TBP | |||||||||
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crystal structure of a yeast brf1-tbp-dna ternary complex | |||||||||
鉴定 | |||||||||
标志 | TBP | ||||||||
Pfam | PF00352 | ||||||||
Pfam宗系 | CL0407 | ||||||||
InterPro | IPR000814 | ||||||||
PROSITE | PDOC00303 | ||||||||
SCOP | 1tbp / SUPFAM | ||||||||
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TATA结合蛋白质(英语:TATA-binding protein,TBP)是一种通用转录因子,具体结合于DNA序列上的TATA盒。TATA盒位于真核基因的转录起始位点上游约30个bp,属于启动子区[1]。TBP可以和各个TBP相关因子共同组成通用转录因子TFIID,再进一步组成RNA聚合酶Ⅱ的转录起始复合物[2]。
蛋白质的相互作用
TATA结合蛋白与下列蛋白质进行互作:
- BRF1,[3][4]
- BTAF1,[5][6]
- C-Fos,[7]
- C-jun,[8]
- EDF1,[9][10][11]
- GTF2B (TFIIB),[12][13]
- GTF2A1 (TFIIA subunit 1),[12][14][15][16]
- GTF2F1 (TFIIF subunit 1)[5][17][18]
- GTF2H4 (TFIIH subunit 4),[5]
- Mdm2,[19][19][20]
- MSX1,[21][22][23]
- NFYB,[24]
- P53,[25][26]
- PAX6,[26]
- POLR2A,[5]
- POU2F1,[27]
- RELA,[28][29]
- NR2B1,[30]
- TAF1,[24][31][32][33]
- TAF4,[34]
- TAF5,[24][32][35]
- TAF6,[24][32][34]
- TAF7,[24][34]
- TAF9.[24][36]
- TAF10,[24][32]
- TAF11,[24][37][38]
- TAF13,[37]
- TAF15.[39]
参考文献
- ↑ The molecular basis of eukaryotic transcription. Proc. Natl. Acad. Sci. U.S.A. 2007, 104 (32): 12955–61. PMC 1941834 . PMID 17670940. doi:10.1073/pnas.0704138104.
- ↑ Transcription of eukaryotic protein–coding genes. Annu. Rev. Genet. 2000, 34: 77–137. PMID 11092823. doi:10.1146/annurev.genet.34.1.77.
- ↑ McCulloch V, Hardin P, Peng W, Ruppert JM, Lobo-Ruppert SM. Alternatively spliced hBRF variants function at different RNA polymerase III promoters. EMBO J. 2000-08, 19 (15): 4134–43. PMC 306597 . PMID 10921893. doi:10.1093/emboj/19.15.4134.
- ↑ Wang Z, Roeder RG. Structure and function of a human transcription factor TFIIIB subunit that is evolutionarily conserved and contains both TFIIB- and high-mobility-group protein 2-related domains. Proc. Natl. Acad. Sci. U.S.A. 1995-07, 92 (15): 7026–30. PMC 41464 . PMID 7624363. doi:10.1073/pnas.92.15.7026.
- ↑ 5.0 5.1 5.2 5.3 Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD. BRCA1 is a component of the RNA polymerase II holoenzyme. Proc. Natl. Acad. Sci. U.S.A. 1997-05, 94 (11): 5605–10. PMC 20825 . PMID 9159119. doi:10.1073/pnas.94.11.5605.
- ↑ Chicca JJ, Auble DT, Pugh BF. Cloning and biochemical characterization of TAF-172, a human homolog of yeast Mot1. Mol. Cell. Biol. 1998-03, 18 (3): 1701–10. PMC 108885 . PMID 9488487.
- ↑ Metz R, Bannister AJ, Sutherland JA, Hagemeier C, O'Rourke EC, Cook A, Bravo R, Kouzarides T. c-Fos-induced activation of a TATA-box-containing promoter involves direct contact with TATA-box-binding protein. Mol. Cell. Biol. 1994-09, 14 (9): 6021–9. PMC 359128 . PMID 8065335. doi:10.1128/MCB.14.9.6021.
- ↑ Franklin CC, McCulloch AV, Kraft AS. In vitro association between the Jun protein family and the general transcription factors, TBP and TFIIB. Biochem. J. 1995-02, 305 (3): 967–74. PMC 1136352 . PMID 7848298. doi:10.1042/bj3050967.
- ↑ Brendel C, Gelman L, Auwerx J. Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism. Mol. Endocrinol. 2002-06, 16 (6): 1367–77. PMID 12040021. doi:10.1210/mend.16.6.0843.
- ↑ Mariotti M, De Benedictis L, Avon E, Maier JA. Interaction between endothelial differentiation-related factor-1 and calmodulin in vitro and in vivo. J. Biol. Chem. 2000-08, 275 (31): 24047–51. PMID 10816571. doi:10.1074/jbc.M001928200.
- ↑ Kabe Y, Goto M, Shima D, Imai T, Wada T, Morohashi Ki, Shirakawa M, Hirose S, Handa H. The role of human MBF1 as a transcriptional coactivator. J. Biol. Chem. 1999-11, 274 (48): 34196–202. PMID 10567391. doi:10.1074/jbc.274.48.34196.
- ↑ 12.0 12.1 Tang H, Sun X, Reinberg D, Ebright RH. Protein–protein interactions in eukaryotic transcription initiation: structure of the preinitiation complex. Proc. Natl. Acad. Sci. U.S.A. 1996-02, 93 (3): 1119–24. PMC 40041 . PMID 8577725. doi:10.1073/pnas.93.3.1119.
- ↑ Bushnell DA, Westover KD, Davis RE, Kornberg RD. Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms. Science. 2004-02, 303 (5660): 983–8. PMID 14963322. doi:10.1126/science.1090838.
- ↑ DeJong J, Bernstein R, Roeder RG. Human general transcription factor TFIIA: characterization of a cDNA encoding the small subunit and requirement for basal and activated transcription. Proc. Natl. Acad. Sci. U.S.A. 1995-04, 92 (8): 3313–7. PMC 42156 . PMID 7724559. doi:10.1073/pnas.92.8.3313.
- ↑ Ozer J, Mitsouras K, Zerby D, Carey M, Lieberman PM. Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding. J. Biol. Chem. 1998-06, 273 (23): 14293–300. PMID 9603936. doi:10.1074/jbc.273.23.14293.
- ↑ Sun X, Ma D, Sheldon M, Yeung K, Reinberg D. Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription. Genes Dev. 1994-10, 8 (19): 2336–48. PMID 7958900. doi:10.1101/gad.8.19.2336.
- ↑ Ruppert S, Tjian R. Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation. Genes Dev. 1995-11, 9 (22): 2747–55. PMID 7590250. doi:10.1101/gad.9.22.2747.
- ↑ Malik S, Guermah M, Roeder RG. A dynamic model for PC4 coactivator function in RNA polymerase II transcription. Proc. Natl. Acad. Sci. U.S.A. 1998-03, 95 (5): 2192–7. PMC 19292 . PMID 9482861. doi:10.1073/pnas.95.5.2192.
- ↑ 19.0 19.1 Thut CJ, Goodrich JA, Tjian R. Repression of p53-mediated transcription by MDM2: a dual mechanism. Genes Dev. 1997-08, 11 (15): 1974–86. PMC 316412 . PMID 9271120. doi:10.1101/gad.11.15.1974.
- ↑ Léveillard T, Wasylyk B. The MDM2 C-terminal region binds to TAFII250 and is required for MDM2 regulation of the cyclin A promoter. J. Biol. Chem. 1997-12, 272 (49): 30651–61. PMID 9388200. doi:10.1074/jbc.272.49.30651.
- ↑ Shetty S, Takahashi T, Matsui H, Ayengar R, Raghow R. Transcriptional autorepression of Msx1 gene is mediated by interactions of Msx1 protein with a multi-protein transcriptional complex containing TATA-binding protein, Sp1 and cAMP-response-element-binding protein-binding protein (CBP/p300). Biochem. J. 1999-05, 339 (3): 751–8. PMC 1220213 . PMID 10215616. doi:10.1042/0264-6021:3390751.
- ↑ Zhang H, Hu G, Wang H, Sciavolino P, Iler N, Shen MM, Abate-Shen C. Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism. Mol. Cell. Biol. 1997-05, 17 (5): 2920–32. PMC 232144 . PMID 9111364. doi:10.1128/mcb.17.5.2920.
- ↑ Zhang H, Catron KM, Abate-Shen C. A role for the Msx-1 homeodomain in transcriptional regulation: residues in the N-terminal arm mediate TATA binding protein interaction and transcriptional repression. Proc. Natl. Acad. Sci. U.S.A. 1996-03, 93 (5): 1764–9. PMC 39855 . PMID 8700832. doi:10.1073/pnas.93.5.1764.
- ↑ 24.0 24.1 24.2 24.3 24.4 24.5 24.6 24.7 Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R. CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues. Nucleic Acids Res. 1997-06, 25 (11): 2174–81. PMC 146709 . PMID 9153318. doi:10.1093/nar/25.11.2174.
- ↑ Seto E, Usheva A, Zambetti GP, Momand J, Horikoshi N, Weinmann R, Levine AJ, Shenk T. Wild-type p53 binds to the TATA-binding protein and represses transcription. Proc. Natl. Acad. Sci. U.S.A. 1992-12, 89 (24): 12028–32. PMC 50691 . PMID 1465435. doi:10.1073/pnas.89.24.12028.
- ↑ 26.0 26.1 Cvekl A, Kashanchi F, Brady JN, Piatigorsky J. Pax-6 interactions with TATA-box-binding protein and retinoblastoma protein. Invest. Ophthalmol. Vis. Sci. 1999-06, 40 (7): 1343–50. PMID 10359315.
- ↑ Zwilling S, Annweiler A, Wirth T. The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP. Nucleic Acids Res. 1994-05, 22 (9): 1655–62. PMC 308045 . PMID 8202368. doi:10.1093/nar/22.9.1655.
- ↑ Guermah M, Malik S, Roeder RG. Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-kappaB and Sp1. Mol. Cell. Biol. 1998-06, 18 (6): 3234–44. PMC 108905 . PMID 9584164. doi:10.1128/mcb.18.6.3234.
- ↑ Schmitz ML, Stelzer G, Altmann H, Meisterernst M, Baeuerle PA. Interaction of the COOH-terminal transactivation domain of p65 NF-kappa B with TATA-binding protein, transcription factor IIB, and coactivators. J. Biol. Chem. 1995-03, 270 (13): 7219–26. PMID 7706261. doi:10.1074/jbc.270.13.7219.
- ↑ Schulman IG, Chakravarti D, Juguilon H, Romo A, Evans RM. Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation. Proc. Natl. Acad. Sci. U.S.A. 1995-08, 92 (18): 8288–92. PMC 41142 . PMID 7667283. doi:10.1073/pnas.92.18.8288.
- ↑ Siegert JL, Robbins PD. Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250. Mol. Cell. Biol. 1999-01, 19 (1): 846–54. PMC 83941 . PMID 9858607.
- ↑ 32.0 32.1 32.2 32.3 Ruppert S, Wang EH, Tjian R. Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation. Nature. 1993-03, 362 (6416): 175–9. PMID 7680771. doi:10.1038/362175a0.
- ↑ O'Brien T, Tjian R. Functional analysis of the human TAFII250 N-terminal kinase domain. Mol. Cell. 1998-05, 1 (6): 905–11. PMID 9660973. doi:10.1016/S1097-2765(00)80089-1.
- ↑ 34.0 34.1 34.2 Pointud JC, Mengus G, Brancorsini S, Monaco L, Parvinen M, Sassone-Corsi P, Davidson I. The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation. J. Cell. Sci. 2003-05, 116 (Pt 9): 1847–58. PMID 12665565. doi:10.1242/jcs.00391.
- ↑ Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG. Specific interactions and potential functions of human TAFII100. J. Biol. Chem. 1997-03, 272 (10): 6714–21. PMID 9045704. doi:10.1074/jbc.272.10.6714.
- ↑ Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG. Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. Mol. Cell. Biol. 2001-10, 21 (20): 6782–95. PMC 99856 . PMID 11564863. doi:10.1128/MCB.21.20.6782-6795.2001.
- ↑ 37.0 37.1 Mengus G, May M, Jacq X, Staub A, Tora L, Chambon P, Davidson I. Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID. EMBO J. 1995-04, 14 (7): 1520–31. PMC 398239 . PMID 7729427.
- ↑ May M, Mengus G, Lavigne AC, Chambon P, Davidson I. Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors. EMBO J. 1996-06, 15 (12): 3093–104. PMC 450252 . PMID 8670810.
- ↑ Hoffmann A, Roeder RG. Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation. J. Biol. Chem. 1996-07, 271 (30): 18194–202. PMID 8663456. doi:10.1074/jbc.271.30.18194.