메뉴 건너뛰기




Volumn 357, Issue 1, 2006, Pages 127-138

Early effects of topoisomerase I inhibition on RNA polymerase II along transcribed genes in human cells

Author keywords

Camptothecin; RNA polymerase II; Topoisomerase I; Transcription; amanitin

Indexed keywords

5,6 DICHLOROBENZIMIDAZOLE RIBOSIDE; ALPHA AMANITIN; CAMPTOTHECIN; CYCLIN DEPENDENT KINASE INHIBITOR; DNA TOPOISOMERASE; RNA POLYMERASE II; TATA BINDING PROTEIN;

EID: 33644772382     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.12.069     Document Type: Article
Times cited : (52)

References (51)
  • 1
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: A molecular perspective
    • J.C. Wang Cellular roles of DNA topoisomerases: a molecular perspective Nature Rev. Mol. Cell Biol. 3 2002 430 440
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 2
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • J.C. Wang DNA topoisomerases Annu. Rev. Biochem. 65 1996 635 692
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 635-692
    • Wang, J.C.1
  • 3
    • 0026555506 scopus 로고
    • Control of bacterial DNA supercoiling
    • K. Drlica Control of bacterial DNA supercoiling Mol. Microbiol. 6 1992 425 433
    • (1992) Mol. Microbiol. , vol.6 , pp. 425-433
    • Drlica, K.1
  • 4
    • 0033814887 scopus 로고    scopus 로고
    • The expression of the Escherichia coli fis gene is strongly dependent on the superhelical density of DNA
    • R. Schneider, A. Travers, and G. Muskhelishvili The expression of the Escherichia coli fis gene is strongly dependent on the superhelical density of DNA Mol. Microbiol. 38 2000 167 175
    • (2000) Mol. Microbiol. , vol.38 , pp. 167-175
    • Schneider, R.1    Travers, A.2    Muskhelishvili, G.3
  • 5
    • 0036953237 scopus 로고    scopus 로고
    • DNA topology-mediated control of global gene expression in Escherichia coli
    • G.W. Hatfield, and C.J. Benham DNA topology-mediated control of global gene expression in Escherichia coli Annu. Rev. Genet. 36 2002 175 203
    • (2002) Annu. Rev. Genet. , vol.36 , pp. 175-203
    • Hatfield, G.W.1    Benham, C.J.2
  • 7
    • 0023433855 scopus 로고
    • Supercoiling of the DNA template during transcription
    • L.F. Liu, and J.C. Wang Supercoiling of the DNA template during transcription Proc. Natl Acad. Sci. USA 84 1987 7024 7027
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7024-7027
    • Liu, L.F.1    Wang, J.C.2
  • 8
    • 0023790970 scopus 로고
    • Supercoiling of intracellular DNA can occur in eukaryotic cells
    • G.N. Giaever, and J.C. Wang Supercoiling of intracellular DNA can occur in eukaryotic cells Cell 55 1988 849 856
    • (1988) Cell , vol.55 , pp. 849-856
    • Giaever, G.N.1    Wang, J.C.2
  • 9
  • 10
    • 0034923502 scopus 로고    scopus 로고
    • DNA topoisomerases: Structure, function, and mechanism
    • J.J. Champoux DNA topoisomerases: structure, function, and mechanism Annu. Rev. Biochem. 70 2001 369 413
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 369-413
    • Champoux, J.J.1
  • 11
    • 0037948842 scopus 로고    scopus 로고
    • DNA relaxation by human topoisomerase I occurs in the closed clamp conformation of the protein
    • J.F. Carey, S.J. Schultz, L. Sisson, T.G. Fazzio, and J.J. Champoux DNA relaxation by human topoisomerase I occurs in the closed clamp conformation of the protein Proc. Natl Acad. Sci. U S A 100 2003 5640 5645
    • (2003) Proc. Natl Acad. Sci. U S a , vol.100 , pp. 5640-5645
    • Carey, J.F.1    Schultz, S.J.2    Sisson, L.3    Fazzio, T.G.4    Champoux, J.J.5
  • 12
    • 0023127037 scopus 로고
    • Need for DNA topoisomerase activity as a swivel for DNA replication for transcription of ribosomal RNA
    • S.J. Brill, S. DiNardo, K. Voelkel-Meiman, and R. Sternglanz Need for DNA topoisomerase activity as a swivel for DNA replication for transcription of ribosomal RNA Nature 326 1987 414 416 (Published erratum appears in Nature (1987), 326, 812).
    • (1987) Nature , vol.326 , pp. 414-416
    • Brill, S.J.1    Dinardo, S.2    Voelkel-Meiman, K.3    Sternglanz, R.4
  • 13
    • 0023958908 scopus 로고
    • Involvement of DNA topoisomerase I in transcription of human ribosomal RNA genes
    • H. Zhang, J.C. Wang, and L.F. Liu Involvement of DNA topoisomerase I in transcription of human ribosomal RNA genes Proc. Natl Acad. Sci. USA 85 1988 1060 1064
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1060-1064
    • Zhang, H.1    Wang, J.C.2    Liu, L.F.3
  • 14
    • 0026725797 scopus 로고
    • Topoisomerases and yeast rRNA transcription: Negative supercoiling stimulates initiation and topoisomerase activity is required for elongation
    • M.C. Schultz, S.J. Brill, Q. Ju, R. Sternglanz, and R.H. Reeder Topoisomerases and yeast rRNA transcription: negative supercoiling stimulates initiation and topoisomerase activity is required for elongation Genes Dev. 6 1992 1332 1341
    • (1992) Genes Dev. , vol.6 , pp. 1332-1341
    • Schultz, M.C.1    Brill, S.J.2    Ju, Q.3    Sternglanz, R.4    Reeder, R.H.5
  • 15
    • 0027186443 scopus 로고
    • DNA topoisomerase I is involved in both repression and activation of transcription
    • A. Merino, K.R. Madden, W.S. Lane, J.J. Champoux, and D. Reinberg DNA topoisomerase I is involved in both repression and activation of transcription Nature 365 1993 227 232
    • (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
  • 16
    • 0031049483 scopus 로고    scopus 로고
    • Topoisomerase I enhances TFIID-TFIIA complex assembly during activation of transcription
    • B.M. Shykind, J. Kim, L. Stewart, J.J. Champoux, and P.A. Sharp Topoisomerase I enhances TFIID-TFIIA complex assembly during activation of transcription Genes Dev. 11 1997 397 407
    • (1997) Genes Dev. , vol.11 , pp. 397-407
    • Shykind, B.M.1    Kim, J.2    Stewart, L.3    Champoux, J.J.4    Sharp, P.A.5
  • 17
    • 0030826233 scopus 로고    scopus 로고
    • A protein-mediated mechanism for the DNA sequence-specific action of topoisomerase II poisons
    • G. Capranico, M. Binaschi, M.E. Borgnetto, F. Zunino, and M. Palumbo A protein-mediated mechanism for the DNA sequence-specific action of topoisomerase II poisons Trends Pharmacol. Sci. 18 1997 323 329
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 323-329
    • Capranico, G.1    Binaschi, M.2    Borgnetto, M.E.3    Zunino, F.4    Palumbo, M.5
  • 18
    • 0032189683 scopus 로고    scopus 로고
    • Mechanism of action of eukaryotic DNA topoisomerase I and drugs targeted to the enzyme
    • Y. Pommier, P. Pourquier, Y. Fan, and D. Strumberg Mechanism of action of eukaryotic DNA topoisomerase I and drugs targeted to the enzyme Biochim. Biophys. Acta 1400 1998 83 105
    • (1998) Biochim. Biophys. Acta , vol.1400 , pp. 83-105
    • Pommier, Y.1    Pourquier, P.2    Fan, Y.3    Strumberg, D.4
  • 19
    • 0035029153 scopus 로고    scopus 로고
    • Tumor cell death induced by topoisomerase-targeting drugs
    • T.K. Li, and L.F. Liu Tumor cell death induced by topoisomerase-targeting drugs Annu. Rev. Pharmacol. Toxicol. 41 2001 53 77
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 53-77
    • Li, T.K.1    Liu, L.F.2
  • 20
    • 0035042602 scopus 로고    scopus 로고
    • Type II topoisomerases as targets for quinolone antibacterials: Turning Dr. Jekyll into Mr. Hyde
    • V.E. Anderson, and N. Osheroff Type II topoisomerases as targets for quinolone antibacterials: turning Dr. Jekyll into Mr. Hyde Curr. Pharm. Des. 7 2001 337 353
    • (2001) Curr. Pharm. Des. , vol.7 , pp. 337-353
    • Anderson, V.E.1    Osheroff, N.2
  • 22
    • 17144371295 scopus 로고    scopus 로고
    • Structures of three classes of anticancer agents bound to the human topoisomerase I-DNA covalent complex
    • B.L. Staker, M.D. Feese, M. Cushman, Y. Pommier, D. Zembower, L. Stewart, and A.B. Burgin Structures of three classes of anticancer agents bound to the human topoisomerase I-DNA covalent complex J. Med. Chem. 48 2005 2336 2345
    • (2005) J. Med. Chem. , vol.48 , pp. 2336-2345
    • Staker, B.L.1    Feese, M.D.2    Cushman, M.3    Pommier, Y.4    Zembower, D.5    Stewart, L.6    Burgin, A.B.7
  • 23
    • 0034124053 scopus 로고    scopus 로고
    • Conversion of topoisomerase I cleavage complexes on the leading strand of ribosomal DNA into 5′-phosphorylated DNA double-strand breaks by replication runoff
    • D. Strumberg, A.A. Pilon, M. Smith, R. Hickey, L. Malkas, and Y. Pommier Conversion of topoisomerase I cleavage complexes on the leading strand of ribosomal DNA into 5′-phosphorylated DNA double-strand breaks by replication runoff Mol. Cell Biol. 20 2000 3977 3987
    • (2000) Mol. Cell Biol. , vol.20 , pp. 3977-3987
    • Strumberg, D.1    Pilon, A.A.2    Smith, M.3    Hickey, R.4    Malkas, L.5    Pommier, Y.6
  • 25
  • 26
    • 0015174240 scopus 로고
    • Ribosome formation is blocked by camptothecin, a reversible inhibitor of RNA synthesis
    • R.S. Wu, A. Kumar, and R.P. Warrell Jr Ribosome formation is blocked by camptothecin, a reversible inhibitor of RNA synthesis Proc. Natl Acad. Sci. USA 68 1971 3009 3014
    • (1971) Proc. Natl Acad. Sci. USA , vol.68 , pp. 3009-3014
    • Wu, R.S.1    Kumar, A.2    Warrell Jr., R.P.3
  • 27
    • 0030658833 scopus 로고    scopus 로고
    • Processing of topoisomerase I cleavable complexes into DNA damage by transcription
    • J. Wu, and L.F. Liu Processing of topoisomerase I cleavable complexes into DNA damage by transcription Nucl. Acids Res. 25 1997 4181 4186
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4181-4186
    • Wu, J.1    Liu, L.F.2
  • 28
    • 0025335205 scopus 로고
    • Camptothecin-stabilized topoisomerase I-DNA adducts cause premature termination of transcription
    • C. Bendixen, B. Thomsen, J. Alsner, and O. Westergaard Camptothecin-stabilized topoisomerase I-DNA adducts cause premature termination of transcription Biochemistry 29 1990 5613 5619
    • (1990) Biochemistry , vol.29 , pp. 5613-5619
    • Bendixen, C.1    Thomsen, B.2    Alsner, J.3    Westergaard, O.4
  • 29
    • 0016161982 scopus 로고
    • Animal DNA-dependent RNA polymerases. 11. Mechanism of the inhibition of RNA polymerases B by amatoxins
    • M. Cochet-Meilhac, and P. Chambon Animal DNA-dependent RNA polymerases. 11. Mechanism of the inhibition of RNA polymerases B by amatoxins Biochim. Biophys. Acta 353 1974 160 184
    • (1974) Biochim. Biophys. Acta , vol.353 , pp. 160-184
    • Cochet-Meilhac, M.1    Chambon, P.2
  • 31
    • 0037022279 scopus 로고    scopus 로고
    • Structural basis of transcription: Alpha-amanitin-RNA polymerase II cocrystal at 2.8 Å resolution
    • D.A. Bushnell, P. Cramer, and R.D. Kornberg Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 Å resolution Proc. Natl Acad. Sci. USA 99 2002 1218 1222
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1218-1222
    • Bushnell, D.A.1    Cramer, P.2    Kornberg, R.D.3
  • 32
    • 3042595545 scopus 로고    scopus 로고
    • Alpha-amanitin blocks translocation by human RNA polymerase II
    • X.Q. Gong, Y.A. Nedialkov, and Z.F. Burton Alpha-amanitin blocks translocation by human RNA polymerase II J. Biol. Chem. 279 2004 27422 27427
    • (2004) J. Biol. Chem. , vol.279 , pp. 27422-27427
    • Gong, X.Q.1    Nedialkov, Y.A.2    Burton, Z.F.3
  • 35
    • 0038820065 scopus 로고    scopus 로고
    • Phosphorylation of histone H2AX and activation of Mre11, Rad50, and Nbs1 in response to replication-dependent DNA double-strand breaks induced by mammalian DNA topoisomerase I cleavage complexes
    • T. Furuta, H. Takemura, Z.Y. Liao, G.J. Aune, C. Redon, and O.A. Sedelnikova Phosphorylation of histone H2AX and activation of Mre11, Rad50, and Nbs1 in response to replication-dependent DNA double-strand breaks induced by mammalian DNA topoisomerase I cleavage complexes J. Biol. Chem. 278 2003 20303 20312
    • (2003) J. Biol. Chem. , vol.278 , pp. 20303-20312
    • Furuta, T.1    Takemura, H.2    Liao, Z.Y.3    Aune, G.J.4    Redon, C.5    Sedelnikova, O.A.6
  • 37
    • 0033860563 scopus 로고    scopus 로고
    • The FBP interacting repressor targets TFIIH to inhibit activated transcription
    • J. Liu, L. He, I. Collins, H. Ge, D. Libutti, J. Li, J.M. Egly, and D. Levens The FBP interacting repressor targets TFIIH to inhibit activated transcription Mol. Cell 5 2000 331 341
    • (2000) Mol. Cell , vol.5 , pp. 331-341
    • Liu, J.1    He, L.2    Collins, I.3    Ge, H.4    Libutti, D.5    Li, J.6    Egly, J.M.7    Levens, D.8
  • 38
    • 17744376368 scopus 로고    scopus 로고
    • Defective interplay of activators and repressors with TFIH in xeroderma pigmentosum
    • J. Liu, S. Akoulitchev, A. Weber, H. Ge, S. Chuikov, and D. Libutti Defective interplay of activators and repressors with TFIH in xeroderma pigmentosum Cell 104 2001 353 363
    • (2001) Cell , vol.104 , pp. 353-363
    • Liu, J.1    Akoulitchev, S.2    Weber, A.3    Ge, H.4    Chuikov, S.5    Libutti, D.6
  • 39
    • 11144274567 scopus 로고    scopus 로고
    • TFIIH operates through an expanded proximal promoter to fine-tune c-myc expression
    • A. Weber, J. Liu, I. Collins, and D. Levens TFIIH operates through an expanded proximal promoter to fine-tune c-myc expression Mol. Cell Biol. 25 2005 147 161
    • (2005) Mol. Cell Biol. , vol.25 , pp. 147-161
    • Weber, A.1    Liu, J.2    Collins, I.3    Levens, D.4
  • 41
    • 0033546210 scopus 로고    scopus 로고
    • The organization of replication and transcription
    • P.R. Cook The organization of replication and transcription Science 284 1999 1790 1795
    • (1999) Science , vol.284 , pp. 1790-1795
    • Cook, P.R.1
  • 43
    • 0030854371 scopus 로고    scopus 로고
    • Ubiquitin-dependent destruction of topoisomerase I is stimulated by the antitumor drug camptothecin
    • S.D. Desai, L.F. Liu, D. Vazquez-Abad, and P. D'Arpa Ubiquitin-dependent destruction of topoisomerase I is stimulated by the antitumor drug camptothecin J. Biol. Chem. 272 1997 24159 24164
    • (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
  • 44
    • 0037007036 scopus 로고    scopus 로고
    • Transcription-coupled and DNA damage-dependent ubiquitination of RNA polymerase II in vitro
    • K.-B. Lee, D. Wang, S.J. Lippard, and P.A. Sharp Transcription-coupled and DNA damage-dependent ubiquitination of RNA polymerase II in vitro Proc. Natl Acad. Sci. USA 99 2002 4239 4244
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 4239-4244
    • Lee, K.-B.1    Wang, D.2    Lippard, S.J.3    Sharp, P.A.4
  • 45
    • 10044251065 scopus 로고    scopus 로고
    • Transcription-dependent polyubiquitination of RNA polymerase II requires lysine 63 of ubiquitin
    • K.B. Lee, and P.A. Sharp Transcription-dependent polyubiquitination of RNA polymerase II requires lysine 63 of ubiquitin Biochemistry 43 2004 15223 15229
    • (2004) Biochemistry , vol.43 , pp. 15223-15229
    • Lee, K.B.1    Sharp, P.A.2
  • 47
    • 0035200324 scopus 로고    scopus 로고
    • Transcriptional consequences of topoisomerase inhibition
    • I. Collins, A. Weber, and D. Levens Transcriptional consequences of topoisomerase inhibition Mol. Cell Biol. 21 2001 8437 8451
    • (2001) Mol. Cell Biol. , vol.21 , pp. 8437-8451
    • Collins, I.1    Weber, A.2    Levens, D.3
  • 48
    • 0033522915 scopus 로고    scopus 로고
    • The transcriptional inhibitors, actinomycin D and alpha-amanitin, activate the HIV-1 promoter and favor phosphorylation of the RNA polymerase II C-terminal domain
    • C. Casse, F. Giannoni, V.T. Nguyen, M.F. Dubois, and O. Bensaude The transcriptional inhibitors, actinomycin D and alpha-amanitin, activate the HIV-1 promoter and favor phosphorylation of the RNA polymerase II C-terminal domain J. Biol. Chem. 274 1999 16097 16106
    • (1999) J. Biol. Chem. , vol.274 , pp. 16097-16106
    • Casse, C.1    Giannoni, F.2    Nguyen, V.T.3    Dubois, M.F.4    Bensaude, O.5
  • 49
    • 14644388222 scopus 로고    scopus 로고
    • The dynamics of histone H1 function in chromatin
    • M. Bustin, F. Catez, and J.H. Lim The dynamics of histone H1 function in chromatin Mol. Cell 17 2005 617 620
    • (2005) Mol. Cell , vol.17 , pp. 617-620
    • Bustin, M.1    Catez, F.2    Lim, J.H.3
  • 50
    • 0035833262 scopus 로고    scopus 로고
    • Large-scale chromatin decondensation and recondensation regulated by transcription from a natural promoter
    • W.G. Muller, D. Walker, G.L. Hager, and J.G. McNally Large-scale chromatin decondensation and recondensation regulated by transcription from a natural promoter J. Cell Biol. 154 2001 33 48
    • (2001) J. Cell Biol. , vol.154 , pp. 33-48
    • Muller, W.G.1    Walker, D.2    Hager, G.L.3    McNally, J.G.4
  • 51
    • 16544393864 scopus 로고    scopus 로고
    • Specific histone patterns and acetylase/deacetylase activity at the breakpoint-cluster region of the human MLL gene
    • A. Khobta, C. Carlo-Stella, and G. Capranico Specific histone patterns and acetylase/deacetylase activity at the breakpoint-cluster region of the human MLL gene Cancer Res. 64 2004 2656 2662
    • (2004) Cancer Res. , vol.64 , pp. 2656-2662
    • Khobta, A.1    Carlo-Stella, C.2    Capranico, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.