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Volumn 388, Issue 4, 2009, Pages 730-750

PARP-1 Expression in the Mouse is Controlled by an Autoregulatory Loop: PARP-1 Binding to an Upstream S/MAR Element and to a Novel Recognition Motif in its Promoter Suppresses Transcription

Author keywords

auto regulation; nuclear architecture; PARP 1; PARP recognition sites; S MAR

Indexed keywords

MATRIX ATTACHMENT REGION BINDING PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; SCAFFOLD MATRIX ATTACHMENT REGION BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 67349093825     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.03.032     Document Type: Article
Times cited : (20)

References (74)
  • 2
    • 67349229964 scopus 로고    scopus 로고
    • DNA break repair: refined rules of an already complicated game
    • Vidaković M., Poznanović G., and Bode J. DNA break repair: refined rules of an already complicated game. Biochem. Cell Biol. 96 (2005) 555-568
    • (2005) Biochem. Cell Biol. , vol.96 , pp. 555-568
    • Vidaković, M.1    Poznanović, G.2    Bode, J.3
  • 3
    • 49049084124 scopus 로고    scopus 로고
    • Scaffold/matrix attachment regions (S/MARs), relevance for disease and therapy
    • Klussmann E., and Scott J.D. (Eds), Springer, New York, NY
    • Gluch A., Vidaković M., and Bode J. Scaffold/matrix attachment regions (S/MARs), relevance for disease and therapy. In: Klussmann E., and Scott J.D. (Eds). Handbook of Experimental Pharmacology (2008), Springer, New York, NY 67-103
    • (2008) Handbook of Experimental Pharmacology , pp. 67-103
    • Gluch, A.1    Vidaković, M.2    Bode, J.3
  • 4
    • 0029087179 scopus 로고
    • Regulation of the human poly(ADP-ribosyl) transferase promoter via alternative DNA racket structures
    • Schweiger M., Oei S.L., Herzog H., Menardi C., Schneider R., Auer B., and Hirsch-Kauffmann M. Regulation of the human poly(ADP-ribosyl) transferase promoter via alternative DNA racket structures. Biochimie 77 (1995) 480-485
    • (1995) Biochimie , vol.77 , pp. 480-485
    • Schweiger, M.1    Oei, S.L.2    Herzog, H.3    Menardi, C.4    Schneider, R.5    Auer, B.6    Hirsch-Kauffmann, M.7
  • 7
    • 0026605619 scopus 로고
    • Structural analysis of the putative regulatory region of the rat gene encoding poly(ADP-ribose) polymerase
    • Potvin F., Thibodeau J., Kirkland J.B., Dandenault B., Duchaine C., and Poirier G.G. Structural analysis of the putative regulatory region of the rat gene encoding poly(ADP-ribose) polymerase. FEBS Lett. 302 (1992) 269-273
    • (1992) FEBS Lett. , vol.302 , pp. 269-273
    • Potvin, F.1    Thibodeau, J.2    Kirkland, J.B.3    Dandenault, B.4    Duchaine, C.5    Poirier, G.G.6
  • 8
    • 0033521029 scopus 로고    scopus 로고
    • Transcriptional down-regulation of poly(ADPribose)polymerase gene expression by E1A binding to pRb proteins protects murine keratinocytes from radiation induced apoptosis
    • Pacini A., Quattrone A., Denegri M., Fiorillo C., Nediani C., Ramon Y., et al. Transcriptional down-regulation of poly(ADPribose)polymerase gene expression by E1A binding to pRb proteins protects murine keratinocytes from radiation induced apoptosis. J. Biol. Chem. 274 (1999) 35107-35112
    • (1999) J. Biol. Chem. , vol.274 , pp. 35107-35112
    • Pacini, A.1    Quattrone, A.2    Denegri, M.3    Fiorillo, C.4    Nediani, C.5    Ramon, Y.6
  • 9
    • 0027275493 scopus 로고
    • The US-1 element from the gene encoding rat poly(ADP-ribose) polymerase binds the transcription factor Sp1
    • Potvin F., Roy R.J., Poirier G.G., and Guerin S.L. The US-1 element from the gene encoding rat poly(ADP-ribose) polymerase binds the transcription factor Sp1. Eur. J. Biochem. 215 (1993) 73-80
    • (1993) Eur. J. Biochem. , vol.215 , pp. 73-80
    • Potvin, F.1    Roy, R.J.2    Poirier, G.G.3    Guerin, S.L.4
  • 11
    • 0031298187 scopus 로고    scopus 로고
    • A nuclear factor other than Sp1 binds the GC-rich promoter of the gene encoding rat poly(ADP-ribose) polymerase in vitro
    • Laniel M.A., Bergeron M.J., Poirier G.G., and Guerin S.L. A nuclear factor other than Sp1 binds the GC-rich promoter of the gene encoding rat poly(ADP-ribose) polymerase in vitro. Biochem. Cell Biol. 75 (1997) 427-434
    • (1997) Biochem. Cell Biol. , vol.75 , pp. 427-434
    • Laniel, M.A.1    Bergeron, M.J.2    Poirier, G.G.3    Guerin, S.L.4
  • 13
    • 0033536186 scopus 로고    scopus 로고
    • Regulation of the human poly(ADP-ribose) polymerase promoter by the ETS transcription factor
    • Soldatenkov V.A., Albor A., Patel B.K.R., Dreszer R., Dritschilo A., and Notario V. Regulation of the human poly(ADP-ribose) polymerase promoter by the ETS transcription factor. Oncogene 18 (1999) 3954-3962
    • (1999) Oncogene , vol.18 , pp. 3954-3962
    • Soldatenkov, V.A.1    Albor, A.2    Patel, B.K.R.3    Dreszer, R.4    Dritschilo, A.5    Notario, V.6
  • 14
    • 0034119514 scopus 로고    scopus 로고
    • Caught in the act, binding of Ku and PARP to MARs reveals novel aspects of their functional interaction
    • Galande S., and Kohwi-Shigematsu T. Caught in the act, binding of Ku and PARP to MARs reveals novel aspects of their functional interaction. Crit. Rev. Eukaryot. Gene Expr. 10 (2000) 63-72
    • (2000) Crit. Rev. Eukaryot. Gene Expr. , vol.10 , pp. 63-72
    • Galande, S.1    Kohwi-Shigematsu, T.2
  • 15
    • 0038682011 scopus 로고    scopus 로고
    • PARP goes transcription
    • Kraus W.L., and Lis J.T. PARP goes transcription. Cell 113 (2003) 677-683
    • (2003) Cell , vol.113 , pp. 677-683
    • Kraus, W.L.1    Lis, J.T.2
  • 16
    • 33646507893 scopus 로고    scopus 로고
    • Correlations between scaffold/matrix attachment region (S/MAR) binding activity and DNA duplex destabilization energy
    • Bode J., Winkelmann S., Goetze S., Spiker S., Tsutsui K., Bi C., Ak P., and Benham C.J. Correlations between scaffold/matrix attachment region (S/MAR) binding activity and DNA duplex destabilization energy. J. Mol. Biol. 358 (2006) 597-613
    • (2006) J. Mol. Biol. , vol.358 , pp. 597-613
    • Bode, J.1    Winkelmann, S.2    Goetze, S.3    Spiker, S.4    Tsutsui, K.5    Bi, C.6    Ak, P.7    Benham, C.J.8
  • 18
    • 37849007576 scopus 로고    scopus 로고
    • Regulation of poly(ADP-ribose) polymerase-1 (PARP-1) gene expression through the post-translational modification of Sp1, a nuclear target protein of PARP-1
    • Zaniolo K., Desnoyers S., Leclerc S., and Guérin S.L. Regulation of poly(ADP-ribose) polymerase-1 (PARP-1) gene expression through the post-translational modification of Sp1, a nuclear target protein of PARP-1. BMC Mol. Biol. 8 (2007) 96-102
    • (2007) BMC Mol. Biol. , vol.8 , pp. 96-102
    • Zaniolo, K.1    Desnoyers, S.2    Leclerc, S.3    Guérin, S.L.4
  • 19
    • 0036710459 scopus 로고    scopus 로고
    • The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-kappaB in inflammatory disorders
    • Hassa P.O., and Hottiger M.O. The functional role of poly(ADP-ribose)polymerase 1 as novel coactivator of NF-kappaB in inflammatory disorders. Cell Mol. Life Sci. 59 (2002) 1534-1553
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 1534-1553
    • Hassa, P.O.1    Hottiger, M.O.2
  • 20
    • 0031007707 scopus 로고    scopus 로고
    • TFIIF, a basal eukaryotic transcription factor, is a substrate for poly(ADP-ribosyl)ation
    • Rawling J.M., and Alvarez-Gonzalez R. TFIIF, a basal eukaryotic transcription factor, is a substrate for poly(ADP-ribosyl)ation. Biochem. J. 324 (1997) 249-253
    • (1997) Biochem. J. , vol.324 , pp. 249-253
    • Rawling, J.M.1    Alvarez-Gonzalez, R.2
  • 21
    • 0032489545 scopus 로고    scopus 로고
    • Interaction of Oct-1 and automodification domain of poly(ADP-ribose) synthetase
    • Nie J., Sakamoto S., Song D., Qu Z., Ota K., and Taniguchi T. Interaction of Oct-1 and automodification domain of poly(ADP-ribose) synthetase. FEBS Lett. 424 (1998) 27-32
    • (1998) FEBS Lett. , vol.424 , pp. 27-32
    • Nie, J.1    Sakamoto, S.2    Song, D.3    Qu, Z.4    Ota, K.5    Taniguchi, T.6
  • 22
    • 0034615948 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a B-MYB coactivator
    • Cervellera M.N., and Sala A. Poly(ADP-ribose) polymerase is a B-MYB coactivator. J. Biol. Chem. 275 (2000) 10692-10696
    • (2000) J. Biol. Chem. , vol.275 , pp. 10692-10696
    • Cervellera, M.N.1    Sala, A.2
  • 23
    • 0037442006 scopus 로고    scopus 로고
    • Poly(ADP-Ribose) Polymerase-1 Regulates Activation of Activator Protein-1 in Murine Fibroblasts
    • Andreone T.L., O'Connor M., Denenberg A., Hake P.W., and Zingarelli B. Poly(ADP-Ribose) Polymerase-1 Regulates Activation of Activator Protein-1 in Murine Fibroblasts. J. Immunol. 170 (2003) 2113-2120
    • (2003) J. Immunol. , vol.170 , pp. 2113-2120
    • Andreone, T.L.1    O'Connor, M.2    Denenberg, A.3    Hake, P.W.4    Zingarelli, B.5
  • 24
    • 20644432426 scopus 로고    scopus 로고
    • Regulation of RNA polymerase II-dependent transcription by poly(ADP-ribosyl)ation of transcription factors
    • Oei S.L., Griesenbeck J., Schweiger M., and Ziegler M. Regulation of RNA polymerase II-dependent transcription by poly(ADP-ribosyl)ation of transcription factors. J. Biol. Chem. 273 (1998) 31644-31647
    • (1998) J. Biol. Chem. , vol.273 , pp. 31644-31647
    • Oei, S.L.1    Griesenbeck, J.2    Schweiger, M.3    Ziegler, M.4
  • 25
    • 4344625329 scopus 로고    scopus 로고
    • Dual regulation of AP-2alpha transcriptional activation by poly(ADP-ribose) polymerase-1
    • Li M., Naidu P., Yu Y., Berger N.A., and Kannan P. Dual regulation of AP-2alpha transcriptional activation by poly(ADP-ribose) polymerase-1. Biochem. J. 382 (2004) 323-329
    • (2004) Biochem. J. , vol.382 , pp. 323-329
    • Li, M.1    Naidu, P.2    Yu, Y.3    Berger, N.A.4    Kannan, P.5
  • 26
    • 21644484729 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 association with the peripheral nuclear lamina in rat hepatocytes
    • Vidaković M., Grdović N., Quesada P., Poznanović G., and Bode J. Poly(ADP-ribose) polymerase-1 association with the peripheral nuclear lamina in rat hepatocytes. J. Cell Biochem. 93 (2004) 1155-1168
    • (2004) J. Cell Biochem. , vol.93 , pp. 1155-1168
    • Vidaković, M.1    Grdović, N.2    Quesada, P.3    Poznanović, G.4    Bode, J.5
  • 27
    • 24744461723 scopus 로고    scopus 로고
    • Colocalization of PARP-1 and lamin B in the nuclear architecture, A halo-fluorescence- and confocal microscopy study
    • Vidaković M., Koester M., Goetze S., Winkelmann S., Klar M., Poznanović G., and Bode J. Colocalization of PARP-1 and lamin B in the nuclear architecture, A halo-fluorescence- and confocal microscopy study. J. Cell Biochem. 96 (2005) 555-568
    • (2005) J. Cell Biochem. , vol.96 , pp. 555-568
    • Vidaković, M.1    Koester, M.2    Goetze, S.3    Winkelmann, S.4    Klar, M.5    Poznanović, G.6    Bode, J.7
  • 28
    • 65949121092 scopus 로고    scopus 로고
    • Subnuclear trafficking and the nuclear matrix
    • Tzfira T. & Citovsky V, eds, chapt. 3, pp, Kluwer Academic/Plenum Publishers, Norwell, MA
    • Meier, I., (2005). Subnuclear trafficking and the nuclear matrix. In Nuclear Import and Export in Plants and Animals (Tzfira T. & Citovsky V., eds), chapt. 3, pp. 35-49, Kluwer Academic/Plenum Publishers, Norwell, MA.
    • (2005) Nuclear Import and Export in Plants and Animals , pp. 35-49
    • Meier, I.1
  • 30
    • 0030690098 scopus 로고    scopus 로고
    • Stress-induced duplex DNA destabilization in scaffold/matrix attachment regions
    • Benham C., Kohwi-Shigematsu T., and Bode J. Stress-induced duplex DNA destabilization in scaffold/matrix attachment regions. J. Mol. Biol. 274 (1997) 181-196
    • (1997) J. Mol. Biol. , vol.274 , pp. 181-196
    • Benham, C.1    Kohwi-Shigematsu, T.2    Bode, J.3
  • 31
    • 0000908807 scopus 로고    scopus 로고
    • Transcription-promoting genomic sites in mammalia, their elucidation and architectural principles
    • Boulikas T. (Ed), Gene Therapy Press, Athens, Greece
    • Bode J., Bartsch J., Boulikas T., Iber M., Mielke C., Schuebeler D., et al. Transcription-promoting genomic sites in mammalia, their elucidation and architectural principles. In: Boulikas T. (Ed). Textbook of Gene Therapy and Molecular Biology (1998), Gene Therapy Press, Athens, Greece 551-580
    • (1998) Textbook of Gene Therapy and Molecular Biology , pp. 551-580
    • Bode, J.1    Bartsch, J.2    Boulikas, T.3    Iber, M.4    Mielke, C.5    Schuebeler, D.6
  • 32
    • 0034103927 scopus 로고    scopus 로고
    • Transcriptional augmentation, modulation of gene expression by scaffold/matrix attached Regions (S/MAR Elements)
    • Bode J., Benham C., Knopp A., and Mielke C. Transcriptional augmentation, modulation of gene expression by scaffold/matrix attached Regions (S/MAR Elements). Crit. Rev. Eukaryot. Gene Expr. 10 (2000) 73-90
    • (2000) Crit. Rev. Eukaryot. Gene Expr. , vol.10 , pp. 73-90
    • Bode, J.1    Benham, C.2    Knopp, A.3    Mielke, C.4
  • 33
    • 27644564304 scopus 로고    scopus 로고
    • Enhanceosome formation over the interferon-beta promoter underlies a remote-control mechanism mediated by YY1 and YY2
    • Klar M., and Bode J. Enhanceosome formation over the interferon-beta promoter underlies a remote-control mechanism mediated by YY1 and YY2. Mol. Cell Biol. 25 (2005) 10159-10170
    • (2005) Mol. Cell Biol. , vol.25 , pp. 10159-10170
    • Klar, M.1    Bode, J.2
  • 34
    • 28844491415 scopus 로고    scopus 로고
    • Dominant genomic structures, detection and potential signal functions
    • Klar M., Stellamanns E., A.K. P., Gluch A., and Bode J. Dominant genomic structures, detection and potential signal functions. Gene 364 (2005) 79-89
    • (2005) Gene , vol.364 , pp. 79-89
    • Klar, M.1    Stellamanns, E.2    A.K., P.3    Gluch, A.4    Bode, J.5
  • 35
    • 0029028802 scopus 로고
    • Detection of Scaffold-Attached Regions (SARs) by in vitro techniques, Activities of these elements in vivo
    • Kay V., and Bode J. Detection of Scaffold-Attached Regions (SARs) by in vitro techniques, Activities of these elements in vivo. Method Mol. Cell Biol. 5 (1995) 186-194
    • (1995) Method Mol. Cell Biol. , vol.5 , pp. 186-194
    • Kay, V.1    Bode, J.2
  • 36
    • 0032496140 scopus 로고    scopus 로고
    • Genomic organization of drosophila poly(ADP-ribose) polymerase and distribution of its mRNA during development
    • Hanai S., Uchida M., Kobayashi S., Miwa M., and Uchida K. Genomic organization of drosophila poly(ADP-ribose) polymerase and distribution of its mRNA during development. J. Biol. Chem. 273 (1998) 11881-11886
    • (1998) J. Biol. Chem. , vol.273 , pp. 11881-11886
    • Hanai, S.1    Uchida, M.2    Kobayashi, S.3    Miwa, M.4    Uchida, K.5
  • 37
    • 3042812467 scopus 로고    scopus 로고
    • A conserved initiator element on the mammalian poly(ADP-ribose) polymerase-1 promoters, in combination with flanking core elements, is necessary to obtain high transcriptional activity
    • Laniel M.A., Poirier G.G., and Guerin S.L. A conserved initiator element on the mammalian poly(ADP-ribose) polymerase-1 promoters, in combination with flanking core elements, is necessary to obtain high transcriptional activity. Biochim. Biophys. Acta 1679 (2004) 37-46
    • (2004) Biochim. Biophys. Acta , vol.1679 , pp. 37-46
    • Laniel, M.A.1    Poirier, G.G.2    Guerin, S.L.3
  • 38
    • 33744805985 scopus 로고    scopus 로고
    • Genome-wide analysis of mammalian promoter architecture and evolution
    • Carninci P., Sandelin A., and Lenhard B. Genome-wide analysis of mammalian promoter architecture and evolution. Nature Genet. 28 (2006) 626-635
    • (2006) Nature Genet. , vol.28 , pp. 626-635
    • Carninci, P.1    Sandelin, A.2    Lenhard, B.3
  • 39
    • 0027131878 scopus 로고
    • The minimal self-sufficient element in a murine G+C-rich promoter is a large element with imperfect dyad symmetry
    • Ackerman S.L., Minden A.G., and Yeung C.Y. The minimal self-sufficient element in a murine G+C-rich promoter is a large element with imperfect dyad symmetry. Proc. Natl Acad. Sci. USA 90 (1993) 11865-11869
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11865-11869
    • Ackerman, S.L.1    Minden, A.G.2    Yeung, C.Y.3
  • 40
    • 0026773938 scopus 로고
    • Localized torsional tension in the DNA of human cells
    • Ljungman M., and Hanawalt P.C. Localized torsional tension in the DNA of human cells. Proc. Natl Acad. Sci. USA 89 (1992) 6055-6059
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6055-6059
    • Ljungman, M.1    Hanawalt, P.C.2
  • 41
    • 0025181252 scopus 로고
    • Hierarchical binding of DNA fragments derived from scaffold-attached regions, correlations of properties in vitro and function in vivo
    • Mielke C., Kohwi Y., Kohwi-Shigematsu T., and Bode J. Hierarchical binding of DNA fragments derived from scaffold-attached regions, correlations of properties in vitro and function in vivo. Biochemistry 29 (1990) 7475-7485
    • (1990) Biochemistry , vol.29 , pp. 7475-7485
    • Mielke, C.1    Kohwi, Y.2    Kohwi-Shigematsu, T.3    Bode, J.4
  • 42
    • 0025323364 scopus 로고
    • The interaction of adenosine diphosphoribosyl transferase (ADPRT) with a cruciform DNA
    • Sastry S.S., and Kun E. The interaction of adenosine diphosphoribosyl transferase (ADPRT) with a cruciform DNA. Biochem. Biophys. Res. Commun. 167 (1990) 842-847
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 842-847
    • Sastry, S.S.1    Kun, E.2
  • 44
    • 0026750139 scopus 로고
    • Crosslinking of nuclear proteins to DNA by cis-diamminedichloroplatinum in intact cells
    • Ferraro A., Grandi P., Eufemi M., Altieri F., and Turano C. Crosslinking of nuclear proteins to DNA by cis-diamminedichloroplatinum in intact cells. FEBS Lett. 307 (1992) 383-385
    • (1992) FEBS Lett. , vol.307 , pp. 383-385
    • Ferraro, A.1    Grandi, P.2    Eufemi, M.3    Altieri, F.4    Turano, C.5
  • 45
    • 0029780361 scopus 로고    scopus 로고
    • Comparison of DNA-Protein interactions in nuclei from avian liver and erythrocytes, a crosslinking study
    • Ferraro A., Cervoni L., Eufemi M., Altieri F., and Turano C. Comparison of DNA-Protein interactions in nuclei from avian liver and erythrocytes, a crosslinking study. J. Cell. Biochem. 62 (1996) 495-505
    • (1996) J. Cell. Biochem. , vol.62 , pp. 495-505
    • Ferraro, A.1    Cervoni, L.2    Eufemi, M.3    Altieri, F.4    Turano, C.5
  • 47
    • 0036613754 scopus 로고    scopus 로고
    • Clustering of housekeeping genes provides a unified model of gene order in the human genome
    • Lercher M.J., Urrutia A.O., and Hurst L.D. Clustering of housekeeping genes provides a unified model of gene order in the human genome. Nature Genet. 31 (2002) 180-183
    • (2002) Nature Genet. , vol.31 , pp. 180-183
    • Lercher, M.J.1    Urrutia, A.O.2    Hurst, L.D.3
  • 48
    • 0141854009 scopus 로고    scopus 로고
    • The human transcriptome map reveals extremes in gene density, intron length, GC content, and repeat pattern for domains of highly and weakly expressed genes
    • Versteeg R., van Schaik B.D., van Batenburg M.F., Roos M., Monajemi R., Caron H., et al. The human transcriptome map reveals extremes in gene density, intron length, GC content, and repeat pattern for domains of highly and weakly expressed genes. Genome Res. 13 (2003) 1998-2004
    • (2003) Genome Res. , vol.13 , pp. 1998-2004
    • Versteeg, R.1    van Schaik, B.D.2    van Batenburg, M.F.3    Roos, M.4    Monajemi, R.5    Caron, H.6
  • 49
    • 0042880630 scopus 로고    scopus 로고
    • Spatial organisation of gene expression, the active chromatin hub
    • de Laat W., and Grosveld F. Spatial organisation of gene expression, the active chromatin hub. Chromosome Res. 11 (2003) 447-459
    • (2003) Chromosome Res. , vol.11 , pp. 447-459
    • de Laat, W.1    Grosveld, F.2
  • 50
    • 0028138645 scopus 로고
    • Dissection of the locus control function located on the chicken lysozyme gene domain in transgenic mice
    • Bonifer C., Yannoutsos N., Kruger G., Grosveld F., and Sippel A.E. Dissection of the locus control function located on the chicken lysozyme gene domain in transgenic mice. Nucl. Acid. Res. 22 (1994) 4202-4210
    • (1994) Nucl. Acid. Res. , vol.22 , pp. 4202-4210
    • Bonifer, C.1    Yannoutsos, N.2    Kruger, G.3    Grosveld, F.4    Sippel, A.E.5
  • 51
    • 0035849451 scopus 로고    scopus 로고
    • The 5′-boundary of the human apolipoprotein B chromatin domain in intestinal cells
    • Antes T.J., Namicu S.J., Fournier R.E.K., and Levy-Wilson B. The 5′-boundary of the human apolipoprotein B chromatin domain in intestinal cells. Biochemistry 40 (2001) 6731-6742
    • (2001) Biochemistry , vol.40 , pp. 6731-6742
    • Antes, T.J.1    Namicu, S.J.2    Fournier, R.E.K.3    Levy-Wilson, B.4
  • 53
    • 0023681595 scopus 로고
    • Nuclear matrix associated poly(ADP-ribose) metabolism in regenerating rat liver
    • Alvarez-Gonzalez R., and Ringer P. Nuclear matrix associated poly(ADP-ribose) metabolism in regenerating rat liver. FEBS Lett. 236 (1988) 362-366
    • (1988) FEBS Lett. , vol.236 , pp. 362-366
    • Alvarez-Gonzalez, R.1    Ringer, P.2
  • 54
    • 0023645755 scopus 로고
    • Endogenous polymers of ADP-ribose are associated with the nuclear matrix
    • Cardenas-Corona M.E., Jacobson E.L., and Jacobson M.K. Endogenous polymers of ADP-ribose are associated with the nuclear matrix. J. Biol. Chem. 262 (1987) 14863-14866
    • (1987) J. Biol. Chem. , vol.262 , pp. 14863-14866
    • Cardenas-Corona, M.E.1    Jacobson, E.L.2    Jacobson, M.K.3
  • 55
    • 33947362037 scopus 로고    scopus 로고
    • Frequency distribution of TATA box and extension sequences on human promoters
    • Shi W., and Zhou W. Frequency distribution of TATA box and extension sequences on human promoters. BMC Bioinformatics 7 (2006) 1-12
    • (2006) BMC Bioinformatics , vol.7 , pp. 1-12
    • Shi, W.1    Zhou, W.2
  • 56
    • 0026504544 scopus 로고
    • Diverse transcriptional functions of the multisubunit eukaryotic TFIID complex
    • Pugh B.F., and Tjian R. Diverse transcriptional functions of the multisubunit eukaryotic TFIID complex. J. Biol. Chem. 267 (1992) 679-682
    • (1992) J. Biol. Chem. , vol.267 , pp. 679-682
    • Pugh, B.F.1    Tjian, R.2
  • 57
    • 0025275438 scopus 로고
    • Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene, Structural similarity to that of the DNA polymerase β gene
    • Ogura T., Nyunoya H., Takahashi-Masutani M., Miwa M., Sugimura T., and Easumi H. Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene, Structural similarity to that of the DNA polymerase β gene. Biochem. Biophys. Res. Commun. 167 (1990) 701-710
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 701-710
    • Ogura, T.1    Nyunoya, H.2    Takahashi-Masutani, M.3    Miwa, M.4    Sugimura, T.5    Easumi, H.6
  • 60
    • 17944385649 scopus 로고    scopus 로고
    • Activation of Reg gene, a gene for insulin-producing beta-cell regeneration, poly(ADP-ribose) polymerase binds Reg promoter and regulates the transcription by autopoly(ADP-ribosyl)ation
    • Akiyama T., Takasawa S., Nata K., Kobayashi S., Abe M., Shervani N.J., et al. Activation of Reg gene, a gene for insulin-producing beta-cell regeneration, poly(ADP-ribose) polymerase binds Reg promoter and regulates the transcription by autopoly(ADP-ribosyl)ation. Proc. Natl Acad. Sci. USA 98 (2001) 48-53
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 48-53
    • Akiyama, T.1    Takasawa, S.2    Nata, K.3    Kobayashi, S.4    Abe, M.5    Shervani, N.J.6
  • 61
    • 34548674438 scopus 로고    scopus 로고
    • Poly-(ADP-ribose) polymerase-1 (Parp-1) binds in a sequence-specific manner at the Bcl-6 locus and contributes to the regulation of Bcl-6 transcription
    • Ambrose H.E., Papadopoulou V., Beswick R.W., and Wagner S.D. Poly-(ADP-ribose) polymerase-1 (Parp-1) binds in a sequence-specific manner at the Bcl-6 locus and contributes to the regulation of Bcl-6 transcription. Oncogene 26 (2007) 6244-6252
    • (2007) Oncogene , vol.26 , pp. 6244-6252
    • Ambrose, H.E.1    Papadopoulou, V.2    Beswick, R.W.3    Wagner, S.D.4
  • 62
    • 0032959888 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase binds with transcription enhancer factor 1 to MCAT1 elements to regulate muscle-specific transcription
    • Butler A.J., and Ordahl C.P. Poly(ADP-ribose) polymerase binds with transcription enhancer factor 1 to MCAT1 elements to regulate muscle-specific transcription. Mol. Cell Biol. 19 (1999) 296-306
    • (1999) Mol. Cell Biol. , vol.19 , pp. 296-306
    • Butler, A.J.1    Ordahl, C.P.2
  • 63
    • 0347716450 scopus 로고    scopus 로고
    • Analysis of nucleotide sequence-dependent DNA binding of poly(ADP-ribose) polymerase in a purified system
    • Huang K., Tidyman W.E., Le K.U., Kirsten E., Kun E., and Ordahl C.P. Analysis of nucleotide sequence-dependent DNA binding of poly(ADP-ribose) polymerase in a purified system. Biochemistry 43 (2004) 217-223
    • (2004) Biochemistry , vol.43 , pp. 217-223
    • Huang, K.1    Tidyman, W.E.2    Le, K.U.3    Kirsten, E.4    Kun, E.5    Ordahl, C.P.6
  • 64
    • 0035937826 scopus 로고    scopus 로고
    • A role for poly(ADP-ribose) polymerase in the transcriptional regulation of the melanoma growth stimulatory activity (CXCL1) gene expression
    • Nirodi C., NagDas S., Gygi S.P., Olson G., Aebersold R., and Richmond A. A role for poly(ADP-ribose) polymerase in the transcriptional regulation of the melanoma growth stimulatory activity (CXCL1) gene expression. J. Biol. Chem. 276 (2001) 9366-9374
    • (2001) J. Biol. Chem. , vol.276 , pp. 9366-9374
    • Nirodi, C.1    NagDas, S.2    Gygi, S.P.3    Olson, G.4    Aebersold, R.5    Richmond, A.6
  • 65
    • 0036348921 scopus 로고    scopus 로고
    • Sequence-specific binding of poly(ADP-ribose) polymerase-1 to the human T cell leukemia virus type-I tax responsive element
    • Zhang Z., Hildebrandt E., Simbulan-Rosenthal C., and Anderson M. Sequence-specific binding of poly(ADP-ribose) polymerase-1 to the human T cell leukemia virus type-I tax responsive element. Virology 296 (2002) 107-116
    • (2002) Virology , vol.296 , pp. 107-116
    • Zhang, Z.1    Hildebrandt, E.2    Simbulan-Rosenthal, C.3    Anderson, M.4
  • 66
    • 27144555760 scopus 로고    scopus 로고
    • Gender differences in the endotoxin-induced inflammatory and vascular responses, Potential role of poly(ADP-ribose) polymerase activation
    • Mabley J.G., Horváth E.M., Murthy K.G.K., Zsengellér Z., Vaslin A., Benko R., et al. Gender differences in the endotoxin-induced inflammatory and vascular responses, Potential role of poly(ADP-ribose) polymerase activation. J. Pharmacol. Exp. Ther. 315 (2005) 812-820
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , pp. 812-820
    • Mabley, J.G.1    Horváth, E.M.2    Murthy, K.G.K.3    Zsengellér, Z.4    Vaslin, A.5    Benko, R.6
  • 67
    • 0025876999 scopus 로고
    • Functional analysis and in vivo footprinting implicate the erythroid transcription factor GATA-1 as a positive regulator of its own promoter
    • Tsai S.F., Strauss E., and Orkin S.H. Functional analysis and in vivo footprinting implicate the erythroid transcription factor GATA-1 as a positive regulator of its own promoter. Genes Dev. 5 (1991) 919-931
    • (1991) Genes Dev. , vol.5 , pp. 919-931
    • Tsai, S.F.1    Strauss, E.2    Orkin, S.H.3
  • 69
    • 0025277540 scopus 로고
    • Autoregulation of Pit-1 gene expression is mediated by to cis-active promoter elements
    • Chen R., Ingraham H.A., Treacy M.N., Albert V.R., Wilson L., and Rosenfeld M.G. Autoregulation of Pit-1 gene expression is mediated by to cis-active promoter elements. Nature 346 (1990) 583-586
    • (1990) Nature , vol.346 , pp. 583-586
    • Chen, R.1    Ingraham, H.A.2    Treacy, M.N.3    Albert, V.R.4    Wilson, L.5    Rosenfeld, M.G.6
  • 70
    • 0026516677 scopus 로고
    • The restricted promoter activity of the liver transcription factor hepatocyte nuclear factor 3 beta involves a cell-specific factor and positive autoactivation
    • Pani L., Qian X., Clevidence D., and Costa R.H. The restricted promoter activity of the liver transcription factor hepatocyte nuclear factor 3 beta involves a cell-specific factor and positive autoactivation. Mol. Cell Biol. 12 (1992) 552-562
    • (1992) Mol. Cell Biol. , vol.12 , pp. 552-562
    • Pani, L.1    Qian, X.2    Clevidence, D.3    Costa, R.H.4
  • 71
    • 35648955118 scopus 로고    scopus 로고
    • The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription
    • Wacker D.A., Ruhl D.D., Balagamwala E.H., Hope K.M., Zhang T., and Kraus W.L. The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription. Mol. Cell Biol. 27 (2007) 7475-7485
    • (2007) Mol. Cell Biol. , vol.27 , pp. 7475-7485
    • Wacker, D.A.1    Ruhl, D.D.2    Balagamwala, E.H.3    Hope, K.M.4    Zhang, T.5    Kraus, W.L.6
  • 72
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • d'Amours D., Desnoyers S., d'Silva I., and Poirier G. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 342 (1999) 249-268
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • d'Amours, D.1    Desnoyers, S.2    d'Silva, I.3    Poirier, G.4
  • 73
    • 0034956937 scopus 로고    scopus 로고
    • Breakpoints of t(4;11) translocations in the human MLL and AF4 genes in ALL patients are preferentially clustered outside of high-affinity matrix attachment regions
    • Hensel J.P., Gillert E., Fey G.H., and Marschalek R. Breakpoints of t(4;11) translocations in the human MLL and AF4 genes in ALL patients are preferentially clustered outside of high-affinity matrix attachment regions. J. Cell Biochem. 82 (2001) 299-309
    • (2001) J. Cell Biochem. , vol.82 , pp. 299-309
    • Hensel, J.P.1    Gillert, E.2    Fey, G.H.3    Marschalek, R.4
  • 74
    • 0028186644 scopus 로고
    • The bicinchoninic acid (BCA) assay for protein quantitation
    • Walker J.M. (Ed), Humana Press Inc, Totowa, NJ
    • Walker J.M. The bicinchoninic acid (BCA) assay for protein quantitation. In: Walker J.M. (Ed). Basic Protein and Peptide Protocols. Methods in Molecular Biology vol. 32 (1994), Humana Press Inc, Totowa, NJ 5-8
    • (1994) Basic Protein and Peptide Protocols. Methods in Molecular Biology , vol.32 , pp. 5-8
    • Walker, J.M.1


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