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Volumn 371, Issue 4, 2007, Pages 1022-1037

Histone Hyperacetylation during SV40 Transcription Is Regulated by p300 and RNA Polymerase II Translocation

Author keywords

chromatin; histone hyperacetylation; RNA polymerase II; SV40; transcription

Indexed keywords

5,6 DICHLOROBENZIMIDAZOLE RIBOSIDE; ALPHA AMANITIN; HISTONE H3; HISTONE H4; PROTEIN P300; RNA POLYMERASE II;

EID: 34547130607     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.06.080     Document Type: Article
Times cited : (15)

References (62)
  • 2
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner M., and Jenuwein T. The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14 (2002) 286-298
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 3
    • 0029925512 scopus 로고    scopus 로고
    • Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation
    • Brownell J.E., and Allis C.D. Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation. Curr. Opin. Genet. Dev. 6 (1996) 176-184
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 176-184
    • Brownell, J.E.1    Allis, C.D.2
  • 4
    • 33751423622 scopus 로고    scopus 로고
    • Histone hyperacetylation in the coding region of chromatin undergoing transcription in SV40 minichromosomes is a dynamic process regulated directly by the presence of RNA polymerase II
    • Balakrishnan L., and Milavetz B. Histone hyperacetylation in the coding region of chromatin undergoing transcription in SV40 minichromosomes is a dynamic process regulated directly by the presence of RNA polymerase II. J. Mol. Biol. 365 (2007) 18-30
    • (2007) J. Mol. Biol. , vol.365 , pp. 18-30
    • Balakrishnan, L.1    Milavetz, B.2
  • 5
    • 0030017431 scopus 로고    scopus 로고
    • RNA polymerase II inhibitor, 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB) causes erythroleukemic differentiation and transcriptional activation of erythroid genes
    • Hensold J.O., Barth D., and Stratton C.A. RNA polymerase II inhibitor, 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB) causes erythroleukemic differentiation and transcriptional activation of erythroid genes. J. Cell Physiol. 168 (1996) 105-113
    • (1996) J. Cell Physiol. , vol.168 , pp. 105-113
    • Hensold, J.O.1    Barth, D.2    Stratton, C.A.3
  • 6
    • 0014959969 scopus 로고
    • Specific inhibition of nuclear RNA polymerase II by alpha-amanitin
    • Lindell T.J., Weinberg F., Morris P.W., Roeder R.G., and Rutter W.J. Specific inhibition of nuclear RNA polymerase II by alpha-amanitin. Science 170 (1970) 447-449
    • (1970) Science , vol.170 , pp. 447-449
    • Lindell, T.J.1    Weinberg, F.2    Morris, P.W.3    Roeder, R.G.4    Rutter, W.J.5
  • 8
    • 0029816105 scopus 로고    scopus 로고
    • Amanitin greatly reduces the rate of transcription by RNA olymerase II ternary complexes but fails to inhibit some transcript cleavage modes
    • Rudd M.D., and Luse D.S. Amanitin greatly reduces the rate of transcription by RNA olymerase II ternary complexes but fails to inhibit some transcript cleavage modes. J. Biol. Chem. 271 (1996) 21549-21558
    • (1996) J. Biol. Chem. , vol.271 , pp. 21549-21558
    • Rudd, M.D.1    Luse, D.S.2
  • 9
    • 0028978695 scopus 로고
    • Action of alpha-amanitin during pyrophosphorolysis and elongation by RNA polymerase II
    • Chafin D.R., Guo H., and Price D.H. Action of alpha-amanitin during pyrophosphorolysis and elongation by RNA polymerase II. J. Biol. Chem. 270 (1995) 19114-19119
    • (1995) J. Biol. Chem. , vol.270 , pp. 19114-19119
    • Chafin, D.R.1    Guo, H.2    Price, D.H.3
  • 10
    • 0037073061 scopus 로고    scopus 로고
    • Regulation of transcription elongation by phosphorylation
    • Kobor M.S., and Greenblatt J. Regulation of transcription elongation by phosphorylation. Biochim. Biophys. Acta 1577 (2002) 261-275
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 261-275
    • Kobor, M.S.1    Greenblatt, J.2
  • 11
    • 0029760928 scopus 로고    scopus 로고
    • Reversible phosphorylation of the C-terminal domain of RNA polymerase II
    • Dahmus M.E. Reversible phosphorylation of the C-terminal domain of RNA polymerase II. J. Biol. Chem. 271 (1996) 19009-19012
    • (1996) J. Biol. Chem. , vol.271 , pp. 19009-19012
    • Dahmus, M.E.1
  • 12
    • 0033678601 scopus 로고    scopus 로고
    • Phosphorylation in transcription: the CTD and more
    • Riedl T., and Egly J.M. Phosphorylation in transcription: the CTD and more. Gene Expr. 9 (2000) 3-13
    • (2000) Gene Expr. , vol.9 , pp. 3-13
    • Riedl, T.1    Egly, J.M.2
  • 13
    • 0036136668 scopus 로고    scopus 로고
    • Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control
    • Oelgeschlager T. Regulation of RNA polymerase II activity by CTD phosphorylation and cell cycle control. J. Cell Physiol. 190 (2002) 160-169
    • (2002) J. Cell Physiol. , vol.190 , pp. 160-169
    • Oelgeschlager, T.1
  • 14
    • 0032549653 scopus 로고    scopus 로고
    • Characterization of the residues phosphorylated in vitro by different C-terminal domain kinases
    • Trigon S., Serizawa H., Conaway J.W., Conaway R.C., Jackson S.P., and Morange M. Characterization of the residues phosphorylated in vitro by different C-terminal domain kinases. J. Biol. Chem. 273 (1998) 6769-6775
    • (1998) J. Biol. Chem. , vol.273 , pp. 6769-6775
    • Trigon, S.1    Serizawa, H.2    Conaway, J.W.3    Conaway, R.C.4    Jackson, S.P.5    Morange, M.6
  • 15
    • 0034111019 scopus 로고    scopus 로고
    • P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II
    • Price D.H. P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II. Mol. Cell. Biol. 20 (2000) 2629-2634
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2629-2634
    • Price, D.H.1
  • 16
    • 3242769187 scopus 로고    scopus 로고
    • Cellular control of gene expression by T-type cyclin/CDK9 complexes
    • Garriga J.G.X. Cellular control of gene expression by T-type cyclin/CDK9 complexes. Gene 337 (2004) 15-23
    • (2004) Gene , vol.337 , pp. 15-23
    • Garriga, J.G.X.1
  • 17
    • 0037450637 scopus 로고    scopus 로고
    • The C-terminal domain of pol II and a DRB-sensitive kinase are required for 3′ processing of U2 snRNA
    • Medlin J.E., Uguen P., Taylor A., Bentley D.L., and Murphy S. The C-terminal domain of pol II and a DRB-sensitive kinase are required for 3′ processing of U2 snRNA. EMBO J. 22 (2003) 925-934
    • (2003) EMBO J. , vol.22 , pp. 925-934
    • Medlin, J.E.1    Uguen, P.2    Taylor, A.3    Bentley, D.L.4    Murphy, S.5
  • 18
    • 30844441204 scopus 로고    scopus 로고
    • Reorganization of RNA polymerase II on the SV40 genome occurs coordinately with the early to late transcriptional switch
    • Balakrishnan L., and Milavetz B. Reorganization of RNA polymerase II on the SV40 genome occurs coordinately with the early to late transcriptional switch. Virology 345 (2006) 31-43
    • (2006) Virology , vol.345 , pp. 31-43
    • Balakrishnan, L.1    Milavetz, B.2
  • 19
    • 14644400380 scopus 로고    scopus 로고
    • Programmed remodeling of hyperacetylated histone H4 and H3 organization on the SV40 genome during lytic infection
    • Balakrishnan L., and Milavetz B. Programmed remodeling of hyperacetylated histone H4 and H3 organization on the SV40 genome during lytic infection. Virology 334 (2005) 111-123
    • (2005) Virology , vol.334 , pp. 111-123
    • Balakrishnan, L.1    Milavetz, B.2
  • 20
    • 1342279567 scopus 로고    scopus 로고
    • Hyperacetylation and differential deacetylation of histones H4 and H3 define two distinct classes of acetylated SV40 chromosomes early in infection
    • Milavetz B. Hyperacetylation and differential deacetylation of histones H4 and H3 define two distinct classes of acetylated SV40 chromosomes early in infection. Virology 319 (2004) 324-336
    • (2004) Virology , vol.319 , pp. 324-336
    • Milavetz, B.1
  • 21
    • 0027364860 scopus 로고
    • RNA polymerase locations in the simian virus 40 transcription complex
    • Eadara J.K., and Lutter L.C. RNA polymerase locations in the simian virus 40 transcription complex. J. Biol. Chem. 268 (1993) 22020-22027
    • (1993) J. Biol. Chem. , vol.268 , pp. 22020-22027
    • Eadara, J.K.1    Lutter, L.C.2
  • 22
    • 0023785164 scopus 로고
    • The separation of transcriptionally engaged genes
    • Ip Y.T., Jackson V., Meier J., and Chalkley R. The separation of transcriptionally engaged genes. J. Biol. Chem. 263 (1988) 14044-14052
    • (1988) J. Biol. Chem. , vol.263 , pp. 14044-14052
    • Ip, Y.T.1    Jackson, V.2    Meier, J.3    Chalkley, R.4
  • 23
    • 33746457753 scopus 로고    scopus 로고
    • Enhanced histone acetylation and transcription: a dynamic perspective
    • Clayton A.L., Hazzalin C.A., and Mahadevan L.C. Enhanced histone acetylation and transcription: a dynamic perspective. Mol. Cell 23 (2006) 289-296
    • (2006) Mol. Cell , vol.23 , pp. 289-296
    • Clayton, A.L.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 24
    • 33646926758 scopus 로고    scopus 로고
    • Dynamic nucleosomes and gene transcription
    • Mellor J. Dynamic nucleosomes and gene transcription. Trends Genet. 22 (2006) 320-329
    • (2006) Trends Genet. , vol.22 , pp. 320-329
    • Mellor, J.1
  • 25
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier R., Penot G., Hubner M.R., Reid G., Brand H., Kos M., and Gannon F. Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115 (2003) 751-763
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 26
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling
    • Reid G., Hubner M.R., Metivier R., Brand H., Denger S., Manu D., et al. Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling. Mol. Cell 11 (2003) 695-707
    • (2003) Mol. Cell , vol.11 , pp. 695-707
    • Reid, G.1    Hubner, M.R.2    Metivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6
  • 27
    • 33947516620 scopus 로고    scopus 로고
    • The rate of c-fos transcription in vivo is continously regulated at the level of elongation by dynamic stimulus-coupled recruitment of P-TEFb
    • Ryser S., Fujita T., Tortola S., Piuz I., and Schlegel W. The rate of c-fos transcription in vivo is continously regulated at the level of elongation by dynamic stimulus-coupled recruitment of P-TEFb. J. Biol. Chem. 282 (2007) 5075-5084
    • (2007) J. Biol. Chem. , vol.282 , pp. 5075-5084
    • Ryser, S.1    Fujita, T.2    Tortola, S.3    Piuz, I.4    Schlegel, W.5
  • 28
    • 15244358670 scopus 로고    scopus 로고
    • Distinction and relationship between elongation rate and processivity of RNA polymerase II in vivo
    • Mason P.B., and Struhl K. Distinction and relationship between elongation rate and processivity of RNA polymerase II in vivo. Mol. Cell 17 (2005) 831-840
    • (2005) Mol. Cell , vol.17 , pp. 831-840
    • Mason, P.B.1    Struhl, K.2
  • 29
    • 27744577727 scopus 로고    scopus 로고
    • Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription
    • Carrozza M.J., Li B., Florens L., Suganuma T., Swanson S.K., Lee K.K., et al. Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. Cell 123 (2005) 581-592
    • (2005) Cell , vol.123 , pp. 581-592
    • Carrozza, M.J.1    Li, B.2    Florens, L.3    Suganuma, T.4    Swanson, S.K.5    Lee, K.K.6
  • 30
    • 16244366803 scopus 로고    scopus 로고
    • Class II histone deacetylases: from sequence to function, regulation, and clinical implication
    • Yang X.J., and Gregoire S. Class II histone deacetylases: from sequence to function, regulation, and clinical implication. Mol. Cell. Biol. 25 (2005) 2873-2884
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2873-2884
    • Yang, X.J.1    Gregoire, S.2
  • 31
    • 20844451181 scopus 로고    scopus 로고
    • Transcriptional complexes engaged by apo-estrogen receptor-alpha isoforms have divergent outcomes
    • Metivier R.P.G., Carmouche R.P., Hubner M.R., Reid G., Denger S., Manu D., et al. Transcriptional complexes engaged by apo-estrogen receptor-alpha isoforms have divergent outcomes. EMBO J. 23 (2004) 3653-3666
    • (2004) EMBO J. , vol.23 , pp. 3653-3666
    • Metivier, R.P.G.1    Carmouche, R.P.2    Hubner, M.R.3    Reid, G.4    Denger, S.5    Manu, D.6
  • 32
    • 33645502548 scopus 로고    scopus 로고
    • Histone deacetylase 3 binds to and regulates the GCMa transcription factor
    • Chuang H.C., Chang C.W., Chang G.D., Yao T.P., and Chen H. Histone deacetylase 3 binds to and regulates the GCMa transcription factor. Nucl. Acids Res. 34 (2006) 1459-1469
    • (2006) Nucl. Acids Res. , vol.34 , pp. 1459-1469
    • Chuang, H.C.1    Chang, C.W.2    Chang, G.D.3    Yao, T.P.4    Chen, H.5
  • 33
    • 0037126388 scopus 로고    scopus 로고
    • The interaction of HTLV-1 Tax with HDAC1 negatively regulates the viral gene expression
    • Ego T., Ariumi Y., and Shimotohno K. The interaction of HTLV-1 Tax with HDAC1 negatively regulates the viral gene expression. Oncogene 21 (2002) 7241-7246
    • (2002) Oncogene , vol.21 , pp. 7241-7246
    • Ego, T.1    Ariumi, Y.2    Shimotohno, K.3
  • 34
    • 33744522801 scopus 로고    scopus 로고
    • Histone deacetylase 3 (HDAC3) is recruited to target promoters by PML-RARalpha as a component of the N-CoR co-repressor complex to repress transcription in vivo
    • Atsumi A.T.A., Kiyoi H., and Naoe T. Histone deacetylase 3 (HDAC3) is recruited to target promoters by PML-RARalpha as a component of the N-CoR co-repressor complex to repress transcription in vivo. Biochem. Biophys. Res. Commun. 345 (2006) 1471-1480
    • (2006) Biochem. Biophys. Res. Commun. , vol.345 , pp. 1471-1480
    • Atsumi, A.T.A.1    Kiyoi, H.2    Naoe, T.3
  • 35
    • 30044441988 scopus 로고    scopus 로고
    • The human SWI/SNF subunit Brm is a regulator of alternative splicing
    • Batsche E.Y.M., and Muchardt C. The human SWI/SNF subunit Brm is a regulator of alternative splicing. Nature Struct. Mol. Biol. 13 (2006) 22-29
    • (2006) Nature Struct. Mol. Biol. , vol.13 , pp. 22-29
    • Batsche, E.Y.M.1    Muchardt, C.2
  • 36
    • 1542328270 scopus 로고    scopus 로고
    • Transcriptional elongation control by RNA polymerase II: a new frontier
    • Shilatifard A. Transcriptional elongation control by RNA polymerase II: a new frontier. Biochim. Biophys. Acta 1677 (2004) 79-86
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 79-86
    • Shilatifard, A.1
  • 38
    • 0030033699 scopus 로고    scopus 로고
    • RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodeling
    • Wilson C.J., Chao D.M., Imbalzano A.N., Schnitzler G.R., Kingston R.E., and Young R.A. RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodeling. Cell 84 (1996) 235-244
    • (1996) Cell , vol.84 , pp. 235-244
    • Wilson, C.J.1    Chao, D.M.2    Imbalzano, A.N.3    Schnitzler, G.R.4    Kingston, R.E.5    Young, R.A.6
  • 40
    • 29144468972 scopus 로고    scopus 로고
    • Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to Pol II elongation
    • Joshi A.A., and Struhl K. Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to Pol II elongation. Mol. Cell 20 (2005) 971-978
    • (2005) Mol. Cell , vol.20 , pp. 971-978
    • Joshi, A.A.1    Struhl, K.2
  • 41
    • 27744587302 scopus 로고    scopus 로고
    • Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex
    • Keogh M.C., Kurdistani S.K., Morris S.A., Ahn S.H., Podolny V., Collins S.R., et al. Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex. Cell 123 (2005) 593-605
    • (2005) Cell , vol.123 , pp. 593-605
    • Keogh, M.C.1    Kurdistani, S.K.2    Morris, S.A.3    Ahn, S.H.4    Podolny, V.5    Collins, S.R.6
  • 43
    • 0033635222 scopus 로고    scopus 로고
    • Activator-dependent transcription from chromatin in vitro involving targeted histone acetylation by p300
    • Kundu T.K., Palhan V.B., Wang Z., An W., Cole P.A., and Roeder R.G. Activator-dependent transcription from chromatin in vitro involving targeted histone acetylation by p300. Mol. Cell 6 (2000) 551-561
    • (2000) Mol. Cell , vol.6 , pp. 551-561
    • Kundu, T.K.1    Palhan, V.B.2    Wang, Z.3    An, W.4    Cole, P.A.5    Roeder, R.G.6
  • 44
    • 25444462807 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional gene regulation of HTLV-1
    • Kashanchi F., and Brady J.N. Transcriptional and post-transcriptional gene regulation of HTLV-1. Oncogene 24 (2005) 5938-5951
    • (2005) Oncogene , vol.24 , pp. 5938-5951
    • Kashanchi, F.1    Brady, J.N.2
  • 45
    • 33745294741 scopus 로고    scopus 로고
    • p300/Cyclic AMP-responsive element binding-binding protein mediates transcriptional coactivation by the CD28 T cell costimulatory receptor
    • Nandiwada S.L., Li W., Zhang R., and Mueller D.L. p300/Cyclic AMP-responsive element binding-binding protein mediates transcriptional coactivation by the CD28 T cell costimulatory receptor. J. Immunol. 177 (2006) 401-413
    • (2006) J. Immunol. , vol.177 , pp. 401-413
    • Nandiwada, S.L.1    Li, W.2    Zhang, R.3    Mueller, D.L.4
  • 46
    • 33751232378 scopus 로고    scopus 로고
    • Functional analysis of CBP/p300 in embryonic orofacial mesenchymal cells
    • Warner D.R., Pisano M.M., and Greene R.M. Functional analysis of CBP/p300 in embryonic orofacial mesenchymal cells. J. Cell Biochem. 99 (2006) 1374-1379
    • (2006) J. Cell Biochem. , vol.99 , pp. 1374-1379
    • Warner, D.R.1    Pisano, M.M.2    Greene, R.M.3
  • 47
    • 33748415010 scopus 로고    scopus 로고
    • A mechanism for coordinating chromatin modification and preinitiation complex assembly
    • Black J.C., Choi J.E., Lombardo S.R., and Carey M. A mechanism for coordinating chromatin modification and preinitiation complex assembly. Mol. Cell 23 (2006) 809-818
    • (2006) Mol. Cell , vol.23 , pp. 809-818
    • Black, J.C.1    Choi, J.E.2    Lombardo, S.R.3    Carey, M.4
  • 48
    • 0036275233 scopus 로고    scopus 로고
    • Acetylation of nucleosomal histones by p300 facilitates transcription from tax-responsive human T-cell leukemia virus type 1 chromatin template
    • Lu H., Pise-Masison C.A., Fletcher T.M., Schiltz R.L., Nagaich A.K., Radonovich M., et al. Acetylation of nucleosomal histones by p300 facilitates transcription from tax-responsive human T-cell leukemia virus type 1 chromatin template. Mol. Cell. Biol. 22 (2002) 4450-4462
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4450-4462
    • Lu, H.1    Pise-Masison, C.A.2    Fletcher, T.M.3    Schiltz, R.L.4    Nagaich, A.K.5    Radonovich, M.6
  • 49
    • 33646066806 scopus 로고    scopus 로고
    • Synergistic functions of SII and p300 in productive activator-dependent transcription of chromatin templates
    • Guermah M., Palhan V.B., Tackett A.J., Chait B.T., and Roeder R.G. Synergistic functions of SII and p300 in productive activator-dependent transcription of chromatin templates. Cell 125 (2006) 275-286
    • (2006) Cell , vol.125 , pp. 275-286
    • Guermah, M.1    Palhan, V.B.2    Tackett, A.J.3    Chait, B.T.4    Roeder, R.G.5
  • 50
    • 1542379618 scopus 로고    scopus 로고
    • A novel hydrogen peroxide-induced phosphorylation and ubiquitination pathway leading to RNA polymerase II proteolysis
    • Inukai N., Yamaguchi Y., Kuraoka I., Yamada T., Kamijo S., Kato J., et al. A novel hydrogen peroxide-induced phosphorylation and ubiquitination pathway leading to RNA polymerase II proteolysis. J. Biol. Chem. 279 (2004) 8190-8195
    • (2004) J. Biol. Chem. , vol.279 , pp. 8190-8195
    • Inukai, N.1    Yamaguchi, Y.2    Kuraoka, I.3    Yamada, T.4    Kamijo, S.5    Kato, J.6
  • 52
    • 13444292904 scopus 로고    scopus 로고
    • Histone modifications defining active genes persist after transcriptional and mitotic inactivation
    • Kouskouti A., and Talianidis I. Histone modifications defining active genes persist after transcriptional and mitotic inactivation. EMBO J. 24 (2005) 347-357
    • (2005) EMBO J. , vol.24 , pp. 347-357
    • Kouskouti, A.1    Talianidis, I.2
  • 53
    • 33644772382 scopus 로고    scopus 로고
    • Early effects of topoisomerase I inhibition on RNA polymerase II along transcribed genes in human cells
    • Khobta A., Ferri F., Lotito L., Montecucco A., Rossi R., and Capranico G. Early effects of topoisomerase I inhibition on RNA polymerase II along transcribed genes in human cells. J. Mol. Biol. 357 (2006) 127-138
    • (2006) J. Mol. Biol. , vol.357 , pp. 127-138
    • Khobta, A.1    Ferri, F.2    Lotito, L.3    Montecucco, A.4    Rossi, R.5    Capranico, G.6
  • 54
    • 0028242341 scopus 로고
    • Inhibitors of transcription such as 5,6-dichloro-1-beta-d-ribofuranosylbenzimidazole and isoquinoline sulfonamide derivatives (H-8 and H-7) promote dephosphorylation of the carboxyl-terminal domain of RNA polymerase II largest subunit
    • Dubois M.F., Nguyen V.T., Bellier S., and Bensaude O. Inhibitors of transcription such as 5,6-dichloro-1-beta-d-ribofuranosylbenzimidazole and isoquinoline sulfonamide derivatives (H-8 and H-7) promote dephosphorylation of the carboxyl-terminal domain of RNA polymerase II largest subunit. J. Biol. Chem. 269 (1994) 13331-13336
    • (1994) J. Biol. Chem. , vol.269 , pp. 13331-13336
    • Dubois, M.F.1    Nguyen, V.T.2    Bellier, S.3    Bensaude, O.4
  • 55
    • 0024598915 scopus 로고
    • 5,6-Dichloro-1-beta-d-ribofuranosylbenzimidazole inhibits a HeLa protein kinase that phosphorylates an RNA polymerase II-derived peptide
    • Stevens A.M.M. 5,6-Dichloro-1-beta-d-ribofuranosylbenzimidazole inhibits a HeLa protein kinase that phosphorylates an RNA polymerase II-derived peptide. Biochem. Biophys. Res. Commun. 159 (1989) 508-515
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 508-515
    • Stevens, A.M.M.1
  • 56
    • 0027452694 scopus 로고
    • Partial purification and characterization of two distinct protein kinases that differentially phosphorylate the carboxyl-terminal domain of RNA polymerase subunit IIa
    • Payne J.M., and Dahmus M.E. Partial purification and characterization of two distinct protein kinases that differentially phosphorylate the carboxyl-terminal domain of RNA polymerase subunit IIa. J. Biol. Chem. 268 (1993) 80-87
    • (1993) J. Biol. Chem. , vol.268 , pp. 80-87
    • Payne, J.M.1    Dahmus, M.E.2
  • 57
    • 0024470273 scopus 로고
    • Generation of a nucleosome-free promoter region in SV40 does not require T-antigen binding to site I
    • Kube D., and Milavetz B. Generation of a nucleosome-free promoter region in SV40 does not require T-antigen binding to site I. Virology 172 (1989) 100-105
    • (1989) Virology , vol.172 , pp. 100-105
    • Kube, D.1    Milavetz, B.2
  • 58
    • 0029903013 scopus 로고    scopus 로고
    • Identification of Simian virus 40 promoter DNA sequences capable of conferring restriction endonuclease hypersensitivity
    • Hermansen R., Sierra M.A., Johnson J., Friez M., and Milavetz B. Identification of Simian virus 40 promoter DNA sequences capable of conferring restriction endonuclease hypersensitivity. J. Virol. 70 (1996) 3416-3422
    • (1996) J. Virol. , vol.70 , pp. 3416-3422
    • Hermansen, R.1    Sierra, M.A.2    Johnson, J.3    Friez, M.4    Milavetz, B.5
  • 59
    • 0033045988 scopus 로고    scopus 로고
    • Chromatin structure of the simian virus 40 late promoter: a deletional analysis
    • Friez M., Hermansen R., and Milavetz B. Chromatin structure of the simian virus 40 late promoter: a deletional analysis. J. Virol. 73 (1999) 1990-1997
    • (1999) J. Virol. , vol.73 , pp. 1990-1997
    • Friez, M.1    Hermansen, R.2    Milavetz, B.3
  • 60
  • 61
    • 0030722098 scopus 로고    scopus 로고
    • Self-assembly and protein-protein interactions between the SV40 capsid proteins produced in insect cells
    • Sandalon Z.O.A. Self-assembly and protein-protein interactions between the SV40 capsid proteins produced in insect cells. Virology 237 (1997) 414-421
    • (1997) Virology , vol.237 , pp. 414-421
    • Sandalon, Z.O.A.1
  • 62
    • 0036061538 scopus 로고    scopus 로고
    • SP1 and AP-1 elements direct chromatin remodeling in SV40 chromosomes during the first 6 hours of infection
    • Milavetz B.I. SP1 and AP-1 elements direct chromatin remodeling in SV40 chromosomes during the first 6 hours of infection. Virology 294 (2002) 170-179
    • (2002) Virology , vol.294 , pp. 170-179
    • Milavetz, B.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.