The Full Wiki

TATA-binding protein: Wikis


Note: Many of our articles have direct quotes from sources you can cite, within the Wikipedia article! This article doesn't yet, but we're working on it! See more info or our list of citable articles.


From Wikipedia, the free encyclopedia

TATA box binding protein

PDB rendering based on 1c9b.
Available structures
1c9b, 1cdw, 1jfi, 1nvp, 1tgh
Symbols TBP; GTF2D; GTF2D1; MGC117320; MGC126054; MGC126055; SCA17; TFIID
External IDs OMIM600075 MGI101838 HomoloGene2404 GeneCards: TBP Gene
RNA expression pattern
PBB GE TBP 203135 at tn.png
More reference expression data
Species Human Mouse
Entrez 6908 21374
Ensembl ENSG00000112592 ENSMUSG00000014767
UniProt P20226 Q6LEM2
RefSeq (mRNA) NM_003194 NM_013684
RefSeq (protein) NP_003185 NP_038712
Location (UCSC) Chr 6:
170.71 - 170.72 Mb
Chr 17:
15.2 - 15.22 Mb
PubMed search [1] [2]

The TATA binding protein (TBP) is a transcription factor that binds specifically to a DNA sequence called the TATA box. This DNA sequence is found about 35 base pairs upstream of the transcription start site in some eukaryotic gene promoters.[1] TBP, along with a variety of TBP-associated factors, make up the TFIID, a general transcription factor that in turn makes up part of the RNA polymerase II preinitiation complex.[2] As one of the few proteins in the preinitiation complex that binds DNA in a sequence-specific manner, it helps position RNA polymerase II over the transcription start site of the gene. However, it is estimated that only 10-20% of human promoters have TATA boxes. Therefore, TBP is probably not the only protein involved in positioning RNA polymerase II.

TBP is involved in DNA melting (double strand separation) by bending the DNA by 80° (the AT-rich sequence to which it binds facilitates easy melting). The TBP is an unusual protein in that it binds the minor groove using a β sheet.

Another distinctive feature of TBP is a long string of glutamines in the N-terminus of the protein. This region modulates the DNA binding activity of the C-terminus, and modulation of DNA binding affects the rate of transcription complex formation and initiation of transcription. Mutations that expand the number of CAG repeats encoding this polyglutamine tract, and thus increase the length of the polyglutamine string, are associated with spinocerebellar ataxia 17, a neurodegenerative disorder classified as a polyglutamine disease.[3]


Role as Transcription Factor Subunit

TBP is a subunit of the eukaryotic transcription factor TFIID. TFIID is the first protein to bind to DNA during the formation of the pre-initiation transcription complex of RNA polymerase II (RNA Pol II). Binding of TFIID to the TATA box in the promoter region of the gene initiates the recruitment of other factors required for RNA Pol II to begin transcription. Some of the other recruited transcription factors include TFIIA, TFIIB and TFIIF. Each of these transcription factors are formed from the interaction of many protein subunits, indicating that transcription is a heavily regulated process.

TBP is also a necessary component of RNA polymerase I and RNA polymerase III, and is perhaps the only common subunit required by all three of the RNA polymerases.

DNA-Protein Interactions

TBP (blue) bound to DNA (red). The bend in the DNA created by TBP binding can clearly be seen. Image by David S. Goodsell based on the crystal structure 1cdw from the Protein Data Bank.

When TBP binds to a TATA box within the DNA, it distorts the DNA by inserting amino acid side chains between base pairs, partially unwinding the helix, and doubly kinking it. The distortion is accomplished through a great amount of surface contact between the protein and DNA. TBP binds with the negatively charged phosphates in the DNA backbone through positively charged lysine and arginine amino acid residues. The sharp bend in the DNA is produced through projection of four bulky phenylalanine residues into the minor groove. As the DNA bends, its contact with TBP increases, thus enhancing the DNA-protein interaction.

The strain imposed on the DNA through this interaction initiates melting, or separation, of the strands. Because this region of DNA is rich in adenine and thymine residues, which base pair through only two hydrogen bonds, the DNA strands are more easily separated. Separation of the two strands exposes the bases and allows RNA polymerase II to begin transcription of the gene.

TBP's C-terminus composes of a helicoidal shape that (incompletely) compliments the T-A-T-A region of DNA. Interestingly this incompleteness allows DNA to be passively bent on binding.

For information on the use of TBP in cells see: RNA polymerase I, RNA polymerase II and RNA polymerase III.


TATA binding protein has been shown to interact with:


  1. ^ Kornberg RD (2007). "The molecular basis of eukaryotic transcription". Proc. Natl. Acad. Sci. U.S.A. 104 (32): 12955–61. doi:10.1073/pnas.0704138104. PMID 17670940. 
  2. ^ Lee TI, Young RA (2000). "Transcription of eukaryotic protein-coding genes". Annu. Rev. Genet. 34: 77–137. doi:10.1146/annurev.genet.34.1.77. PMID 11092823. 
  3. ^ "Entrez Gene: TBP TATA box binding protein". 
  4. ^ McCulloch, V; Hardin P, Peng W, Ruppert J M, Lobo-Ruppert S M (Aug. 2000). "Alternatively spliced hBRF variants function at different RNA polymerase III promoters". EMBO J. (ENGLAND) 19 (15): 4134–43. doi:10.1093/emboj/19.15.4134. ISSN 0261-4189. PMID 10921893. 
  5. ^ Wang, Z; Roeder R G (Jul. 1995). "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. (UNITED STATES) 92 (15): 7026–30. ISSN 0027-8424. PMID 7624363. 
  6. ^ a b c d e Scully, R; Anderson S F, Chao D M, Wei W, Ye L, Young R A, Livingston D M, Parvin J D (May. 1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 94 (11): 5605–10. ISSN 0027-8424. PMID 9159119. 
  7. ^ Chicca, J J; Auble D T, Pugh B F (Mar. 1998). "Cloning and biochemical characterization of TAF-172, a human homolog of yeast Mot1". Mol. Cell. Biol. (UNITED STATES) 18 (3): 1701–10. ISSN 0270-7306. PMID 9488487. 
  8. ^ Metz, R; Bannister A J, Sutherland J A, Hagemeier C, O'Rourke E C, Cook A, Bravo R, Kouzarides T (Sep. 1994). "c-Fos-induced activation of a TATA-box-containing promoter involves direct contact with TATA-box-binding protein". Mol. Cell. Biol. (UNITED STATES) 14 (9): 6021–9. ISSN 0270-7306. PMID 8065335. 
  9. ^ Franklin, C C; McCulloch A V, Kraft A S (Feb. 1995). "In vitro association between the Jun protein family and the general transcription factors, TBP and TFIIB". Biochem. J. (ENGLAND) 305 ( Pt 3): 967–74. ISSN 0264-6021. PMID 7848298. 
  10. ^ Brendel, Carole; Gelman Laurent, Auwerx Johan (Jun. 2002). "Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism". Mol. Endocrinol. (United States) 16 (6): 1367–77. ISSN 0888-8809. PMID 12040021. 
  11. ^ Mariotti, M; De Benedictis L, Avon E, Maier J A (Aug. 2000). "Interaction between endothelial differentiation-related factor-1 and calmodulin in vitro and in vivo". J. Biol. Chem. (UNITED STATES) 275 (31): 24047–51. doi:10.1074/jbc.M001928200. ISSN 0021-9258. PMID 10816571. 
  12. ^ Kabe, Y; Goto M, Shima D, Imai T, Wada T, Morohashi K i, Shirakawa M, Hirose S, Handa H (Nov. 1999). "The role of human MBF1 as a transcriptional coactivator". J. Biol. Chem. (UNITED STATES) 274 (48): 34196–202. ISSN 0021-9258. PMID 10567391. 
  13. ^ Bushnell, David A; Westover Kenneth D, Davis Ralph E, Kornberg Roger D (Feb. 2004). "Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms". Science (United States) 303 (5660): 983–8. doi:10.1126/science.1090838. PMID 14963322. 
  14. ^ DeJong, J; Bernstein R, Roeder R G (Apr. 1995). "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. (UNITED STATES) 92 (8): 3313–7. ISSN 0027-8424. PMID 7724559. 
  15. ^ Langelier, M F; Forget D, Rojas A, Porlier Y, Burton Z F, Coulombe B (Oct. 2001). "Structural and functional interactions of transcription factor (TF) IIA with TFIIE and TFIIF in transcription initiation by RNA polymerase II". J. Biol. Chem. (United States) 276 (42): 38652–7. doi:10.1074/jbc.M106422200. ISSN 0021-9258. PMID 11509574. 
  16. ^ Ozer, J; Mitsouras K, Zerby D, Carey M, Lieberman P M (Jun. 1998). "Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding". J. Biol. Chem. (UNITED STATES) 273 (23): 14293–300. ISSN 0021-9258. PMID 9603936. 
  17. ^ Solow, S; Salunek M, Ryan R, Lieberman P M (May. 2001). "Taf(II) 250 phosphorylates human transcription factor IIA on serine residues important for TBP binding and transcription activity". J. Biol. Chem. (United States) 276 (19): 15886–92. doi:10.1074/jbc.M009385200. ISSN 0021-9258. PMID 11278496. 
  18. ^ Sun, X; Ma D, Sheldon M, Yeung K, Reinberg D (Oct. 1994). "Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription". Genes Dev. (UNITED STATES) 8 (19): 2336–48. ISSN 0890-9369. PMID 7958900. 
  19. ^ Ruppert, S; Tjian R (Nov. 1995). "Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation". Genes Dev. (UNITED STATES) 9 (22): 2747–55. ISSN 0890-9369. PMID 7590250. 
  20. ^ Malik, S; Guermah M, Roeder R G (Mar. 1998). "A dynamic model for PC4 coactivator function in RNA polymerase II transcription". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (5): 2192–7. ISSN 0027-8424. PMID 9482861. 
  21. ^ Léveillard, T; Wasylyk B (Dec. 1997). "The MDM2 C-terminal region binds to TAFII250 and is required for MDM2 regulation of the cyclin A promoter". J. Biol. Chem. (UNITED STATES) 272 (49): 30651–61. ISSN 0021-9258. PMID 9388200. 
  22. ^ Thut, C J; Goodrich J A, Tjian R (Aug. 1997). "Repression of p53-mediated transcription by MDM2: a dual mechanism". Genes Dev. (UNITED STATES) 11 (15): 1974–86. ISSN 0890-9369. PMID 9271120. 
  23. ^ Shetty, S; Takahashi T, Matsui H, Ayengar R, Raghow R (May. 1999). "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. (ENGLAND) 339 ( Pt 3): 751–8. ISSN 0264-6021. PMID 10215616. 
  24. ^ Zhang, H; Hu G, Wang H, Sciavolino P, Iler N, Shen M M, Abate-Shen C (May. 1997). "Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism". Mol. Cell. Biol. (UNITED STATES) 17 (5): 2920–32. ISSN 0270-7306. PMID 9111364. 
  25. ^ Zhang, H; Catron K M, Abate-Shen C (Mar. 1996). "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. (UNITED STATES) 93 (5): 1764–9. ISSN 0027-8424. PMID 8700832. 
  26. ^ a b c d e f g h i Bellorini, M; Lee D K, Dantonel J C, Zemzoumi K, Roeder R G, Tora L, Mantovani R (Jun. 1997). "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. (ENGLAND) 25 (11): 2174–81. ISSN 0305-1048. PMID 9153318. 
  27. ^ Seto, E; Usheva A, Zambetti G P, Momand J, Horikoshi N, Weinmann R, Levine A J, Shenk T (Dec. 1992). "Wild-type p53 binds to the TATA-binding protein and represses transcription". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 89 (24): 12028–32. ISSN 0027-8424. PMID 1465435. 
  28. ^ a b Cvekl, A; Kashanchi F, Brady J N, Piatigorsky J (Jun. 1999). "Pax-6 interactions with TATA-box-binding protein and retinoblastoma protein". Invest. Ophthalmol. Vis. Sci. (UNITED STATES) 40 (7): 1343–50. ISSN 0146-0404. PMID 10359315. 
  29. ^ Zwilling, S; Annweiler A, Wirth T (May. 1994). "The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP". Nucleic Acids Res. (ENGLAND) 22 (9): 1655–62. ISSN 0305-1048. PMID 8202368. 
  30. ^ Guermah, M; Malik S, Roeder R G (Jun. 1998). "Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-kappaB and Sp1". Mol. Cell. Biol. (UNITED STATES) 18 (6): 3234–44. ISSN 0270-7306. PMID 9584164. 
  31. ^ Schmitz, M L; Stelzer G, Altmann H, Meisterernst M, Baeuerle P A (Mar. 1995). "Interaction of the COOH-terminal transactivation domain of p65 NF-kappa B with TATA-binding protein, transcription factor IIB, and coactivators". J. Biol. Chem. (UNITED STATES) 270 (13): 7219–26. ISSN 0021-9258. PMID 7706261. 
  32. ^ Schulman, I G; Chakravarti D, Juguilon H, Romo A, Evans R M (Aug. 1995). "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. (UNITED STATES) 92 (18): 8288–92. ISSN 0027-8424. PMID 7667283. 
  33. ^ Siegert, J L; Robbins P D (Jan. 1999). "Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250". Mol. Cell. Biol. (UNITED STATES) 19 (1): 846–54. ISSN 0270-7306. PMID 9858607. 
  34. ^ a b c d Ruppert, S; Wang E H, Tjian R (Mar. 1993). "Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation". Nature (ENGLAND) 362 (6416): 175–9. doi:10.1038/362175a0. ISSN 0028-0836. PMID 7680771. 
  35. ^ O'Brien, T; Tjian R (May. 1998). "Functional analysis of the human TAFII250 N-terminal kinase domain". Mol. Cell (UNITED STATES) 1 (6): 905–11. ISSN 1097-2765. PMID 9660973. 
  36. ^ a b Mengus, G; May M, Jacq X, Staub A, Tora L, Chambon P, Davidson I (Apr. 1995). "Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID". EMBO J. (ENGLAND) 14 (7): 1520–31. ISSN 0261-4189. PMID 7729427. 
  37. ^ May, M; Mengus G, Lavigne A C, Chambon P, Davidson I (Jun. 1996). "Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors". EMBO J. (ENGLAND) 15 (12): 3093–104. ISSN 0261-4189. PMID 8670810. 
  38. ^ Hoffmann, A; Roeder R G (Jul. 1996). "Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation". J. Biol. Chem. (UNITED STATES) 271 (30): 18194–202. ISSN 0021-9258. PMID 8663456. 
  39. ^ a b c Pointud, Jean-Christophe; Mengus Gabrielle, Brancorsini Stefano, Monaco Lucia, Parvinen Martti, Sassone-Corsi Paolo, Davidson Irwin (May. 2003). "The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation". J. Cell. Sci. (England) 116 (Pt 9): 1847–58. ISSN 0021-9533. PMID 12665565. 
  40. ^ Tao, Y; Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder R G (Mar. 1997). "Specific interactions and potential functions of human TAFII100". J. Biol. Chem. (UNITED STATES) 272 (10): 6714–21. ISSN 0021-9258. PMID 9045704. 
  41. ^ Martinez, E; Palhan V B, Tjernberg A, Lymar E S, Gamper A M, Kundu T K, Chait B T, Roeder R G (Oct. 2001). "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. (United States) 21 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. ISSN 0270-7306. PMID 11564863. 

External links

Got something to say? Make a comment.
Your name
Your email address