메뉴 건너뛰기




Volumn 20, Issue 2, 2006, Pages 335-347

Thanatos-associated protein 7 associates with template activating factor-Iβ and inhibits histone acetylation to repress transcription

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CARRIER PROTEIN; CELL NUCLEUS RECEPTOR; CELL PROTEIN; DNA BINDING PROTEIN; HISTONE; HISTONE H3; HISTONE H4; NUCLEAR HORMONE RECEPTOR COREPRESSOR PROTEIN; NUCLEAR PROTEIN; RETINOIC ACID RECEPTOR; SMALL INTERFERING RNA; TEMPLATE ACTIVATING FACTOR I BETA; THANATOS ASSOCIATED PROTEIN 7; THYROID HORMONE RECEPTOR; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 31444456303     PISSN: 08888809     EISSN: 08888809     Source Type: Journal    
DOI: 10.1210/me.2005-0248     Document Type: Article
Times cited : (36)

References (49)
  • 1
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M 1997 Histone acetylation in chromatin structure and transcription. Nature 389:349-352
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 2
    • 0034387004 scopus 로고    scopus 로고
    • 25 Years after the nucleosome model: Chromatin modifications
    • Wu J, Grunstein M 2000 25 years after the nucleosome model: chromatin modifications. Trends Biochem Sci 25:619-623
    • (2000) Trends Biochem Sci , vol.25 , pp. 619-623
    • Wu, J.1    Grunstein, M.2
  • 4
  • 5
    • 0037381213 scopus 로고    scopus 로고
    • Structure and dynamic behavior of nucleosomes
    • Luger K 2003 Structure and dynamic behavior of nucleosomes. Curr Opin Genet Dev 13:127-135
    • (2003) Curr Opin Genet Dev , vol.13 , pp. 127-135
    • Luger, K.1
  • 6
    • 0033515428 scopus 로고    scopus 로고
    • Increasing the complexity of coactivation in nuclear receptor signaling
    • Freedman LP 1999 Increasing the complexity of coactivation in nuclear receptor signaling. Cell 97:5-8
    • (1999) Cell , vol.97 , pp. 5-8
    • Freedman, L.P.1
  • 7
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG 2000 The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 14:121-141
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 10
    • 0033499866 scopus 로고    scopus 로고
    • Biochemical analysis of distinct activation functions in p300 that enhance transcription initiation with chromatin templates
    • Kraus WL, Manning ET, Kadonaga JT 1999 Biochemical analysis of distinct activation functions in p300 that enhance transcription initiation with chromatin templates. Mol Cell Biol 19:8123-8135
    • (1999) Mol Cell Biol , vol.19 , pp. 8123-8135
    • Kraus, W.L.1    Manning, E.T.2    Kadonaga, J.T.3
  • 11
    • 0034234237 scopus 로고    scopus 로고
    • CBP/p300 in cell growth, transformation, and development
    • Goodman RH, Smolik S 2000 CBP/p300 in cell growth, transformation, and development. Genes Dev 14:1553-1577
    • (2000) Genes Dev , vol.14 , pp. 1553-1577
    • Goodman, R.H.1    Smolik, S.2
  • 13
    • 0242582360 scopus 로고    scopus 로고
    • The human proliferating Cell nuclear antigen regulates transcriptional coactivator p300 activity and promotes transcriptional repression
    • Hong R, Chakravarti D 2003 The human proliferating Cell nuclear antigen regulates transcriptional coactivator p300 activity and promotes transcriptional repression. J Biol Chem 278:44505-44513
    • (2003) J Biol Chem , vol.278 , pp. 44505-44513
    • Hong, R.1    Chakravarti, D.2
  • 14
    • 0037160106 scopus 로고    scopus 로고
    • Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities
    • Li F, Macfarlan T, Pittman RN, Chakravarti D 2002 Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities. J Biol Chem 277:45004-45012
    • (2002) J Biol Chem , vol.277 , pp. 45004-45012
    • Li, F.1    Macfarlan, T.2    Pittman, R.N.3    Chakravarti, D.4
  • 15
    • 0035846894 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the Set oncoprotein
    • Seo S-b, McNamara P, Heo S, Turner A, Lane WS, Chakravarti D 2001 Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the Set oncoprotein. Cell 104:119-130
    • (2001) Cell , vol.104 , pp. 119-130
    • Seo, S.-B.1    McNamara, P.2    Heo, S.3    Turner, A.4    Lane, W.S.5    Chakravarti, D.6
  • 16
    • 0037134538 scopus 로고    scopus 로고
    • Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex
    • Seo SB, Macfarlan T, McNamara P, Hong R, Mukai Y, Heo S, Chakravarti D 2002 Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex. J Biol Chem 277:14005-14010
    • (2002) J Biol Chem , vol.277 , pp. 14005-14010
    • Seo, S.B.1    Macfarlan, T.2    McNamara, P.3    Hong, R.4    Mukai, Y.5    Heo, S.6    Chakravarti, D.7
  • 17
    • 0037925529 scopus 로고    scopus 로고
    • A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation
    • Yu J, Li Y, Ishizuka T, Guenther MG, Lazar MA 2003 A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation. EMBO J 22:3403-3410
    • (2003) EMBO J , vol.22 , pp. 3403-3410
    • Yu, J.1    Li, Y.2    Ishizuka, T.3    Guenther, M.G.4    Lazar, M.A.5
  • 18
    • 10944229755 scopus 로고    scopus 로고
    • The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains
    • Choi YB, Ko JK, Shin J 2004 The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains. J Biol Chem 279:50930-50941
    • (2004) J Biol Chem , vol.279 , pp. 50930-50941
    • Choi, Y.B.1    Ko, J.K.2    Shin, J.3
  • 19
    • 12244256087 scopus 로고    scopus 로고
    • A novel estrogen receptor α-associated protein, template-activating factor Iβ, inhibits acetylation and transactivation
    • Loven MA, Muster N, Yates JR, Nardulli AM 2003 A novel estrogen receptor α-associated protein, template-activating factor Iβ, inhibits acetylation and transactivation. Mol Endocrinol 17:67-78
    • (2003) Mol Endocrinol , vol.17 , pp. 67-78
    • Loven, M.A.1    Muster, N.2    Yates, J.R.3    Nardulli, A.M.4
  • 20
    • 8344256470 scopus 로고    scopus 로고
    • A novel estrogen receptor α-associated protein alters receptor-deoxyribonucleic acid interactions and represses receptor-mediated transcription
    • Loven MA, Davis RE, Curtis CD, Muster N, Yates JR, Nardulli AM 2004 A novel estrogen receptor α-associated protein alters receptor- deoxyribonucleic acid interactions and represses receptor-mediated transcription. Mol Endocrinol 18:2649-2645
    • (2004) Mol Endocrinol , vol.18 , pp. 2649-12645
    • Loven, M.A.1    Davis, R.E.2    Curtis, C.D.3    Muster, N.4    Yates, J.R.5    Nardulli, A.M.6
  • 21
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD 2001 Translating the histone code. Science 293:1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 22
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD 2000 The language of covalent histone modifications. Nature 403:41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 23
    • 0037074010 scopus 로고    scopus 로고
    • Signaling network model of chromatin
    • Schreiber SL, Bernstein BE 2002 Signaling network model of chromatin. Cell 111:771-778
    • (2002) Cell , vol.111 , pp. 771-778
    • Schreiber, S.L.1    Bernstein, B.E.2
  • 24
    • 3142730622 scopus 로고    scopus 로고
    • A signaling role of histone-binding proteins and INHAT subunits pp32 and Set/TAF-Iβ in integrating chromatin hypoacetylation and transcriptional repression
    • Kutney SN, Hong R, Macfarlan T, Chakravarti D 2004 A signaling role of histone-binding proteins and INHAT subunits pp32 and Set/TAF-Iβ in integrating chromatin hypoacetylation and transcriptional repression. J Biol Chem 279:30850-30855
    • (2004) J Biol Chem , vol.279 , pp. 30850-30855
    • Kutney, S.N.1    Hong, R.2    Macfarlan, T.3    Chakravarti, D.4
  • 25
    • 2642536094 scopus 로고    scopus 로고
    • Direct binding of INHAT to H3 tails disrupted by modifications
    • Schneider R, Bannister AJ, Weise C, Kouzarides T 2004 Direct binding of INHAT to H3 tails disrupted by modifications. J Biol Chem 279:23859-23862
    • (2004) J Biol Chem , vol.279 , pp. 23859-23862
    • Schneider, R.1    Bannister, A.J.2    Weise, C.3    Kouzarides, T.4
  • 26
    • 0042707934 scopus 로고    scopus 로고
    • Functional interaction of the DNA-binding transcription factor Sp1 through its DNA-binding domain with the histone chaperone TAF-I
    • Suzuki T, Muto S, Miyamoto S, Aizawa K, Horikoshi M, Nagai R 2003 Functional interaction of the DNA-binding transcription factor Sp1 through its DNA-binding domain with the histone chaperone TAF-I. J Biol Chem 278:28758-28764
    • (2003) J Biol Chem , vol.278 , pp. 28758-28764
    • Suzuki, T.1    Muto, S.2    Miyamoto, S.3    Aizawa, K.4    Horikoshi, M.5    Nagai, R.6
  • 27
    • 0242637390 scopus 로고    scopus 로고
    • Positive and negative regulation of the cardiovascular transcription factor KLF5 by p300 and the oncogenic regulator SET through interaction and acetylation on the DNA-binding domain
    • Miyamoto S, Suzuki T, Muto S, Aizawa K, Kimura A, Mizuno Y, Nagino T, Imai Y, Adachi N, Horikoshi M, Nagai R 2003 Positive and negative regulation of the cardiovascular transcription factor KLF5 by p300 and the oncogenic regulator SET through interaction and acetylation on the DNA-binding domain. Mol Cell Biol 23:8528-8541
    • (2003) Mol Cell Biol , vol.23 , pp. 8528-8541
    • Miyamoto, S.1    Suzuki, T.2    Muto, S.3    Aizawa, K.4    Kimura, A.5    Mizuno, Y.6    Nagino, T.7    Imai, Y.8    Adachi, N.9    Horikoshi, M.10    Nagai, R.11
  • 29
    • 18744396089 scopus 로고    scopus 로고
    • The THAP domain of THAP1 is a large C2CH module with zinc-dependent sequence-specific DNA-binding activity
    • USA
    • Clouaire T, Roussigne M, Ecochard V, Mathe C, Amalric F, Girard JP 2005 The THAP domain of THAP1 is a large C2CH module with zinc-dependent sequence-specific DNA-binding activity. Proc Natl Acad Sci USA 102:6907-6912
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 6907-6912
    • Clouaire, T.1    Roussigne, M.2    Ecochard, V.3    Mathe, C.4    Amalric, F.5    Girard, J.P.6
  • 30
    • 14844333086 scopus 로고    scopus 로고
    • Human THAP7 is a chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressor
    • Macfarlan T, Kutney S, Altman B, Montross R, Yu J, Chakravarti D 2005 Human THAP7 is a chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressor. J Biol Chem 280:7346-7358
    • (2005) J Biol Chem , vol.280 , pp. 7346-7358
    • Macfarlan, T.1    Kutney, S.2    Altman, B.3    Montross, R.4    Yu, J.5    Chakravarti, D.6
  • 32
    • 0037423932 scopus 로고    scopus 로고
    • Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor
    • Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J 2003 Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell 112:659-672
    • (2003) Cell , vol.112 , pp. 659-672
    • Fan, Z.1    Beresford, P.J.2    Oh, D.Y.3    Zhang, D.4    Lieberman, J.5
  • 33
    • 0033532586 scopus 로고    scopus 로고
    • Functional domains of template-activating factor-I as a protein phosphatase 2A inhibitor
    • Saito S, Miyaji-Yamaguchi M, Shimoyama T, Nagata K 1999 Functional domains of template-activating factor-I as a protein phosphatase 2A inhibitor. Biochem Biophys Res Commun 259:471-475
    • (1999) Biochem Biophys Res Commun , vol.259 , pp. 471-475
    • Saito, S.1    Miyaji-Yamaguchi, M.2    Shimoyama, T.3    Nagata, K.4
  • 35
    • 0028931302 scopus 로고
    • Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney
    • Li M, Guo H, Damuni Z 1995 Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney. Biochemistry 34:1988-1996
    • (1995) Biochemistry , vol.34 , pp. 1988-1996
    • Li, M.1    Guo, H.2    Damuni, Z.3
  • 36
    • 0035724413 scopus 로고    scopus 로고
    • The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3
    • Guenther MG, Barak O, Lazar MA 2001 The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3. Mol Cell Biol 21:6091-6101
    • (2001) Mol Cell Biol , vol.21 , pp. 6091-6101
    • Guenther, M.G.1    Barak, O.2    Lazar, M.A.3
  • 38
    • 0032528302 scopus 로고    scopus 로고
    • DNA binding by the KP repressor protein inhibits P-element transposase activity in vitro
    • Lee CC, Beall EL, Rio DC 1998 DNA binding by the KP repressor protein inhibits P-element transposase activity in vitro. EMBO J 17:4166-4174
    • (1998) EMBO J , vol.17 , pp. 4166-4174
    • Lee, C.C.1    Beall, E.L.2    Rio, D.C.3
  • 39
    • 2642648639 scopus 로고    scopus 로고
    • Regulation of interferon-induced protein kinase PKR: Modulation of P58IPK inhibitory function by a novel protein, P52rIPK
    • Gale Jr M, Blakely CM, Hopkins DA, Melville MW, Wambach M, Romano PR, Katze MG 1998 Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPK. Mol Cell Biol 18:859-871
    • (1998) Mol Cell Biol , vol.18 , pp. 859-871
    • Gale Jr., M.1    Blakely, C.M.2    Hopkins, D.A.3    Melville, M.W.4    Wambach, M.5    Romano, P.R.6    Katze, M.G.7
  • 40
    • 0038330739 scopus 로고    scopus 로고
    • THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis- response-4 (Par-4) to PML nuclear bodies
    • Roussigne M, Cayrol C, Clouaire T, Amalric F, Girard JP 2003 THAP1 is a nuclear proapoptotic factor that links prostate-apoptosis-response-4 (Par-4) to PML nuclear bodies. Oncogene 22:2432-2442
    • (2003) Oncogene , vol.22 , pp. 2432-2442
    • Roussigne, M.1    Cayrol, C.2    Clouaire, T.3    Amalric, F.4    Girard, J.P.5
  • 41
    • 0037423949 scopus 로고    scopus 로고
    • SET-ting the stage for life and death
    • Chakravarti D, Hong R 2003 SET-ting the stage for life and death. Cell 112:589-591
    • (2003) Cell , vol.112 , pp. 589-591
    • Chakravarti, D.1    Hong, R.2
  • 42
    • 0024975211 scopus 로고
    • Drosophila P element transposase recognizes internal P element DNA sequences
    • Kaufman PD, Doll RF, Rio DC 1989 Drosophila P element transposase recognizes internal P element DNA sequences. Cell 59:359-371
    • (1989) Cell , vol.59 , pp. 359-371
    • Kaufman, P.D.1    Doll, R.F.2    Rio, D.C.3
  • 43
    • 0042592941 scopus 로고    scopus 로고
    • The N-CoR/histone deacetylase 3 complex is required for repression by thyroid hormone receptor
    • Ishizuka T, Lazar MA 2003 The N-CoR/histone deacetylase 3 complex is required for repression by thyroid hormone receptor. Mol Cell Biol 23:5122-5131
    • (2003) Mol Cell Biol , vol.23 , pp. 5122-5131
    • Ishizuka, T.1    Lazar, M.A.2
  • 44
    • 0027263966 scopus 로고
    • Template activating factor I, a novel host factor required to stimulate the adenovirus core DNA replication
    • Matsumoto K, Nagata K, Ui M, Hanaoka F 1993 Template activating factor I, a novel host factor required to stimulate the adenovirus core DNA replication. J Biol Chem 268:10582-10587
    • (1993) J Biol Chem , vol.268 , pp. 10582-10587
    • Matsumoto, K.1    Nagata, K.2    Ui, M.3    Hanaoka, F.4
  • 45
    • 0028898807 scopus 로고
    • Stimulation of DNA transcription by the replication factor from the adenovirus genome in a chromatin-like structure
    • Matsumoto K, Okuwaki M, Kawase H, Handa H, Hanaoka F, Nagata K 1995 Stimulation of DNA transcription by the replication factor from the adenovirus genome in a chromatin-like structure. J Biol Chem 270:9645-9650
    • (1995) J Biol Chem , vol.270 , pp. 9645-9650
    • Matsumoto, K.1    Okuwaki, M.2    Kawase, H.3    Handa, H.4    Hanaoka, F.5    Nagata, K.6
  • 46
    • 0032545296 scopus 로고    scopus 로고
    • Template activating factor-I remodels the chromatin structure and stimulates transcription from the chromatin template
    • Okuwaki M, Nagata K 1998 Template activating factor-I remodels the chromatin structure and stimulates transcription from the chromatin template. J Biol Chem 273:34511-34518
    • (1998) J Biol Chem , vol.273 , pp. 34511-34518
    • Okuwaki, M.1    Nagata, K.2
  • 47
    • 0037067661 scopus 로고    scopus 로고
    • The oncoprotein Set/TAF-1β, an inhibitor of histone acetyltransferase, inhibits active demethylation of DNA, integrating DNA methylation and transcriptional silencing
    • Cervoni N, Detich N, Seo SB, Chakravarti D, Szyf M 2002 The oncoprotein Set/TAF-1β, an inhibitor of histone acetyltransferase, inhibits active demethylation of DNA, integrating DNA methylation and transcriptional silencing. J Biol Chem 277:25026-25031
    • (2002) J Biol Chem , vol.277 , pp. 25026-25031
    • Cervoni, N.1    Detich, N.2    Seo, S.B.3    Chakravarti, D.4    Szyf, M.5
  • 48
    • 11844263936 scopus 로고    scopus 로고
    • The histone chaperone TAF-I/SET/INHAT is required for transcription in vitro of chromatin templates
    • Gamble MJ, Erdjument-Bromage H, Tempst P, Freedman LP, Fisher RP 2005 The histone chaperone TAF-I/SET/INHAT is required for transcription in vitro of chromatin templates. Mol Cell Biol 25:797-807
    • (2005) Mol Cell Biol , vol.25 , pp. 797-807
    • Gamble, M.J.1    Erdjument-Bromage, H.2    Tempst, P.3    Freedman, L.P.4    Fisher, R.P.5
  • 49
    • 0035967914 scopus 로고    scopus 로고
    • Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: A humoral mechanism to reset a peripheral clock
    • McNamara P, Seo S-b, Rudic RD, Sehgal A, Chakravarti D, FitzGerald GA 2001 Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: a humoral mechanism to reset a peripheral clock. Cell 105:877-889
    • (2001) Cell , vol.105 , pp. 877-889
    • McNamara, P.1    Seo, S.-B.2    Rudic, R.D.3    Sehgal, A.4    Chakravarti, D.5    FitzGerald, G.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.