate, R. J. & Marians, K. J. Identification of a potent decatenating enzyme from Escherichia coli. J. Biol. Chem. 263, 13366-13373 (1988).
    • (1988) J. Biol. Chem , vol.263 , pp. 13366-13373
    • Digate, R.J.1    Marians, K.J.2
  • 11
    • 26244451561 scopus 로고    scopus 로고
    • A role for topoisomerase III in a recombination pathway alternative to RuvABC
    • Lopez, C. R. et al. A role for topoisomerase III in a recombination pathway alternative to RuvABC. Mol. Microbiol. 58, 80-101 (2005).
    • (2005) Mol. Microbiol , vol.58 , pp. 80-101
    • Lopez, C.R.1
  • 12
    • 0021154312 scopus 로고
    • Reverse gyrase-a topoisomerase which introduces positive superhelical turns into DNA
    • Kikuchi, A. & Asai, K. Reverse gyrase-a topoisomerase which introduces positive superhelical turns into DNA. Nature 309, 677-681 (1984).
    • (1984) Nature , vol.309 , pp. 677-681
    • Kikuchi, A.1    Asai, K.2
  • 13
    • 33646832425 scopus 로고    scopus 로고
    • Reverse gyrase functions as a DNA renaturase
    • Hsieh, T. & Plank, J. L. Reverse gyrase functions as a DNA renaturase. J. Biol. Chem. 281, 5640-5647 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 5640-5647
    • Hsieh, T.1    Plank, J.L.2
  • 14
    • 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. & Hol, W. G. Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science 279, 1504-1513 (1998).
    • (1998) Science , vol.279 , pp. 1504-1513
    • Redinbo, M.R.1    Stewart, L.2    Kuhn, P.3    Champoux, J.J.4    Hol, W.G.5
  • 15
    • 15844383117 scopus 로고    scopus 로고
    • Friction and torque govern the relaxation of DNA supercoils by eukaryotic topoisomerase IB
    • Koster, D. A., Croquette, V., Dekker, C., Shuman, S. & Dekker, N. H. Friction and torque govern the relaxation of DNA supercoils by eukaryotic topoisomerase IB. Nature 434, 671-674 (2005).
    • (2005) Nature , vol.434 , pp. 671-674
    • Koster, D.A.1    Croquette, V.2    Dekker, C.3    Shuman, S.4    Dekker, N.H.5
  • 16
    • 0015262632 scopus 로고
    • An activity from mammalian cells that untwists superhelical DNA-a possible swivel for DNA replication (polyoma-ethidium bromide-mouse-embryo cells-dye binding assay)
    • Champoux, J. J. & Dulbecco, R. An activity from mammalian cells that untwists superhelical DNA-a possible swivel for DNA replication (polyoma-ethidium bromide-mouse-embryo cells-dye binding assay). Proc. Natl Acad. Sci. USA 69, 143-146 (1972).
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 143-146
    • Champoux, J.J.1    Dulbecco, R.2
  • 17
    • 0028787255 scopus 로고
    • Preferential binding of human topoisomerase i to superhelical DNA
    • Madden, K. R., Stewart, L. & Champoux, J. J. Preferential binding of human topoisomerase I to superhelical DNA. EMBO J. 14, 5399-5409 (1995).
    • (1995) EMBO J , vol.14 , pp. 5399-5409
    • Madden, K.R.1    Stewart, L.2    Champoux, J.J.3
  • 18
    • 35548983057 scopus 로고    scopus 로고
    • Tryptophan-205 of human topoisomerase i is essential for camptothecin inhibition of negative but not positive supercoil removal
    • Frohlich, R. F. et al. Tryptophan-205 of human topoisomerase I is essential for camptothecin inhibition of negative but not positive supercoil removal. Nucleic Acids Res. 35, 6170-6180 (2007).
    • (2007) Nucleic Acids Res , vol.35 , pp. 6170-6180
    • Frohlich, R.F.1
  • 19
    • 77953583981 scopus 로고    scopus 로고
    • Crystal structure of a bacterial topoisomerase IB in complex with DNA reveals a secondary DNA binding site
    • Patel, A., Yakovleva, L., Shuman, S. & Mondragón, A. Crystal structure of a bacterial topoisomerase IB in complex with DNA reveals a secondary DNA binding site. Structure 18, 725-733 (2010).
    • (2010) Structure , vol.18 , pp. 725-733
    • Patel, A.1    Yakovleva, L.2    Shuman, S.3    Mondragón, A.4
  • 20
    • 0032489675 scopus 로고    scopus 로고
    • A model for the mechanism of human topoisomerase i
    • Stewart, L., Redinbo, M. R., Qiu, X., Hol, W. G. & Champoux, J. J. A model for the mechanism of human topoisomerase I. Science 279, 1534-1541 (1998).
    • (1998) Science , vol.279 , pp. 1534-1541
    • Stewart, L.1    Redinbo, M.R.2    Qiu, X.3    Hol, W.G.4    Champoux, J.J.5
  • 21
    • 0032549763 scopus 로고    scopus 로고
    • Conservation of structure and mechanism between eukaryotic topoisomerase i and site-specific recombinases
    • Cheng, C., Kussie, P., Pavletich, N. & Shuman, S. Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases. Cell 92, 841-850 (1998).
    • (1998) Cell , vol.92 , pp. 841-850
    • Cheng, C.1    Kussie, P.2    Pavletich, N.3    Shuman, S.4
  • 22
    • 0037133321 scopus 로고    scopus 로고
    • A poxvirus-like type IB topoisomerase family in bacteria
    • Krogh, B. O. & Shuman, S. A poxvirus-like type IB topoisomerase family in bacteria. Proc. Natl Acad. Sci. USA 99, 1853-1858 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1853-1858
    • Krogh, B.O.1    Shuman, S.2
  • 23
    • 33744811420 scopus 로고    scopus 로고
    • DNA topoisomerase V: A new fold of mysterious origin
    • Forterre, P. DNA topoisomerase V: a new fold of mysterious origin. Trends Biotechnol. 24, 245-247 (2006).
    • (2006) Trends Biotechnol , vol.24 , pp. 245-247
    • Forterre, P.1
  • 25
    • 0027328116 scopus 로고
    • DNA topoisomerase v is a relative of eukaryotic topoisomerase i from a hyperthermophilic prokaryote
    • Slesarev, A. I. et al. DNA topoisomerase V is a relative of eukaryotic topoisomerase I from a hyperthermophilic prokaryote. Nature 364, 735-737 (1993).
    • (1993) Nature , vol.364 , pp. 735-737
    • Slesarev, A.I.1
  • 26
    • 31444456899 scopus 로고    scopus 로고
    • Structure of the N-terminal fragment of topoisomerase v reveals a new family of topoisomerases
    • Taneja, B., Patel, A., Slesarev, A. & Mondragon, A. Structure of the N-terminal fragment of topoisomerase V reveals a new family of topoisomerases. EMBO J. 25, 398-408 (2006).
    • (2006) EMBO J , vol.25 , pp. 398-408
    • Taneja, B.1    Patel, A.2    Slesarev, A.3    Mondragon, A.4
  • 27
    • 0035933191 scopus 로고    scopus 로고
    • A type IB topoisomerase with DNA repair activities
    • Belova, G. I. et al. A type IB topoisomerase with DNA repair activities. Proc. Natl Acad. Sci. USA 98, 6015-6020 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 6015-6020
    • Belova, G.I.1
  • 28
    • 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. D. & Koonin, E. V. 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).
    • (1998) Nucleic Acids Res , vol.26 , pp. 4205-4213
    • Aravind, L.1    Leipe, D.D.2    Koonin, E.V.3
  • 29
    • 0032493293 scopus 로고    scopus 로고
    • Structural similarities between topoisomerases that cleave one or both DNA strands
    • Berger, J. M., Fass, D., Wang, J. C. & Harrison, S. C. Structural similarities between topoisomerases that cleave one or both DNA strands. Proc. Natl Acad. Sci. USA 95, 7876-7881 (1998).
    • (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
  • 30
    • 0018882091 scopus 로고
    • Type II DNA topoisomerases: Enzymes that can unknot a topologically knotted DNA molecule via a reversible double-strand break
    • Liu, L. F., Liu, C. C. & Alberts, B. M. Type II DNA topoisomerases: enzymes that can unknot a topologically knotted DNA molecule via a reversible double-strand break. Cell 19, 697-707 (1980).
    • (1980) Cell , vol.19 , pp. 697-707
    • Liu, L.F.1    Liu, C.C.2    Alberts, B.M.3
  • 31
    • 0018666498 scopus 로고
    • A sign inversion mechanism for enzymatic supercoiling of DNA
    • Brown, P. O. & Cozzarelli, N. R. A sign inversion mechanism for enzymatic supercoiling of DNA. Science 206, 1081-1083 (1979).
    • (1979) Science , vol.206 , pp. 1081-1083
    • Brown, P.O.1    Cozzarelli, N.R.2
  • 32
    • 0012127194 scopus 로고
    • DNA gyrase action involves the introduction of transient double-strand breaks into DNA
    • Mizuuchi, K., Fisher, L. M., O'Dea, M. H. & Gellert, M. DNA gyrase action involves the introduction of transient double-strand breaks into DNA. Proc. Natl Acad. Sci. USA 77, 1847-1851 (1980).
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 1847-1851
    • Mizuuchi, K.1    Fisher, L.M.2    O'Dea, M.H.3    Gellert, M.4
  • 33
    • 0000576165 scopus 로고
    • DNA gyrase: An enzyme that introduces superhelical turns into DNA
    • Gellert, M., Mizuuchi, K., O'Dea, M. H. & Nash, H. A. DNA gyrase: an enzyme that introduces superhelical turns into DNA. Proc. Natl Acad. Sci. USA 73, 3872-3876 (1976).
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 3872-3876
    • Gellert, M.1    Mizuuchi, K.2    O'Dea, M.H.3    Nash, H.A.4
  • 34
    • 0020490617 scopus 로고
    • Yeast DNA topoisomerase II. An ATP-dependent type II topoisomerase that catalyzes the catenation, decatenation, unknotting, and relaxation of double-stranded DNA rings
    • Goto, T. & Wang, J. C. Yeast DNA topoisomerase II. An ATP-dependent type II topoisomerase that catalyzes the catenation, decatenation, unknotting, and relaxation of double-stranded DNA rings. J. Biol. Chem. 257, 5866-5872 (1982).
    • (1982) J. Biol. Chem , vol.257 , pp. 5866-5872
    • Goto, T.1    Wang, J.C.2
  • 35
    • 0018964943 scopus 로고
    • ATP-dependent DNA topoisonmerase from D. melanogaster reversibly catenates duplex DNA rings
    • Hsieh, T. & Brutlag, D. ATP-dependent DNA topoisonmerase from D. melanogaster reversibly catenates duplex DNA rings. Cell 21, 115-125 (1980).
    • (1980) Cell , vol.21 , pp. 115-125
    • Hsieh, T.1    Brutlag, D.2
  • 36
    • 0027171678 scopus 로고
    • Decatenation activity of topoisomerase IV during oriC and pBR322 DNA replication in vitro
    • Peng, H. & Marians, K. J. Decatenation activity of topoisomerase IV during oriC and pBR322 DNA replication in vitro. Proc. Natl Acad. Sci. USA 90, 8571-8575 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8571-8575
    • Peng, H.1    Marians, K.J.2
  • 37
    • 0028858007 scopus 로고
    • Roles of topoisomerase IV and DNA gyrase in DNA unlinking during replication in Escherichia coli
    • Zechiedrich, E. & Cozzarelli, N. Roles of topoisomerase IV and DNA gyrase in DNA unlinking during replication in Escherichia coli. Genes Dev. 9, 2859-2869 (1995).
    • (1995) Genes Dev , vol.9 , pp. 2859-2869
    • Zechiedrich, E.1    Cozzarelli, N.2
  • 38
    • 0034669232 scopus 로고    scopus 로고
    • Preferential relaxation of positively supercoiled DNA by E. coli topoisomerase IV in single-molecule and ensemble measurements
    • Crisona, N. J., Strick, T. R., Bensimon, D., Croquette, V. & Cozzarelli, N. R. Preferential relaxation of positively supercoiled DNA by E. coli topoisomerase IV in single-molecule and ensemble measurements. Genes Dev. 14, 2881-2892 (2000).
    • (2000) Genes Dev , vol.14 , pp. 2881-2892
    • Crisona, N.J.1    Strick, T.R.2    Bensimon, D.3    Croquette, V.4    Cozzarelli, N.R.5
  • 39
    • 28244433817 scopus 로고    scopus 로고
    • Human topoisomerase II α rapidly relaxes positively supercoiled DNA: Implications for enzyme action ahead of replication forks
    • McClendon, A. K., Rodriguez, A. C. & Osheroff, N. Human topoisomerase II α rapidly relaxes positively supercoiled DNA: implications for enzyme action ahead of replication forks. J. Biol. Chem. 280, 39337-39345 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 39337-39345
    • McClendon, A.K.1    Rodriguez, A.C.2    Osheroff, N.3
  • 40
    • 79952514729 scopus 로고    scopus 로고
    • Positive supercoiling of mitotic DNA drives decatenation by topoisomerase II in eukaryotes
    • Baxter, J. et al. Positive supercoiling of mitotic DNA drives decatenation by topoisomerase II in eukaryotes. Science 331, 1328-1332 (2011).
    • (2011) Science , vol.331 , pp. 1328-1332
    • Baxter, J.1
  • 41
    • 37549023863 scopus 로고    scopus 로고
    • Structural basis for gate-DNA recognition and bending by type IIA topoisomerases
    • Dong, K. C. & Berger, J. M. Structural basis for gate-DNA recognition and bending by type IIA topoisomerases. Nature 450, 1201-1205 (2007).
    • (2007) Nature , vol.450 , pp. 1201-1205
    • Dong, K.C.1    Berger, J.M.2
  • 42
    • 77955334540 scopus 로고    scopus 로고
    • Structural basis of gate-DNA breakage and resealing by type II topoisomerases
    • Laponogov, I. et al. Structural basis of gate-DNA breakage and resealing by type II topoisomerases. PLoS ONE 5, e11338 (2010).
    • (2010) PLoS ONE , vol.5
    • Laponogov, I.1
  • 43
    • 0035853134 scopus 로고    scopus 로고
    • Mechanism of topology simplification by type II DNA topoisomerases
    • Vologodskii, A. V. et al. Mechanism of topology simplification by type II DNA topoisomerases. Proc. Natl Acad. Sci. USA 98, 3045-3049 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3045-3049
    • Vologodskii, A.V.1
  • 44
    • 0043194014 scopus 로고    scopus 로고
    • Single-molecule study of DNA unlinking by eukaryotic and prokaryotic type-II topoisomerases
    • Charvin, G., Bensimon, D. & Croquette, V. Single-molecule study of DNA unlinking by eukaryotic and prokaryotic type-II topoisomerases. Proc. Natl Acad. Sci. USA 100, 9820-9825 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9820-9825
    • Charvin, G.1    Bensimon, D.2    Croquette, V.3
  • 45
    • 0029678247 scopus 로고    scopus 로고
    • The probabilities of supercoil removal and decatenation by yeast DNA topoisomerase II
    • Roca, J. & Wang, J. C. The probabilities of supercoil removal and decatenation by yeast DNA topoisomerase II. Genes Cells 1, 17-27 (1996).
    • (1996) Genes Cells , vol.1 , pp. 17-27
    • Roca, J.1    Wang, J.C.2
  • 46
    • 0030987132 scopus 로고    scopus 로고
    • An atypical topoisomerase II from archaea with implications for meiotic recombination
    • Bergerat, A. et al. An atypical topoisomerase II from archaea with implications for meiotic recombination. Nature 386, 414-417 (1997).
    • (1997) Nature , vol.386 , pp. 414-417
    • Bergerat, A.1
  • 47
    • 37549056250 scopus 로고    scopus 로고
    • Protist homologs of the meiotic Spo11 gene and topoisomerase VI reveal an evolutionary history of gene duplication and lineage-specific loss
    • Malik, S. B., Ramesh, M. A., Hulstrand, A. M. & Logsdon, J. M. Jr. Protist homologs of the meiotic Spo11 gene and topoisomerase VI reveal an evolutionary history of gene duplication and lineage-specific loss. Mol. Biol. Evol. 24, 2827-2841 (2007).
    • (2007) Mol. Biol. Evol , vol.24 , pp. 2827-2841
    • Malik, S.B.1    Ramesh, M.A.2    Hulstrand, A.M.3    Logsdon Jr., J.M.4
  • 48
    • 0027960665 scopus 로고
    • Purification of a DNA topoisomerase II from the hyperthermophilic archaeon Sulfolobus shibatae. A thermostable enzyme with both bacterial and eucaryal features
    • Bergerat, A., Gadelle, D. & Forterre, P. Purification of a DNA topoisomerase II from the hyperthermophilic archaeon Sulfolobus shibatae. A thermostable enzyme with both bacterial and eucaryal features. J. Biol. Chem. 269, 27663-27669 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 27663-27669
    • Bergerat, A.1    Gadelle, D.2    Forterre, P.3
  • 49
    • 0037413727 scopus 로고    scopus 로고
    • Structure of the topoisomerase VI-B subunit: Implications for type II topoisomerase mechanism and evolution
    • Corbett, K. D. & Berger, J. M. Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution. EMBO J. 22, 151-163 (2003).
    • (2003) EMBO J , vol.22 , pp. 151-163
    • Corbett, K.D.1    Berger, J.M.2
  • 50
    • 0033229826 scopus 로고    scopus 로고
    • Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11
    • Nichols, M. D., DeAngelis, K., Keck, J. L. & Berger, J. M. Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11. EMBO J. 18, 6177-6188 (1999).
    • (1999) EMBO J , vol.18 , pp. 6177-6188
    • Nichols, M.D.1    Deangelis, K.2    Keck, J.L.3    Berger, J.M.4
  • 51
    • 34447136857 scopus 로고    scopus 로고
    • Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI
    • Corbett, K. D., Benedetti, P. & Berger, J. M. Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI. Nature Struct. Mol. Biol. 14, 611-619 (2007).
    • (2007) Nature Struct. Mol. Biol , vol.14 , pp. 611-619
    • Corbett, K.D.1    Benedetti, P.2    Berger, J.M.3
  • 52
    • 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, C. N. & Kleckner, N. Meiosis-specific DNA double-strand breaks are catalyzed by Spo11, a member of a widely conserved protein family. Cell 88, 375-384 (1997).
    • (1997) Cell , vol.88 , pp. 375-384
    • Keeney, S.1    Giroux, C.N.2    Kleckner, N.3
  • 53
    • 57749209893 scopus 로고    scopus 로고
    • The major architects of chromatin: Architectural proteins in bacteria, archaea and eukaryotes
    • Luijsterburg, M. S., White, M. F., Van Driel, R. & Dame, R. T. The major architects of chromatin: architectural proteins in bacteria, archaea and eukaryotes. Crit. Rev. Biochem. Mol. Biol. 43, 393-418 (2008).
    • (2008) Crit. Rev. Biochem. Mol. Biol , vol.43 , pp. 393-418
    • Luijsterburg, M.S.1    White, M.F.2    Van Driel, R.3    Dame, R.T.4
  • 54
    • 0025363121 scopus 로고
    • Structure of plectonemically supercoiled DNA
    • Boles, T. C., White, J. H. & Cozzarelli, N. R. Structure of plectonemically supercoiled DNA. J. Mol. Biol. 213, 931-951 (1990).
    • (1990) J. Mol. Biol , vol.213 , pp. 931-951
    • Boles, T.C.1    White, J.H.2    Cozzarelli, N.R.3
  • 55
    • 0034677898 scopus 로고    scopus 로고
    • Roles of topoisomerases in maintaining steady-state DNA supercoiling in Escherichia coli
    • Zechiedrich, E. L. et al. Roles of topoisomerases in maintaining steady-state DNA supercoiling in Escherichia coli. J. Biol. Chem. 275, 8103-8113 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 8103-8113
    • Zechiedrich, E.L.1
  • 56
    • 0035950182 scopus 로고    scopus 로고
    • Complete genome sequence of Salmonella enterica serovar Typhimurium LT2
    • McClelland, M. et al. Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature 413, 852-856 (2001).
    • (2001) Nature , vol.413 , pp. 852-856
    • McClelland, M.1
  • 57
    • 34547817672 scopus 로고    scopus 로고
    • Growth rate toxicity phenotypes and homeostatic supercoil control differentiate Escherichia coli from Salmonella enterica serovar Typhimurium
    • Champion, K. & Higgins, N. P. Growth rate toxicity phenotypes and homeostatic supercoil control differentiate Escherichia coli from Salmonella enterica serovar Typhimurium. J. Bacteriol. 189, 5839-5849 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 5839-5849
    • Champion, K.1    Higgins, N.P.2
  • 58
    • 78650653937 scopus 로고    scopus 로고
    • A naturally chimeric type IIA topoisomerase in Aquifex aeolicus highlights an evolutionary path for the emergence of functional paralogs
    • Tretter, E. M., Lerman, J. C. & Berger, J. M. A naturally chimeric type IIA topoisomerase in Aquifex aeolicus highlights an evolutionary path for the emergence of functional paralogs. Proc. Natl Acad. Sci. USA 107, 22055-22059 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 22055-22059
    • Tretter, E.M.1    Lerman, J.C.2    Berger, J.M.3
  • 59
    • 34250896106 scopus 로고    scopus 로고
    • Widespread distribution of archaeal reverse gyrase in thermophilic bacteria suggests a complex history of vertical inheritance and lateral gene transfers
    • Brochier-Armanet, C. & Forterre, P. Widespread distribution of archaeal reverse gyrase in thermophilic bacteria suggests a complex history of vertical inheritance and lateral gene transfers. Archaea 2, 83-93 (2007).
    • (2007) Archaea , vol.2 , pp. 83-93
    • Brochier-Armanet, C.1    Forterre, P.2
  • 60
    • 0000239569 scopus 로고
    • High positive supercoiling in vitro catalyzed by an ATP and polyethylene glycol-stimulated topoisomerase from Sulfolobus acidocaldarius
    • Forterre, P., Mirambeau, G., Jaxel, C., Nadal, M. & Duguet, M. High positive supercoiling in vitro catalyzed by an ATP and polyethylene glycol-stimulated topoisomerase from Sulfolobus acidocaldarius. EMBO J. 4, 2123-2128 (1985).
    • (1985) EMBO J , vol.4 , pp. 2123-2128
    • Forterre, P.1    Mirambeau, G.2    Jaxel, C.3    Nadal, M.4    Duguet, M.5
  • 62
    • 0028345358 scopus 로고
    • Comparison of plasmid DNA topology among mesophilic and thermophilic eubacteria and archaebacteria
    • Charbonnier, F. & Forterre, P. Comparison of plasmid DNA topology among mesophilic and thermophilic eubacteria and archaebacteria. J. Bacteriol. 176, 1251-1259 (1994).
    • (1994) J. Bacteriol , vol.176 , pp. 1251-1259
    • Charbonnier, F.1    Forterre, P.2
  • 63
    • 27744490770 scopus 로고    scopus 로고
    • Genetic interaction of the SMC complex with topoisomerase IV in Bacillus subtilis
    • Tadesse, S., Mascarenhas, J., Koesters, B., Hasilik, A. & Graumann, P. L. Genetic interaction of the SMC complex with topoisomerase IV in Bacillus subtilis. Microbiology 151, 1-9 (2005).
    • (2005) Microbiology , vol.151 , pp. 1-9
    • Tadesse, S.1    Mascarenhas, J.2    Koesters, B.3    Hasilik, A.4    Graumann, P.L.5
  • 64
    • 78650495032 scopus 로고    scopus 로고
    • Physical and functional interaction between the condensin MukB and the decatenase topoisomerase IV in Escherichia coli
    • Hayama, R. & Marians, K. J. Physical and functional interaction between the condensin MukB and the decatenase topoisomerase IV in Escherichia coli. Proc. Natl Acad. Sci. USA 107, 18826-18831 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 18826-18831
    • Hayama, R.1    Marians, K.J.2
  • 65
    • 78650438598 scopus 로고    scopus 로고
    • Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction
    • Li, Y. et al. Escherichia coli condensin MukB stimulates topoisomerase IV activity by a direct physical interaction. Proc. Natl Acad. Sci. USA 107, 18832-18837 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 18832-18837
    • Li, Y.1
  • 66
    • 0030582717 scopus 로고    scopus 로고
    • Chromatid segregation at anaphase requires the barren product, a novel chromosome-associated protein that interacts with Topoisomerase II
    • Bhat, M. A., Philp, A. V., Glover, D. M. & Bellen, H. J. Chromatid segregation at anaphase requires the barren product, a novel chromosome-associated protein that interacts with Topoisomerase II. Cell 87, 1103-1114 (1996).
    • (1996) Cell , vol.87 , pp. 1103-1114
    • Bhat, M.A.1    Philp, A.V.2    Glover, D.M.3    Bellen, H.J.4
  • 67
    • 0037387829 scopus 로고    scopus 로고
    • A two-step scaffolding model for mitotic chromosome assembly
    • Maeshima, K. & Laemmli, U. K. A two-step scaffolding model for mitotic chromosome assembly. Dev. Cell 4, 467-480 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 467-480
    • Maeshima, K.1    Laemmli, U.K.2
  • 68
    • 33646177549 scopus 로고    scopus 로고
    • At the heart of the chromosome: SMC proteins in action
    • Hirano, T. At the heart of the chromosome: SMC proteins in action. Nature Rev. Mol. Cell Biol. 7, 311-322 (2006).
    • (2006) Nature Rev. Mol. Cell Biol , vol.7 , pp. 311-322
    • Hirano, T.1
  • 69
    • 0036182726 scopus 로고    scopus 로고
    • Mutation of YCS4, a budding yeast condensin subunit, affects mitotic and nonmitotic chromosome behavior
    • Bhalla, N., Biggins, S. & Murray, A. W. Mutation of YCS4, a budding yeast condensin subunit, affects mitotic and nonmitotic chromosome behavior. Mol. Biol. Cell 13, 632-645 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 632-645
    • Bhalla, N.1    Biggins, S.2    Murray, A.W.3
  • 70
    • 0037108321 scopus 로고    scopus 로고
    • An archaebacterial topoisomerase homolog not present in other eukaryotes is indispensable for cell proliferation of plants
    • Hartung, F. et al. An archaebacterial topoisomerase homolog not present in other eukaryotes is indispensable for cell proliferation of plants. Curr. Biol. 12, 1787-1791 (2002).
    • (2002) Curr. Biol , vol.12 , pp. 1787-1791
    • Hartung, F.1
  • 71
    • 0037108467 scopus 로고    scopus 로고
    • DNA topoisomerase VI is essential for endoreduplication in Arabidopsis
    • Sugimoto-Shirasu, K., Stacey, N. J., Corsar, J., Roberts, K. & McCann, M. C. DNA topoisomerase VI is essential for endoreduplication in Arabidopsis. Curr. Biol. 12, 1782-1786 (2002).
    • (2002) Curr. Biol , vol.12 , pp. 1782-1786
    • Sugimoto-Shirasu, K.1    Stacey, N.J.2    Corsar, J.3    Roberts, K.4    McCann, M.C.5
  • 72
    • 0037162483 scopus 로고    scopus 로고
    • A crucial role for the putative Arabidopsis topoisomerase VI in plant growth and development
    • Yin, Y. et al. A crucial role for the putative Arabidopsis topoisomerase VI in plant growth and development. Proc. Natl Acad. Sci. USA 99, 10191-10196 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 10191-10196
    • Yin, Y.1
  • 73
    • 37849040260 scopus 로고    scopus 로고
    • BIN4, a novel component of the plant DNA topoisomerase VI complex, is required for endoreduplication in Arabidopsis
    • Breuer, C. et al. BIN4, a novel component of the plant DNA topoisomerase VI complex, is required for endoreduplication in Arabidopsis. Plant Cell 19, 3655-3668 (2007).
    • (2007) Plant Cell , vol.19 , pp. 3655-3668
    • Breuer, C.1
  • 74
    • 70350629054 scopus 로고    scopus 로고
    • Endoreplication: Polyploidy with purpose
    • Lee, H. O., Davidson, J. M. & Duronio, R. J. Endoreplication: polyploidy with purpose. Genes Dev. 23, 2461-2477 (2009).
    • (2009) Genes Dev , vol.23 , pp. 2461-2477
    • Lee, H.O.1    Davidson, J.M.2    Duronio, R.J.3
  • 75
    • 29444450736 scopus 로고    scopus 로고
    • RHL1 is an essential component of the plant DNA topoisomerase VI complex and is required for ploidy-dependent cell growth
    • Sugimoto-Shirasu, K. et al. RHL1 is an essential component of the plant DNA topoisomerase VI complex and is required for ploidy-dependent cell growth. Proc. Natl Acad. Sci. USA 102, 18736-18741 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18736-18741
    • Sugimoto-Shirasu, K.1
  • 76
    • 71049171605 scopus 로고    scopus 로고
    • Adaptation of topoisomerase i paralogs to nuclear and mitochondrial DNA
    • Rosa, I. D. et al. Adaptation of topoisomerase I paralogs to nuclear and mitochondrial DNA. Nucleic Acids Res. 37, 6414-6428 (2009).
    • (2009) Nucleic Acids Res , vol.37 , pp. 6414-6428
    • Rosa, I.D.1
  • 77
    • 54849425967 scopus 로고    scopus 로고
    • Mitochondrial topoisomerase i sites in the regulatory D-Loop region of mitochondrial DNA
    • Zhang, H. & Pommier, Y. Mitochondrial topoisomerase I sites in the regulatory D-Loop region of mitochondrial DNA. Biochemistry 47, 11196-11203 (2008).
    • (2008) Biochemistry , vol.47 , pp. 11196-11203
    • Zhang, H.1    Pommier, Y.2
  • 78
    • 0021268392 scopus 로고
    • Topoisomerase i confers specificity in enzymatic replication of the Escherichia coli chromosomal origin
    • Kaguni, J. M. & Kornberg, A. Topoisomerase I confers specificity in enzymatic replication of the Escherichia coli chromosomal origin. J. Biol. Chem. 259, 8578-8583 (1984).
    • (1984) J. Biol. Chem , vol.259 , pp. 8578-8583
    • Kaguni, J.M.1    Kornberg, A.2
  • 79
    • 0028364870 scopus 로고
    • Topoisomerase IV can support oriC DNA replication in vitro
    • Hiasa, H. & Marians, K. J. Topoisomerase IV can support oriC DNA replication in vitro. J. Biol. Chem. 269, 16371-16375 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 16371-16375
    • Hiasa, H.1    Marians, K.J.2
  • 80
    • 33847221417 scopus 로고    scopus 로고
    • Functional interactions of DNA topoisomerases with a human replication origin
    • Abdurashidova, G. et al. Functional interactions of DNA topoisomerases with a human replication origin. EMBO J. 26, 998-1009 (2007).
    • (2007) EMBO J , vol.26 , pp. 998-1009
    • Abdurashidova, G.1
  • 81
    • 33750301347 scopus 로고    scopus 로고
    • Role of topoisomerase IIβ in the expression of developmentally regulated genes
    • Lyu, Y. L. et al. Role of topoisomerase IIβ in the expression of developmentally regulated genes. Mol. Cell. Biol. 26, 7929-7941 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 7929-7941
    • Lyu, Y.L.1
  • 82
    • 0034614266 scopus 로고    scopus 로고
    • DNA topoisomerase IIβ and neural development
    • Yang, X., Li, W., Prescott, E. D., Burden, S. J. & Wang, J. C. DNA topoisomerase IIβ and neural development. Science 287, 131-134 (2000).
    • (2000) Science , vol.287 , pp. 131-134
    • Yang, X.1    Li, W.2    Prescott, E.D.3    Burden, S.J.4    Wang, J.C.5
  • 83
    • 33745255099 scopus 로고    scopus 로고
    • A topoisomerase IIβ-mediated dsDNA break required for regulated transcription
    • Ju, B. G. et al. A topoisomerase IIβ-mediated dsDNA break required for regulated transcription. Science 312, 1798-1802 (2006).
    • (2006) Science , vol.312 , pp. 1798-1802
    • Ju, B.G.1
  • 84
    • 73049110256 scopus 로고    scopus 로고
    • Transient dsDNA breaks during pre-replication complex assembly
    • Rampakakis, E. & Zannis-Hadjopoulos, M. Transient dsDNA breaks during pre-replication complex assembly. Nucleic Acids Res. 37, 5714-5724 (2009).
    • (2009) Nucleic Acids Res , vol.37 , pp. 5714-5724
    • Rampakakis, E.1    Zannis-Hadjopoulos, M.2
  • 86
    • 0034662998 scopus 로고    scopus 로고
    • Analysis of topoisomerase function in bacterial replication fork movement: Use of DNA microarrays
    • Khodursky, A. B. et al. Analysis of topoisomerase function in bacterial replication fork movement: use of DNA microarrays. Proc. Natl Acad. Sci. USA 97, 9419-9424 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9419-9424
    • Khodursky, A.B.1
  • 87
    • 0029831664 scopus 로고    scopus 로고
    • Two distinct modes of strand unlinking during θ-type DNA replication
    • Hiasa, H. & Marians, K. J. Two distinct modes of strand unlinking during θ-type DNA replication. J. Biol. Chem. 271, 21529-21535 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 21529-21535
    • Hiasa, H.1    Marians, K.J.2
  • 88
    • 0023127037 scopus 로고
    • Need for DNA topoisomerase activity as a swivel for DNA replication for transcription of ribosomal RNA
    • Brill, S. J., DiNardo, S., Voelkel-Meiman, K. & Sternglanz, R. Need for DNA topoisomerase activity as a swivel for DNA replication for transcription of ribosomal RNA. Nature 326, 414-416 (1987).
    • (1987) Nature , vol.326 , pp. 414-416
    • Brill, S.J.1    Dinardo, S.2    Voelkel-Meiman, K.3    Sternglanz, R.4
  • 89
    • 0024338961 scopus 로고
    • Function of DNA topoisomerases as replication swivels in Saccharomyces cerevisiae
    • Kim, R. A. & Wang, J. C. Function of DNA topoisomerases as replication swivels in Saccharomyces cerevisiae. J. Mol. Biol. 208, 257-267 (1989).
    • (1989) J. Mol. Biol , vol.208 , pp. 257-267
    • Kim, R.A.1    Wang, J.C.2
  • 90
    • 2642625363 scopus 로고
    • Roles of DNA topoisomerases in simian virus 40 DNA replication in vitro
    • Yang, L., Wold, M. S., Li, J. J., Kelly, T. J. & Liu, L. F. Roles of DNA topoisomerases in simian virus 40 DNA replication in vitro. Proc. Natl Acad. Sci. USA 84, 950-954 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 950-954
    • Yang, L.1    Wold, M.S.2    Li, J.J.3    Kelly, T.J.4    Liu, L.F.5
  • 91
    • 79952813905 scopus 로고    scopus 로고
    • Chromosome length influences replication-induced topological stress
    • Kegel, A. et al. Chromosome length influences replication-induced topological stress. Nature 471, 392-396 (2011).
    • (2011) Nature , vol.471 , pp. 392-396
    • Kegel, A.1
  • 93
    • 0032544699 scopus 로고    scopus 로고
    • The structure of supercoiled intermediates in DNA replication
    • Peter, B. J., Ullsperger, C., Hiasa, H., Marians, K. J. & Cozzarelli, N. R. The structure of supercoiled intermediates in DNA replication. Cell 94, 819-827 (1998).
    • (1998) Cell , vol.94 , pp. 819-827
    • Peter, B.J.1    Ullsperger, C.2    Hiasa, H.3    Marians, K.J.4    Cozzarelli, N.R.5
  • 94
    • 0022400533 scopus 로고
    • DNA topoisomerase II is required at the time of mitosis in yeast
    • Holm, C., Goto, T., Wang, J. C. & Botstein, D. DNA topoisomerase II is required at the time of mitosis in yeast. Cell 41, 553-563 (1985).
    • (1985) Cell , vol.41 , pp. 553-563
    • Holm, C.1    Goto, T.2    Wang, J.C.3    Botstein, D.4
  • 95
    • 0009543358 scopus 로고
    • Isolation of type i and II DNA topoisomerase mutants from fission yeast: Single and double mutants show different phenotypes in cell growth and chromatin organization
    • Uemura, T. & Yanagida, M. Isolation of type I and II DNA topoisomerase mutants from fission yeast: single and double mutants show different phenotypes in cell growth and chromatin organization. EMBO J. 3, 1737-1744 (1984).
    • (1984) EMBO J , vol.3 , pp. 1737-1744
    • Uemura, T.1    Yanagida, M.2
  • 96
    • 44949208460 scopus 로고    scopus 로고
    • Topoisomerase II inactivation prevents the completion of DNA replication in budding yeast
    • Baxter, J. & Diffley, J. F. Topoisomerase II inactivation prevents the completion of DNA replication in budding yeast. Mol. Cell 30, 790-802 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 790-802
    • Baxter, J.1    Diffley, J.F.2
  • 97
    • 0023651332 scopus 로고
    • DNA topoisomerase II is required for condensation and separation of mitotic chromosomes in S. pombe
    • Uemura, T. et al. DNA topoisomerase II is required for condensation and separation of mitotic chromosomes in S. pombe. Cell 50, 917-925 (1987).
    • (1987) Cell , vol.50 , pp. 917-925
    • Uemura, T.1
  • 98
    • 0026712869 scopus 로고
    • The role of topoisomerase IV in partitioning bacterial replicons and the structure of catenated intermediates in DNA replication
    • Adams, D. E., Shekhtman, E. M., Zechiedrich, E. L., Schmid, M. B. & Cozzarelli, N. R. The role of topoisomerase IV in partitioning bacterial replicons and the structure of catenated intermediates in DNA replication. Cell 71, 277-288 (1992).
    • (1992) Cell , vol.71 , pp. 277-288
    • Adams, D.E.1    Shekhtman, E.M.2    Zechiedrich, E.L.3    Schmid, M.B.4    Cozzarelli, N.R.5
  • 99
    • 0024499711 scopus 로고
    • DNA topoisomerase II must act at mitosis to prevent nondisjunction and chromosome breakage
    • Holm, C., Stearns, T. & Botstein, D. DNA topoisomerase II must act at mitosis to prevent nondisjunction and chromosome breakage. Mol. Cell. Biol. 9, 159-168 (1989).
    • (1989) Mol. Cell. Biol , vol.9 , pp. 159-168
    • Holm, C.1    Stearns, T.2    Botstein, D.3
  • 100
    • 0011173714 scopus 로고
    • DNA topoisomerase II mutant of Saccharomyces cerevisiae: Topoisomerase II is required for segregation of daughter molecules at the termination of DNA replication
    • DiNardo, S., Voelkel, K. & Sternglanz, R. DNA topoisomerase II mutant of Saccharomyces cerevisiae: topoisomerase II is required for segregation of daughter molecules at the termination of DNA replication. Proc. Natl Acad. Sci. USA 81, 2616-2620 (1984).
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 2616-2620
    • Dinardo, S.1    Voelkel, K.2    Sternglanz, R.3
  • 101
    • 0001262820 scopus 로고
    • Mitotic spindle pulls but fails to separate chromosomes in type II DNA topoisomerase mutants: Uncoordinated mitosis
    • Uemura, T. & Yanagida, M. Mitotic spindle pulls but fails to separate chromosomes in type II DNA topoisomerase mutants: uncoordinated mitosis. EMBO J. 5, 1003-1010 (1986).
    • (1986) EMBO J , vol.5 , pp. 1003-1010
    • Uemura, T.1    Yanagida, M.2
  • 102
    • 0037424533 scopus 로고    scopus 로고
    • Topoisomerase III can serve as the cellular decatenase in Escherichia coli
    • Nurse, P., Levine, C., Hassing, H. & Marians, K. J. Topoisomerase III can serve as the cellular decatenase in Escherichia coli. J. Biol. Chem. 278, 8653-8660 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 8653-8660
    • Nurse, P.1    Levine, C.2    Hassing, H.3    Marians, K.J.4
  • 103
    • 44949225070 scopus 로고    scopus 로고
    • Resolution of converging replication forks by RecQ and topoisomerase III
    • Suski, C. & Marians, K. J. Resolution of converging replication forks by RecQ and topoisomerase III. Mol. Cell 30, 779-789 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 779-789
    • Suski, C.1    Marians, K.J.2
  • 104
    • 21244434850 scopus 로고    scopus 로고
    • RMI1/NCE4, a suppressor of genome instability, encodes a member of the RecQ helicase/Topo III complex
    • Chang, M. et al. RMI1/NCE4, a suppressor of genome instability, encodes a member of the RecQ helicase/Topo III complex. EMBO J. 24, 2024-2033 (2005).
    • (2005) EMBO J , vol.24 , pp. 2024-2033
    • Chang, M.1
  • 105
    • 54349099705 scopus 로고    scopus 로고
    • RMI, a new OB-fold complex essential for Bloom syndrome protein to maintain genome stability
    • Xu, D. et al. RMI, a new OB-fold complex essential for Bloom syndrome protein to maintain genome stability. Genes Dev. 22, 2843-2855 (2008).
    • (2008) Genes Dev , vol.22 , pp. 2843-2855
    • Xu, D.1
  • 106
    • 34547192058 scopus 로고    scopus 로고
    • BLM is required for faithful chromosome segregation and its localization defines a class of ultrafine anaphase bridges
    • Chan, K. L., North, P. S. & Hickson, I. D. BLM is required for faithful chromosome segregation and its localization defines a class of ultrafine anaphase bridges. EMBO J. 26, 3397-3409 (2007).
    • (2007) EMBO J , vol.26 , pp. 3397-3409
    • Chan, K.L.1    North, P.S.2    Hickson, I.D.3
  • 107
    • 0027159512 scopus 로고
    • Reverse gyrase: A helicase-like domain and a type i topoisomerase in the same polypeptide
    • Confalonieri, F. et al. Reverse gyrase: a helicase-like domain and a type I topoisomerase in the same polypeptide. Proc. Natl Acad. Sci. USA 90, 4753-4757 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4753-4757
    • Confalonieri, F.1
  • 108
    • 0039172550 scopus 로고    scopus 로고
    • Reverse gyrase, the two domains intimately cooperate to promote positive supercoiling
    • Dclais, A. C., Marsault, J., Confalonieri, F., de La Tour, C. B. & Duguet, M. Reverse gyrase, the two domains intimately cooperate to promote positive supercoiling. J. Biol. Chem. 275, 19498-19504 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 19498-19504
    • Dclais, A.C.1    Marsault, J.2    Confalonieri, F.3    De La Tour, C.B.4    Duguet, M.5
  • 109
    • 27444442749 scopus 로고    scopus 로고
    • Tus-mediated arrest of DNA replication in Escherichia coli is modulated by DNA supercoiling
    • Valjavec-Gratian, M., Henderson, T. A. & Hill, T. M. Tus-mediated arrest of DNA replication in Escherichia coli is modulated by DNA supercoiling. Mol. Microbiol. 58, 758-773 (2005).
    • (2005) Mol. Microbiol , vol.58 , pp. 758-773
    • Valjavec-Gratian, M.1    Henderson, T.A.2    Hill, T.M.3
  • 110
    • 77955997707 scopus 로고    scopus 로고
    • Replication termination at eukaryotic chromosomes is mediated by Top2 and occurs at genomic loci containing pausing elements
    • Fachinetti, D. et al. Replication termination at eukaryotic chromosomes is mediated by Top2 and occurs at genomic loci containing pausing elements. Mol. Cell 39, 595-605 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 595-605
    • Fachinetti, D.1
  • 111
    • 78049300491 scopus 로고    scopus 로고
    • FtsK DNA translocase: The fast motor that knows where it's going
    • Crozat, E. & Grainge, I. FtsK DNA translocase: the fast motor that knows where it's going. Chembiochem 11, 2232-2243 (2010).
    • (2010) Chembiochem , vol.11 , pp. 2232-2243
    • Crozat, E.1    Grainge, I.2
  • 112
    • 77953236795 scopus 로고    scopus 로고
    • DNA chirality-dependent stimulation of topoisomerase IV activity by the C-terminal AAA+ domain of FtsK
    • Bigot, S. & Marians, K. J. DNA chirality-dependent stimulation of topoisomerase IV activity by the C-terminal AAA+ domain of FtsK. Nucleic Acids Res. 38, 3031-3040 (2010).
    • (2010) Nucleic Acids Res , vol.38 , pp. 3031-3040
    • Bigot, S.1    Marians, K.J.2
  • 113
    • 0242582268 scopus 로고    scopus 로고
    • A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV
    • Espeli, O., Lee, C. & Marians, K. J. A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV. J. Biol. Chem. 278, 44639-44644 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 44639-44644
    • Espeli, O.1    Lee, C.2    Marians, K.J.3
  • 114
    • 58649111971 scopus 로고    scopus 로고
    • Actin homolog MreB affects chromosome segregation by regulating topoisomerase IV in Escherichia coli
    • Madabhushi, R. & Marians, K. J. Actin homolog MreB affects chromosome segregation by regulating topoisomerase IV in Escherichia coli. Mol. Cell 33, 171-180 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 171-180
    • Madabhushi, R.1    Marians, K.J.2
  • 115
    • 50249129235 scopus 로고    scopus 로고
    • Dual role of topoisomerase II in centromere resolution and aurora B activity
    • Coelho, P. A. et al. Dual role of topoisomerase II in centromere resolution and aurora B activity. PLoS Biol. 6, e207 (2008).
    • (2008) PLoS Biol , vol.6
    • Coelho, P.A.1
  • 116
    • 44449103826 scopus 로고    scopus 로고
    • Plk1-dependent phosphorylation regulates functions of DNA topoisomerase IIα in cell cycle progression
    • Li, H., Wang, Y. & Liu, X. Plk1-dependent phosphorylation regulates functions of DNA topoisomerase IIα in cell cycle progression. J. Biol. Chem. 283, 6209-6221 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 6209-6221
    • Li, H.1    Wang, Y.2    Liu, X.3
  • 117
    • 0037249352 scopus 로고    scopus 로고
    • Temporal regulation of topoisomerase IV activity in E. coli
    • Espeli, O., Levine, C., Hassing, H. & Marians, K. J. Temporal regulation of topoisomerase IV activity in E. coli. Mol. Cell 11, 189-201 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 189-201
    • Espeli, O.1    Levine, C.2    Hassing, H.3    Marians, K.J.4
  • 118
    • 1542571848 scopus 로고    scopus 로고
    • SeqA protein stimulates the relaxing and decatenating activities of topoisomerase IV
    • Kang, S., Han, J., Park, J., Skarstad, K. & Wang, D. H. SeqA protein stimulates the relaxing and decatenating activities of topoisomerase IV. J. Biol. Chem. 278, 48779-48785 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 48779-48785
    • Kang, S.1    Han, J.2    Park, J.3    Skarstad, K.4    Wang, D.H.5
  • 119
    • 0023433855 scopus 로고
    • Supercoiling of the DNA template during transcription
    • Liu, L. F. & Wang, J. C. Supercoiling of the DNA template during transcription. Proc. Natl Acad. Sci. USA 84, 7024-7027 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7024-7027
    • Liu, L.F.1    Wang, J.C.2
  • 120
    • 0024279845 scopus 로고
    • Transcription generates positively and negatively supercoiled domains in the template
    • Wu, H. Y., Shyy, S. H., Wang, J. C. & Liu, L. F. Transcription generates positively and negatively supercoiled domains in the template. Cell 53, 433-440 (1988).
    • (1988) Cell , vol.53 , pp. 433-440
    • Wu, H.Y.1    Shyy, S.H.2    Wang, J.C.3    Liu, L.F.4
  • 121
    • 33745612978 scopus 로고    scopus 로고
    • Homeostatic regulation of supercoiling sensitivity coordinates transcription of the bacterial genome
    • Blot, N., Mavathur, R., Geertz, M., Travers, A. & Muskhelishvili, G. Homeostatic regulation of supercoiling sensitivity coordinates transcription of the bacterial genome. EMBO Rep. 7, 710-715 (2006).
    • (2006) EMBO Rep , vol.7 , pp. 710-715
    • Blot, N.1    Mavathur, R.2    Geertz, M.3    Travers, A.4    Muskhelishvili, G.5
  • 122
    • 0028006543 scopus 로고
    • Hypernegative supercoiling of the DNA template during transcription elongation in vitro
    • Drolet, M., Bi, X. & Liu, L. F. Hypernegative supercoiling of the DNA template during transcription elongation in vitro. J. Biol. Chem. 269, 2068-2074 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 2068-2074
    • Drolet, M.1    Bi, X.2    Liu, L.F.3
  • 123
    • 70449522304 scopus 로고    scopus 로고
    • Topoisomerase i suppresses genomic instability by preventing interference between replication and transcription
    • Tuduri, S. et al. Topoisomerase I suppresses genomic instability by preventing interference between replication and transcription. Nature Cell Biol. 11, 1315-1324 (2009).
    • (2009) Nature Cell Biol , vol.11 , pp. 1315-1324
    • Tuduri, S.1
  • 124
    • 0028966185 scopus 로고
    • Overexpression of RNase H partially complements the growth defect of an Escherichia coli ΔtopA mutant: R-loop formation is a major problem in the absence of DNA topoisomerase i
    • Drolet, M. et al. Overexpression of RNase H partially complements the growth defect of an Escherichia coli ΔtopA mutant: R-loop formation is a major problem in the absence of DNA topoisomerase I. Proc. Natl Acad. Sci. USA 92, 3526-3530 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3526-3530
    • Drolet, M.1
  • 125
    • 0033523016 scopus 로고    scopus 로고
    • Relaxation of transcription-induced negative supercoiling is an essential function of Escherichia coli DNA topoisomerase i
    • Mass, E. & Drolet, M. Relaxation of transcription-induced negative supercoiling is an essential function of Escherichia coli DNA topoisomerase I. J. Biol. Chem. 274, 16654-16658 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 16654-16658
    • Mass, E.1    Drolet, M.2
  • 126
    • 0042733395 scopus 로고    scopus 로고
    • Direct interaction between Escherichia coli RNA polymerase and the zinc ribbon domains of DNA topoisomerase i
    • Cheng, B., Zhu, C. X., Ji, C., Ahumada, A. & Tse-Dinh, Y. C. Direct interaction between Escherichia coli RNA polymerase and the zinc ribbon domains of DNA topoisomerase I. J. Biol. Chem. 278, 30705-30710 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 30705-30710
    • Cheng, B.1    Zhu, C.X.2    Ji, C.3    Ahumada, A.4    Tse-Dinh, Y.C.5
  • 127
    • 0027186443 scopus 로고
    • DNA topoisomerase i is involved in both repression and activation of transcription
    • Merino, A., Madden, K. R., Lane, W. S., Champoux, J. J. & Reinberg, D. DNA topoisomerase I is involved in both repression and activation of transcription. Nature 365, 227-232 (1993).
    • (1993) Nature , vol.365 , pp. 227-232
    • Merino, A.1    Madden, K.R.2    Lane, W.S.3    Champoux, J.J.4    Reinberg, D.5
  • 128
    • 0344875486 scopus 로고    scopus 로고
    • Elongation by RNA polymerase II on chromatin templates requires topoisomerase activity
    • Mondal, N. et al. Elongation by RNA polymerase II on chromatin templates requires topoisomerase activity. Nucleic Acids Res. 31, 5016-5024 (2003).
    • (2003) Nucleic Acids Res , vol.31 , pp. 5016-5024
    • Mondal, N.1
  • 129
    • 77954957199 scopus 로고    scopus 로고
    • Topoisomerase i regulates open chromatin and controls gene expression in vivo
    • Durand-Dubief, M., Persson, J., Norman, U., Hartsuiker, E. & Ekwall, K. Topoisomerase I regulates open chromatin and controls gene expression in vivo. EMBO J. 29, 2126-2134 (2010).
    • (2010) EMBO J , vol.29 , pp. 2126-2134
    • Durand-Dubief, M.1    Persson, J.2    Norman, U.3    Hartsuiker, E.4    Ekwall, K.5
  • 130
    • 40049085952 scopus 로고    scopus 로고
    • Global transcription regulation by DNA topoisomerase i in exponentially growing Saccharomyces cerevisiae cells: Activation of telomere-proximal genes by TOP1 deletion
    • Lotito, L. et al. Global transcription regulation by DNA topoisomerase I in exponentially growing Saccharomyces cerevisiae cells: activation of telomere-proximal genes by TOP1 deletion. J. Mol. Biol. 377, 311-322 (2008).
    • (2008) J. Mol. Biol , vol.377 , pp. 311-322
    • Lotito, L.1
  • 131
    • 15844415445 scopus 로고    scopus 로고
    • Specific phosphorylation of SR proteins by mammalian DNA topoisomerase i
    • Rossi, F. et al. Specific phosphorylation of SR proteins by mammalian DNA topoisomerase I. Nature 381, 80-82 (1996).
    • (1996) Nature , vol.381 , pp. 80-82
    • Rossi, F.1
  • 132
    • 78049422337 scopus 로고    scopus 로고
    • The SR protein B52/SRp55 is required for DNA topoisomerase i recruitment to chromatin, mRNA release and transcription shutdown
    • Juge, F., Fernando, C., Fic, W. & Tazi, J. The SR protein B52/SRp55 is required for DNA topoisomerase I recruitment to chromatin, mRNA release and transcription shutdown. PLoS Genet. 6, e1001124 (2010).
    • (2010) PLoS Genet , vol.6
    • Juge, F.1    Fernando, C.2    Fic, W.3    Tazi, J.4
  • 133
    • 50649093361 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to the splicing factor ASF/SF2 and regulates its phosphorylation by DNA topoisomerase i
    • Malanga, M., Czubaty, A., Girstun, A., Staron, K. & Althaus, F. R. Poly(ADP-ribose) binds to the splicing factor ASF/SF2 and regulates its phosphorylation by DNA topoisomerase I. J. Biol. Chem. 283, 19991-19998 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 19991-19998
    • Malanga, M.1    Czubaty, A.2    Girstun, A.3    Staron, K.4    Althaus, F.R.5
  • 134
    • 40349114500 scopus 로고    scopus 로고
    • Topoisomerase IIβ negatively modulates retinoic acid receptor a function: A novel mechanism of retinoic acid resistance
    • Mcnamara, S., Wang, H., Hanna, N. & Miller, W. Topoisomerase IIβ negatively modulates retinoic acid receptor a function: a novel mechanism of retinoic acid resistance. Mol. Cell. Biol. 28, 2066-2077 (2008).
    • (2008) Mol. Cell. Biol , vol.28 , pp. 2066-2077
    • McNamara, S.1    Wang, H.2    Hanna, N.3    Miller, W.4
  • 135
    • 0037131525 scopus 로고    scopus 로고
    • Targeted stimulation of meiotic recombination
    • Pecia, A. et al. Targeted stimulation of meiotic recombination. Cell 111, 173-184 (2002).
    • (2002) Cell , vol.111 , pp. 173-184
    • Pecia, A.1
  • 136
    • 36448991603 scopus 로고    scopus 로고
    • Spo11 and the formation of DNA double-strand breaks in meiosis
    • Keeney, S. Spo11 and the formation of DNA double-strand breaks in meiosis. Genome Dyn. Stab. 2, 81-123 (2008).
    • (2008) Genome Dyn. Stab , vol.2 , pp. 81-123
    • Keeney, S.1
  • 137
    • 23944459784 scopus 로고    scopus 로고
    • Endonucleolytic processing of covalent protein-linked double-strand breaks
    • Neale, M. J., Pan, J. & Keeney, S. Endonucleolytic processing of covalent protein-linked double-strand breaks. Nature 436, 1053-1057 (2005).
    • (2005) Nature , vol.436 , pp. 1053-1057
    • Neale, M.J.1    Pan, J.2    Keeney, S.3
  • 138
    • 33745611147 scopus 로고    scopus 로고
    • Double-stranded DNA breaks and gene functions in recombination and meiosis
    • Li, W. & Ma, H. Double-stranded DNA breaks and gene functions in recombination and meiosis. Cell Res. 16, 402-412 (2006).
    • (2006) Cell Res , vol.16 , pp. 402-412
    • Li, W.1    Ma, H.2
  • 139
    • 0033638183 scopus 로고    scopus 로고
    • Chromosome synapsis defects and sexually dimorphic meiotic progression in mice lacking Spo11
    • Baudat, F., Manova, K., Yuen, J. P., Jasin, M. & Keeney, S. Chromosome synapsis defects and sexually dimorphic meiotic progression in mice lacking Spo11. Mol. Cell 6, 989-998 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 989-998
    • Baudat, F.1    Manova, K.2    Yuen, J.P.3    Jasin, M.4    Keeney, S.5
  • 140
    • 58149308077 scopus 로고    scopus 로고
    • Ctp1 CtIP and Rad32 Mre11 nuclease activity are required for Rec12e Spo11 removal, but Rec12 Spo11 removal is dispensable for other MRN-dependent meiotic functions
    • Hartsuiker, E. et al. Ctp1 CtIP and Rad32 Mre11 nuclease activity are required for Rec12 Spo11 removal, but Rec12 Spo11 removal is dispensable for other MRN-dependent meiotic functions. Mol. Cell. Biol. 29, 1671-1681 (2009).
    • (2009) Mol. Cell. Biol , vol.29 , pp. 1671-1681
    • Hartsuiker, E.1
  • 141
    • 77953236291 scopus 로고    scopus 로고
    • Meiotic recombination provokes functional activation of the p53 regulatory network
    • Lu, W. J., Chapo, J., Roig, I. & Abrams, J. M. Meiotic recombination provokes functional activation of the p53 regulatory network. Science 328, 1278-1281 (2010).
    • (2010) Science , vol.328 , pp. 1278-1281
    • Lu, W.J.1    Chapo, J.2    Roig, I.3    Abrams, J.M.4
  • 142
    • 0037059331 scopus 로고    scopus 로고
    • Phase and G2 arrests induced by topoisomerase i poisons are dependent on ATR kinase function
    • Cliby, W. A. S. Phase and G2 arrests induced by topoisomerase I poisons are dependent on ATR kinase function. J. Biol. Chem. 277, 1599-1606 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 1599-1606
    • Cliby, W.A.S.1
  • 143
    • 34547617889 scopus 로고    scopus 로고
    • BRCA1-and BRCA2-deficient cells are sensitive to etoposide-induced DNA double-strand breaks via topoisomerase II
    • Treszezamsky, A. D. et al. BRCA1-and BRCA2-deficient cells are sensitive to etoposide-induced DNA double-strand breaks via topoisomerase II. Cancer Res. 67, 7078-7081 (2007).
    • (2007) Cancer Res , vol.67 , pp. 7078-7081
    • Treszezamsky, A.D.1
  • 144
    • 70350502118 scopus 로고    scopus 로고
    • Proteasome-dependent processing of topoisomerase I-DNA adducts into DNA double strand breaks at arrested replication forks
    • Lin, C. P., Ban, Y., Lyu, Y. L. & Liu, L. F. Proteasome-dependent processing of topoisomerase I-DNA adducts into DNA double strand breaks at arrested replication forks. J. Biol. Chem. 284, 28084-28092 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 28084-28092
    • Lin, C.P.1    Ban, Y.2    Lyu, Y.L.3    Liu, L.F.4
  • 145
    • 0034635958 scopus 로고    scopus 로고
    • SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damage
    • Mao, Y., Sun, M., Desai, S. D. & Liu, L. F. SUMO-1 conjugation to topoisomerase I: a possible repair response to topoisomerase-mediated DNA damage. Proc. Natl Acad. Sci. USA 97, 4046-4051 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4046-4051
    • Mao, Y.1    Sun, M.2    Desai, S.D.3    Liu, L.F.4
  • 146
    • 0035798622 scopus 로고    scopus 로고
    • 26 Sproteasome-mediated degradation of topoisomerase II cleavable complexes
    • Mao, Y., Desai, S. D., Ting, C. Y., Hwang, J. & Liu, L. F. 26 Sproteasome-mediated degradation of topoisomerase II cleavable complexes. J. Biol. Chem. 276, 40652-40658 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 40652-40658
    • Mao, Y.1    Desai, S.D.2    Ting, C.Y.3    Hwang, J.4    Liu, L.F.5
  • 147
    • 0033569666 scopus 로고    scopus 로고
    • Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase i complexes
    • Pouliot, J. J., Yao, K. C., Robertson, C. A. & Nash, H. A. Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes. Science 286, 552-555 (1999).
    • (1999) Science , vol.286 , pp. 552-555
    • Pouliot, J.J.1    Yao, K.C.2    Robertson, C.A.3    Nash, H.A.4
  • 148
    • 33745154128 scopus 로고    scopus 로고
    • Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage
    • Nitiss, K. C., Malik, M., He, X., White, S. W. & Nitiss, J. L. Tyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damage. Proc. Natl Acad. Sci. USA 103, 8953-8958 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8953-8958
    • Nitiss, K.C.1    Malik, M.2    He, X.3    White, S.W.4    Nitiss, J.L.5
  • 149
    • 70349673605 scopus 로고    scopus 로고
    • A human 5′-tyrosyl DNA phosphodiesterase that repairs topoisomerase-mediated DNA damage
    • Cortes Ledesma, F., El Khamisy, S. F., Zuma, M. C., Osborn, K. & Caldecott, K. W. A human 5′-tyrosyl DNA phosphodiesterase that repairs topoisomerase-mediated DNA damage. Nature 461, 674-678 (2009).
    • (2009) Nature , vol.461 , pp. 674-678
    • Cortes Ledesma, F.1    El Khamisy, S.F.2    Zuma, M.C.3    Osborn, K.4    Caldecott, K.W.5
  • 150
    • 78650964114 scopus 로고    scopus 로고
    • TDP2/TTRAP is the major 5′-tyrosyl DNA phosphodiesterase activity in vertebrate cells and is critical for cellular resistance to topoisomerase II-induced DNA damage
    • Zeng, Z., Cortes-Ledesma, F., El Khamisy, S. F. & Caldecott, K. W. TDP2/TTRAP is the major 5′-tyrosyl DNA phosphodiesterase activity in vertebrate cells and is critical for cellular resistance to topoisomerase II-induced DNA damage. J. Biol. Chem. 286, 403-409 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 403-409
    • Zeng, Z.1    Cortes-Ledesma, F.2    El Khamisy, S.F.3    Caldecott, K.W.4
  • 151
    • 0034714278 scopus 로고    scopus 로고
    • SUMO-1 conjugation to human DNA topoisomerase II isozymes
    • Mao, Y., Desai, S. D. & Liu, L. F. SUMO-1 conjugation to human DNA topoisomerase II isozymes. J. Biol. Chem. 275, 26066-26073 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 26066-26073
    • Mao, Y.1    Desai, S.D.2    Liu, L.F.3
  • 152
    • 0030854371 scopus 로고    scopus 로고
    • Ubiquitin-dependent destruction of topoisomerase i is stimulated by the antitumor drug camptothecin
    • Desai, S. D., Liu, L. F., Vazquez-Abad, D. & D'Arpa, P. Ubiquitin-dependent destruction of topoisomerase I is stimulated by the antitumor drug camptothecin. J. Biol. Chem. 272, 24159-24164 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 24159-24164
    • Desai, S.D.1    Liu, L.F.2    Vazquez-Abad, D.3    D'Arpa, P.4
  • 153
    • 47849130071 scopus 로고    scopus 로고
    • Hyperphosphorylation of RNA polymerase II in response to topoisomerase i cleavage complexes and its association with transcription-and BRCA1-dependent degradation of topoisomerase i
    • Sordet, O. et al. Hyperphosphorylation of RNA polymerase II in response to topoisomerase I cleavage complexes and its association with transcription-and BRCA1-dependent degradation of topoisomerase I. J. Mol. Biol. 381, 540-549 (2008).
    • (2008) J. Mol. Biol , vol.381 , pp. 540-549
    • Sordet, O.1
  • 154
    • 0037378557 scopus 로고    scopus 로고
    • Transcription-dependent degradation of topoisomerase I-DNA covalent complexes
    • Desai, S. D. et al. Transcription-dependent degradation of topoisomerase I-DNA covalent complexes. Mol. Cell. Biol. 23, 2341-2350 (2003).
    • (2003) Mol. Cell. Biol , vol.23 , pp. 2341-2350
    • Desai, S.D.1
  • 155
    • 0037452830 scopus 로고    scopus 로고
    • The topoisomerase IIβ circular clamp arrests transcription and signals a 26S proteasome pathway
    • Xiao, H. et al. The topoisomerase IIβ circular clamp arrests transcription and signals a 26S proteasome pathway. Proc. Natl Acad. Sci. USA 100, 3239-3244 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 3239-3244
    • Xiao, H.1
  • 156
    • 0029065571 scopus 로고
    • Association of increased spontaneous mutation rates with high levels of transcription in yeast
    • Datta, A. & Jinks-Robertson, S. Association of increased spontaneous mutation rates with high levels of transcription in yeast. Science 268, 1616-1619 (1995).
    • (1995) Science , vol.268 , pp. 1616-1619
    • Datta, A.1    Jinks-Robertson, S.2
  • 157
    • 79551675372 scopus 로고    scopus 로고
    • Role for topoisomerase 1 in transcription-associated mutagenesis in yeast
    • Lippert, M. J. et al. Role for topoisomerase 1 in transcription- associated mutagenesis in yeast. Proc. Natl Acad. Sci. USA 108, 698-703 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 698-703
    • Lippert, M.J.1
  • 158
    • 79551661538 scopus 로고    scopus 로고
    • Topoisomerase 1 provokes the formation of short deletions in repeated sequences upon high transcription in Saccharomyces cerevisiae
    • Takahashi, T., Burguiere-Slezak, G., Van der Kemp, P. A. & Boiteux, S. Topoisomerase 1 provokes the formation of short deletions in repeated sequences upon high transcription in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 108, 692-697 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 692-697
    • Takahashi, T.1    Burguiere-Slezak, G.2    Van Der Kemp, P.A.3    Boiteux, S.4
  • 159
    • 79959504063 scopus 로고    scopus 로고
    • Mutagenic processing of ribonucleotides in DNA by yeast topoisomerase i
    • Kim, N. et al. Mutagenic processing of ribonucleotides in DNA by yeast topoisomerase I. Science 332, 1561-1564 (2011).
    • (2011) Science , vol.332 , pp. 1561-1564
    • Kim, N.1
  • 160
    • 0033529696 scopus 로고    scopus 로고
    • Stimulated activity of human topoisomerases IIα and IIβ on RNA-containing substrates
    • Wang, Y., Knudsen, B. R., Bjergbaek, L., Westergaard, O. & Andersen, A. H. Stimulated activity of human topoisomerases IIα and IIβ on RNA-containing substrates. J. Biol. Chem. 274, 22839-22846 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 22839-22846
    • Wang, Y.1    Knudsen, B.R.2    Bjergbaek, L.3    Westergaard, O.4    Andersen, A.H.5
  • 161
    • 61749089887 scopus 로고    scopus 로고
    • Coordinating the two protomer active sites of human topoisomerase IIα: Nicks as topoisomerase II poisons
    • Deweese, J. E. & Osheroff, N. Coordinating the two protomer active sites of human topoisomerase IIα: nicks as topoisomerase II poisons. Biochemistry 48, 1439-1441 (2009).
    • (2009) Biochemistry , vol.48 , pp. 1439-1441
    • Deweese, J.E.1    Osheroff, N.2
  • 162
    • 4644251969 scopus 로고    scopus 로고
    • Individual nucleotide bases, not base pairs, are critical for triggering site-specific DNA cleavage by vaccinia topoisomerase
    • Sayer, J., Jerina, D. & Shuman, S. Individual nucleotide bases, not base pairs, are critical for triggering site-specific DNA cleavage by vaccinia topoisomerase. J. Biol. Chem. 39718-39726 (2004).
    • (2004) J. Biol. Chem. , pp. 39718-39726
    • Sayer, J.1    Jerina, D.2    Shuman, S.3
  • 163
    • 0031012785 scopus 로고    scopus 로고
    • Apurinic sites are position-specific topoisomerase II poisons
    • Kingma, P. S. & Osheroff, N. Apurinic sites are position-specific topoisomerase II poisons. J. Biol. Chem. 272, 1148-1155 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 1148-1155
    • Kingma, P.S.1    Osheroff, N.2
  • 164
    • 0030900937 scopus 로고    scopus 로고
    • Spontaneous DNA damage stimulates topoisomerase II-mediated DNA cleavage
    • Kingma, P. S. & Osheroff, N. Spontaneous DNA damage stimulates topoisomerase II-mediated DNA cleavage. J. Biol. Chem. 272, 7488-7493 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 7488-7493
    • Kingma, P.S.1    Osheroff, N.2
  • 165
    • 0345447604 scopus 로고    scopus 로고
    • Srs2 and Sgs1-Top3 suppress crossovers during double-strand break repair in yeast
    • Ira, G., Malkova, A., Liberi, G., Foiani, M. & Haber, J. E. Srs2 and Sgs1-Top3 suppress crossovers during double-strand break repair in yeast. Cell 115, 401-411 (2003).
    • (2003) Cell , vol.115 , pp. 401-411
    • Ira, G.1    Malkova, A.2    Liberi, G.3    Foiani, M.4    Haber, J.E.5
  • 166
    • 0347987856 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase suppresses crossing over during homologous recombination
    • Wu, L. & Hickson, I. D. The Bloom's syndrome helicase suppresses crossing over during homologous recombination. Nature 426, 870-874 (2003).
    • (2003) Nature , vol.426 , pp. 870-874
    • Wu, L.1    Hickson, I.D.2
  • 167
    • 33746600628 scopus 로고    scopus 로고
    • Topoisomerase IIIα and Bloom's helicase can resolve a mobile double Holliday junction substrate through convergent branch migration
    • Plank, J. L., Wu, J. & Hsieh, T. S. Topoisomerase IIIα and Bloom's helicase can resolve a mobile double Holliday junction substrate through convergent branch migration. Proc. Natl Acad. Sci. USA 103, 11118-11123 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 11118-11123
    • Plank, J.L.1    Wu, J.2    Hsieh, T.S.3
  • 168
    • 0142180061 scopus 로고    scopus 로고
    • RecQ helicase stimulates both DNA catenation and changes in DNA topology by topoisomerase III
    • Harmon, F. G., Brockman, J. P. & Kowalczykowski, S. C. RecQ helicase stimulates both DNA catenation and changes in DNA topology by topoisomerase III. J. Biol. Chem. 278, 42668-42678 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 42668-42678
    • Harmon, F.G.1    Brockman, J.P.2    Kowalczykowski, S.C.3
  • 169
    • 54349114671 scopus 로고    scopus 로고
    • BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome
    • Singh, T. R. et al. BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome. Genes Dev. 22, 2856-2868 (2008).
    • (2008) Genes Dev , vol.22 , pp. 2856-2868
    • Singh, T.R.1
  • 170
    • 77956325620 scopus 로고    scopus 로고
    • DNA end resection by Dna2-Sgs1-RPA and its stimulation by Top3-Rmi1 and Mre11-Rad50-Xrs2
    • Cejka, P. et al. DNA end resection by Dna2-Sgs1-RPA and its stimulation by Top3-Rmi1 and Mre11-Rad50-Xrs2. Nature 467, 112-116 (2010).
    • (2010) Nature , vol.467 , pp. 112-116
    • Cejka, P.1
  • 171
    • 77956302112 scopus 로고    scopus 로고
    • Mechanism of the ATP-dependent DNA end-resection machinery from Saccharomyces cerevisiae
    • Niu, H. et al. Mechanism of the ATP-dependent DNA end-resection machinery from Saccharomyces cerevisiae. Nature 467, 108-111 (2010).
    • (2010) Nature , vol.467 , pp. 108-111
    • Niu, H.1
  • 172
    • 0028114974 scopus 로고
    • Serine 1524 is a major site of phosphorylation on human topoisomerase II α protein in vivo and is a substrate for casein kinase II in vitro
    • Wells, N. J., Addison, C. M., Fry, A. M., Ganapathi, R. & Hickson, I. D. Serine 1524 is a major site of phosphorylation on human topoisomerase II α protein in vivo and is a substrate for casein kinase II in vitro. J. Biol. Chem. 269, 29746-29751 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 29746-29751
    • Wells, N.J.1    Addison, C.M.2    Fry, A.M.3    Ganapathi, R.4    Hickson, I.D.5
  • 173
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary, C. et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325, 834-840 (2009).
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1
  • 174
    • 78349263872 scopus 로고    scopus 로고
    • PIASy-dependent SUMOylation regulates DNA topoisomerase II α activity
    • Ryu, H., Furuta, M., Kirkpatrick, D., Gygi, S. P. & Azuma, Y. PIASy-dependent SUMOylation regulates DNA topoisomerase II α activity. J. Cell Biol. 191, 783-794 (2010).
    • (2010) J. Cell Biol , vol.191 , pp. 783-794
    • Ryu, H.1    Furuta, M.2    Kirkpatrick, D.3    Gygi, S.P.4    Azuma, Y.5
  • 175
    • 41149146735 scopus 로고    scopus 로고
    • Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIα
    • Dawlaty, M. M. et al. Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIα. Cell 133, 103-115 (2008).
    • (2008) Cell , vol.133 , pp. 103-115
    • Dawlaty, M.M.1
  • 176
    • 0036291014 scopus 로고    scopus 로고
    • The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II
    • Bachant, J., Alcasabas, A., Blat, Y., Kleckner, N. & Elledge, S. J. The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II. Mol. Cell 9, 1169-1182 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 1169-1182
    • Bachant, J.1    Alcasabas, A.2    Blat, Y.3    Kleckner, N.4    Elledge, S.J.5
  • 177
    • 0032961902 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase activates topoisomerase IIα through a mechanism independent of phosphorylation
    • Shapiro, P. et al. Extracellular signal-regulated kinase activates topoisomerase IIα through a mechanism independent of phosphorylation. Mol. Cell. Biol. 19, 3551-3560 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , pp. 3551-3560
    • Shapiro, P.1
  • 178
    • 0037200032 scopus 로고    scopus 로고
    • Overexpression of the atypical protein kinase C ζ reduces topoisomerase II catalytic activity, cleavable complexes formation, and drug-induced cytotoxicity in monocytic U937 leukemia cells
    • Plo, I. et al. Overexpression of the atypical protein kinase C ζ reduces topoisomerase II catalytic activity, cleavable complexes formation, and drug-induced cytotoxicity in monocytic U937 leukemia cells. J. Biol. Chem. 277, 31407-31415 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 31407-31415
    • Plo, I.1
  • 179
    • 17544379830 scopus 로고    scopus 로고
    • Phosphorylation-independent stimulation of DNA topoisomerase II α activity
    • Kimura, K., Saijo, M., Tanaka, M. & Enomoto, T. Phosphorylation- independent stimulation of DNA topoisomerase II α activity. J. Biol. Chem. 271, 10990-10995 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 10990-10995
    • Kimura, K.1    Saijo, M.2    Tanaka, M.3    Enomoto, T.4
  • 180
    • 0026728290 scopus 로고
    • Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes
    • Bernard, P. & Couturier, M. Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes. J. Mol. Biol. 226, 735-745 (1992).
    • (1992) J. Mol. Biol , vol.226 , pp. 735-745
    • Bernard, P.1    Couturier, M.2
  • 181
    • 33750206130 scopus 로고    scopus 로고
    • A strand-passage conformation of DNA gyrase is required to allow the bacterial toxin, CcdB, to access its binding site
    • Smith, A. B. & Maxwell, A. A strand-passage conformation of DNA gyrase is required to allow the bacterial toxin, CcdB, to access its binding site. Nucleic Acids Res. 34, 4667-4676 (2006).
    • (2006) Nucleic Acids Res , vol.34 , pp. 4667-4676
    • Smith, A.B.1    Maxwell, A.2
  • 182
    • 0025964113 scopus 로고
    • The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase
    • Vizαn, J., Hernαndez-Chico, C., del Castillo, I. & Moreno, F. The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase. EMBO J. 10, 467-476 (1991).
    • (1991) EMBO J , vol.10 , pp. 467-476
    • Vizn, J.1    Hernndez-Chico, C.2    Del Castillo, I.3    Moreno, F.4
  • 183
    • 20344367084 scopus 로고    scopus 로고
    • A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA
    • Hegde, S. et al. A fluoroquinolone resistance protein from Mycobacterium tuberculosis that mimics DNA. Science 308, 1480-1483 (2005).
    • (2005) Science , vol.308 , pp. 1480-1483
    • Hegde, S.1
  • 184
    • 0037180432 scopus 로고    scopus 로고
    • The mechanism of topoisomerase i poisoning by a camptothecin analog
    • Staker, B. L. et al. The mechanism of topoisomerase I poisoning by a camptothecin analog. Proc. Natl Acad. Sci. USA 99, 15387-15392 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 15387-15392
    • Staker, B.L.1
  • 185
    • 0029978822 scopus 로고    scopus 로고
    • The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallography
    • Lewis, R. J. et al. The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallography. EMBO J. 15, 1412-1420 (1996).
    • (1996) EMBO J , vol.15 , pp. 1412-1420
    • Lewis, R.J.1
  • 186
    • 0030893658 scopus 로고    scopus 로고
    • The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin
    • Tsai, F. T. et al. The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin. Proteins 28, 41-52 (1997).
    • (1997) Proteins , vol.28 , pp. 41-52
    • Tsai, F.T.1
  • 187
    • 0141591551 scopus 로고    scopus 로고
    • Structure of the topoisomerase II ATPase region and its mechanism of inhibition by the chemotherapeutic agent ICRF-187
    • Classen, S., Olland, S. & Berger, J. M. Structure of the topoisomerase II ATPase region and its mechanism of inhibition by the chemotherapeutic agent ICRF-187. Proc. Natl Acad. Sci. USA 100, 10629-10634 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10629-10634
    • Classen, S.1    Olland, S.2    Berger, J.M.3
  • 188
    • 33749129568 scopus 로고    scopus 로고
    • Structural basis for topoisomerase VI inhibition by the anti-Hsp90 drug radicicol
    • Corbett, K. D. & Berger, J. M. Structural basis for topoisomerase VI inhibition by the anti-Hsp90 drug radicicol. Nucleic Acids Res. 34, 4269-4277 (2006).
    • (2006) Nucleic Acids Res , vol.34 , pp. 4269-4277
    • Corbett, K.D.1    Berger, J.M.2
  • 189
    • 71549138377 scopus 로고    scopus 로고
    • A crystal structure of the bifunctional antibiotic simocyclinone D8, bound to DNA gyrase
    • Edwards, M. J. et al. A crystal structure of the bifunctional antibiotic
    • (2009) Science , vol.326 , pp. 1415-1418
    • Edwards, M.J.1
  • 190
    • 77955917935 scopus 로고    scopus 로고
    • Type IIA topoisomerase inhibition by a new class of antibacterial agents
    • Bax, B. D. et al. Type IIA topoisomerase inhibition by a new class of antibacterial agents. Nature 466, 935-940 (2010).
    • (2010) Nature , vol.466 , pp. 935-940
    • Bax, B.D.1
  • 191
    • 58149083577 scopus 로고    scopus 로고
    • Asp-to-Asn substitution at the first position of the DxD TOPRIM motif of recombinant bacterial topoisomerase i is extremely lethal to E. coli
    • Cheng, B. et al. Asp-to-Asn substitution at the first position of the DxD TOPRIM motif of recombinant bacterial topoisomerase I is extremely lethal to E. coli. J. Mol. Biol. 385, 558-567 (2009).
    • (2009) J. Mol. Biol , vol.385 , pp. 558-567
    • Cheng, B.1
  • 192
    • 33947247352 scopus 로고    scopus 로고
    • Gyrase inhibitors induce an oxidative damage cellular death pathway in Escherichia coli
    • Dwyer, D. J., Kohanski, M. A., Hayete, B. & Collins, J. J. Gyrase inhibitors induce an oxidative damage cellular death pathway in Escherichia coli. Mol. Syst. Biol. 3, 91 (2007).
    • (2007) Mol. Syst. Biol , vol.3 , pp. 91
    • Dwyer, D.J.1    Kohanski, M.A.2    Hayete, B.3    Collins, J.J.4
  • 193
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski, M. A., Dwyer, D. J., Hayete, B., Lawrence, C. A. & Collins, J. J. A common mechanism of cellular death induced by bactericidal antibiotics. Cell 130, 797-810 (2007).
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 194
    • 77950325093 scopus 로고    scopus 로고
    • Contribution of reactive oxygen species to pathways of quinolone-mediated bacterial cell death
    • Wang, X., Zhao, X., Malik, M. & Drlica, K. Contribution of reactive oxygen species to pathways of quinolone-mediated bacterial cell death. J. Antimicrob. Chemother. 65, 520-524 (2010).
    • (2010) J. Antimicrob. Chemother , vol.65 , pp. 520-524
    • Wang, X.1    Zhao, X.2    Malik, M.3    Drlica, K.4
  • 195
    • 0035137364 scopus 로고    scopus 로고
    • Differential effects of the poly (ADP-ribose) polymerase (PARP) inhibitor NU1025 on topoisomerase i and II inhibitor cytotoxicity in L1210 cells in vitro
    • Bowman, K. J., Newell, D. R., Calvert, A. H. & Curtin, N. J. Differential effects of the poly (ADP-ribose) polymerase (PARP) inhibitor NU1025 on topoisomerase I and II inhibitor cytotoxicity in L1210 cells in vitro. Br. J. Cancer 84, 106-112 (2001).
    • (2001) Br. J. Cancer , vol.84 , pp. 106-112
    • Bowman, K.J.1    Newell, D.R.2    Calvert, A.H.3    Curtin, N.J.4
  • 196
    • 3042741064 scopus 로고    scopus 로고
    • Increased susceptibility of poly(ADP-ribose) polymerase-1 knockout cells to antitumor triazoloacridone C-1305 is associated with permanent G2 cell cycle arrest
    • Wesierska-Gadek, J., Schloffer, D., Gueorguieva, M., Uhl, M. & Skladanowski, A. Increased susceptibility of poly(ADP-ribose) polymerase-1 knockout cells to antitumor triazoloacridone C-1305 is associated with permanent G2 cell cycle arrest. Cancer Res. 64, 4487-4497 (2004).
    • (2004) Cancer Res , vol.64 , pp. 4487-4497
    • Wesierska-Gadek, J.1    Schloffer, D.2    Gueorguieva, M.3    Uhl, M.4    Skladanowski, A.5
  • 197
    • 78650556334 scopus 로고    scopus 로고
    • Inhibition of poly (ADP-ribose) polymerase-1 enhances doxorubicin activity against liver cancer cells
    • Munoz-Gamez, J. A. et al. Inhibition of poly (ADP-ribose) polymerase-1 enhances doxorubicin activity against liver cancer cells. Cancer Lett. 301, 47-56.
    • Cancer Lett , vol.301 , pp. 47-56
    • Munoz-Gamez, J.A.1
  • 198
    • 0027516123 scopus 로고
    • Novel HeLa topoisomerase II is the IIβ isoform: Complete coding sequence and homology with other type II topoisomerases
    • Austin, C., Sng, J., Patel, S. & Fisher, L. Novel HeLa topoisomerase II is the IIβ isoform: complete coding sequence and homology with other type II topoisomerases. Biochim. Biophys. Acta 1172, 283-291 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1172 , pp. 283-291
    • Austin, C.1    Sng, J.2    Patel, S.3    Fisher, L.4
  • 199
    • 34547119974 scopus 로고    scopus 로고
    • C-terminal regions of topoisomerase IIα and IIβ determine isoform-specific functioning of the enzymes in vivo
    • Linka, R. M. et al. C-terminal regions of topoisomerase IIα and IIβ determine isoform-specific functioning of the enzymes in vivo. Nucleic Acids Res. 35, 3810-3822 (2007).
    • (2007) Nucleic Acids Res , vol.35 , pp. 3810-3822
    • Linka, R.M.1
  • 200
    • 77954958609 scopus 로고    scopus 로고
    • TRF2 and apollo cooperate with topoisomerase 2 α to protect human telomeres from replicative damage
    • Ye, J. et al. TRF2 and apollo cooperate with topoisomerase 2 α to protect human telomeres from replicative damage. Cell 142, 230-242 (2010).
    • (2010) Cell , vol.142 , pp. 230-242
    • Ye, J.1
  • 201
    • 0034988263 scopus 로고    scopus 로고
    • Co-localization of chicken DNA topoisomerase IIa, but not β, with sites of DNA replication and possible involvement of a C-terminal region of a through its binding to PCNA
    • Niimi, A., Suka, N., Harata, M., Kikuchi, A. & Mizuno, S. Co-localization of chicken DNA topoisomerase IIa, but not β, with sites of DNA replication and possible involvement of a C-terminal region of a through its binding to PCNA. Chromosoma 110, 102-114 (2001).
    • (2001) Chromosoma , vol.110 , pp. 102-114
    • Niimi, A.1    Suka, N.2    Harata, M.3    Kikuchi, A.4    Mizuno, S.5
  • 202
    • 0032509551 scopus 로고    scopus 로고
    • Essential mitotic functions of DNA topoisomerase IIα are not adopted by topoisomerase IIβ in human H69 cells
    • Grue, P. et al. Essential mitotic functions of DNA topoisomerase IIα are not adopted by topoisomerase IIβ in human H69 cells. J. Biol. Chem. 273, 33660-33666 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 33660-33666
    • Grue, P.1
  • 203
    • 0027490939 scopus 로고
    • Escherichia coli topoisomerase IV. Purification, characterization, subunit structure, and subunit interactions
    • Peng, H. & Marians, K. J. Escherichia coli topoisomerase IV. Purification, characterization, subunit structure, and subunit interactions. J. Biol. Chem. 268, 24481-24490 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 24481-24490
    • Peng, H.1    Marians, K.J.2
  • 204
    • 0025027077 scopus 로고
    • New topoisomerase essential for chromosome segregation in E. coli
    • Kato, J. et al. New topoisomerase essential for chromosome segregation in E. coli. Cell 63, 393-404 (1990).
    • (1990) Cell , vol.63 , pp. 393-404
    • Kato, J.1
  • 205
    • 0029955899 scopus 로고    scopus 로고
    • Conversion of DNA gyrase into a conventional type II topoisomerase
    • Kampranis, S. C. & Maxwell, A. Conversion of DNA gyrase into a conventional type II topoisomerase. Proc. Natl Acad. Sci. USA 93, 14416-14421 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14416-14421
    • Kampranis, S.C.1    Maxwell, A.2
  • 206
    • 22544467771 scopus 로고    scopus 로고
    • The structural basis for substrate specificity in DNA topoisomerase IV
    • Corbett, K. D., Schoeffler, A. J., Thomsen, N. D. & Berger, J. M. The structural basis for substrate specificity in DNA topoisomerase IV. J. Mol. Biol. 351, 545-561 (2005).
    • (2005) J. Mol. Biol , vol.351 , pp. 545-561
    • Corbett, K.D.1    Schoeffler, A.J.2    Thomsen, N.D.3    Berger, J.M.4
  • 207
    • 11244308067 scopus 로고    scopus 로고
    • Structure of the topoisomerase IV C-terminal domain: A broken β-propeller implies a role as geometry facilitator in catalysis
    • Hsieh, T.-J., Farh, L., Huang, W. M. & Chan, N.L. Structure of the topoisomerase IV C-terminal domain: a broken β-propeller implies a role as geometry facilitator in catalysis. J. Biol. Chem. 279, 55587-55593 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 55587-55593
    • Hsieh, T.-J.1    Farh, L.2    Huang, W.M.3    Chan, N.L.4
  • 208
    • 2442611949 scopus 로고    scopus 로고
    • The C-terminal domain of DNA gyrase A adopts a DNA-bending β-pinwheel fold
    • Corbett, K. D., Shultzaberger, R. K. & Berger, J. M. The C-terminal domain of DNA gyrase A adopts a DNA-bending β-pinwheel fold. Proc. Natl Acad. Sci. USA 101, 7293-7298 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7293-7298
    • Corbett, K.D.1    Shultzaberger, R.K.2    Berger, J.M.3
  • 209
    • 22544447404 scopus 로고    scopus 로고
    • A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias
    • Ruthenburg, A. J., Graybosch, D. M., Huetsch, J. C. & Verdine, G. L. A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias. J. Biol. Chem. 280, 26177-26184 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 26177-26184
    • Ruthenburg, A.J.1    Graybosch, D.M.2    Huetsch, J.C.3    Verdine, G.L.4
  • 210
    • 0035963340 scopus 로고    scopus 로고
    • Crystal structure of a complex of a type IA DNA topoisomerase with a single-stranded DNA molecule
    • Changela, A., DiGate, R. J. & Mondragn, A. Crystal structure of a complex of a type IA DNA topoisomerase with a single-stranded DNA molecule. Nature 411, 1077-1081 (2001).
    • (2001) Nature , vol.411 , pp. 1077-1081
    • Changela, A.1    Digate, R.J.2    Mondragn, A.3
  • 211
    • 77953229439 scopus 로고    scopus 로고
    • A novel and unified two-metal mechanism for DNA cleavage by type II and IA topoisomerases
    • Schmidt, B., Burgin, A., Deweese, J., Osheroff, N. & Berger, J. A novel and unified two-metal mechanism for DNA cleavage by type II and IA topoisomerases. Nature 465, 641-644 (2010).
    • (2010) Nature , vol.465 , pp. 641-644
    • Schmidt, B.1    Burgin, A.2    Deweese, J.3    Osheroff, N.4    Berger, J.5


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