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Gene Review

TBP  -  TATA box binding protein

Homo sapiens

Synonyms: GTF2D, GTF2D1, HDL4, SCA17, TATA sequence-binding protein, ...
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Disease relevance of TBP

  • We conclude that a non-classical transcriptional mechanism combats an anticellular action of poliovirus, through a TBP-free TAF-containing complex and GCN5 [1].
  • In contrast, the TBP-containing complex TFIIIB restores adenovirus VAI but not human U6 transcription in RB-treated extracts, suggesting that TFIIIB is important for RB regulation of tRNA-like genes [2].
  • We have previously reported the direct physical interaction between the human immunodeficiency virus (HIV) type I Tat protein and the basal transcription factor TBP/TFIID [3].
  • Susceptibility to the autoimmune disease type 1 diabetes has been linked to human chromosome 6q27 and, moreover, recently associated with one of the genes in the region, TATA box-binding protein (TBP) [4].
  • To further dissect the contribution of individual TAF(II) subunits to mammalian TFIID function, we employed a vaccinia virus-based protein expression system to study protein-protein interactions and complex assembly [5].

Psychiatry related information on TBP


High impact information on TBP

  • Together, TBP and the TAFIIS direct assembly of the transcription machinery and play critical regulatory roles in eukaryotic gene expression [11].
  • TFIIB greatly accelerates formation of a bent TFIIB-TBP-TATA box complex, and the inhibitory DNA binding surface of TBP contributes to the cooperativity of binding to TFIIB [12].
  • A regulated two-step mechanism of TBP binding to DNA: a solvent-exposed surface of TBP inhibits TATA box recognition [12].
  • By mutagenesis, we have discovered a solvent-exposed surface of the structured TBP core domain that is important for inhibition of the DNA binding and DNA-bending activities of full-length wild-type TBP [12].
  • First, the enhanceosome recruits the SWI/SNF chromatin-remodeling complex that modifies the nucleosome to allow binding of TBP [13].

Chemical compound and disease context of TBP

  • We show that alanine substitution mutations in a single loop of TBP can disrupt its association in vitro with the activation domains of the herpes simplex virus activator VP16 and of the human tumor suppressor protein p53; these mutations do not, however, disrupt the transcriptional response of TBP to either activation domain in vivo [14].
  • Indeed, DNase I footprinting patterns reveal that TBP protects equally 4 nucleotides upstream and 6 nucleotides downstream from the A-T (at position -29 of the noncoding strand) of the adenovirus major late promoter and from the G-G of a cisplatin-induced 1,2-d(GpG) cross-link [15].
  • The acidic activation domain of the Epstein-Barr virus transcription factor R interacts in vitro with both TBP and TFIIB and is cell-specifically potentiated by a proline-rich region [16].
  • Coordinate regulation of RARgamma2, TBP, and TAFII135 by targeted proteolysis during retinoic acid-induced differentiation of F9 embryonal carcinoma cells [17].
  • Surprisingly, the HIV promoter in unactivated Jurkat T cells is partially occupied and carries Mediator containing the CDK8 repressive module, TFIID and RNAP II that is hypophosphorylated and confined to the promoter region [18].

Biological context of TBP

  • This largest TAF may therefore play a central role in TFIID assembly by interacting with both TBP and other TAFs, as well as serving to link the control of transcription to the cell cycle [19].
  • Computer-assisted 3D structural analysis reveals a remarkable similarity between the structure of the TATA box as found in its TBP complex and that of either platinated or UV-damaged oligonucleotides [20].
  • Regulation of transcription initiation by RNA polymerase II requires TFIID, a multisubunit complex composed of the TATA binding protein (TBP) and at least seven tightly associated factors (TAFs) [21].
  • Thus, cisplatin-treated or UV-irradiated DNA could be used as a competing binding site which may lure TBP/TFIID away from its normal promoter sequence, partially explaining the phenomenon of DNA damage-induced inhibition of RNA synthesis [20].
  • A mechanism for repression of class II gene transcription through specific binding of NC2 to TBP-promoter complexes via heterodimeric histone fold domains [22].

Anatomical context of TBP

  • Consistent with an involvement of damaged DNA-specific binding of TBP in inhibiting transcription, we find that microinjection of additional TBP in living human fibroblasts alleviates the reduction in RNA synthesis after UV irradiation [20].
  • In eukaryotic cells the TATA-binding protein (TBP) associates with other proteins known as TBP-associated factors (TAFs) to form multisubunit transcription factors important for gene expression by all three nuclear RNA polymerases [23].
  • We hypothesize that EDF-1 serves two main functions in endothelial cells as follows: (i) to bind CaM in the cytosol at physiologic concentrations of Ca(2+) and (ii) to act in the nucleus as a transcriptional coactivator through its binding to TBP [24].
  • Co-transfection of human TBP and Oct2 expression vectors into B cells resulted in a synergistic activation of an octamer motif containing promoter [25].
  • Coimmunoprecipitation of transiently expressed TBP in HeLa cells demonstrated that HSF1 AD2 and AD1+AD2 are able to bind TBP in vivo [26].

Associations of TBP with chemical compounds

  • Cisplatin- and UV-damaged DNA lure the basal transcription factor TFIID/TBP [20].
  • The effect of hTAFII(28) on RXR AF-2 activities did not appear to require direct RXR-TAFII(28) interactions, but correlated with the ability of hTAFII(28) to interact with TBP [27].
  • Taf(II) 250 phosphorylates human transcription factor IIA on serine residues important for TBP binding and transcription activity [28].
  • ZNF76 is sumoylated by PIAS1 at lysine 411, which is in the minimal TBP-interacting region [29].
  • Significantly, the binding of TBP was modulated by induced folding of the TAD with TMAO [30].

Physical interactions of TBP

  • Negative co-factor 2 (NC2) regulates transcription of the class II genes through binding to TFIID and inhibition of pre-initiation complex formation [22].
  • Our results show that recombinant GR AF1 acquires a significant amount of helical content when it interacts with TBP [31].
  • By generating complexes smaller than mini-SNAP(c), we have identified a 50-amino-acid region within SNAP190 that is (i) required for cooperative binding with TBP in the context of mini-SNAP(c) and (ii) sufficient for cooperative binding with TBP when fused to a heterologous DNA binding domain [32].
  • TFIID and TFTC complexes in which both TAF9 and TAF9b are present exist [33].
  • This complex prevents TFIIB binding to TBP and consequently blocks formation of the preinitiation complex [34].

Enzymatic interactions of TBP

  • Dr1 is phosphorylated in vivo and phosphorylation of Dr1 affected its interaction with TBP [35].
  • Further analyses using deletion mutants of RAP74 revealed that amino acid residues 206-256 are phosphorylated by the TFIID fraction [36].

Regulatory relationships of TBP

  • TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain [31].
  • These results suggest a dynamic TFIID structure in which the switch from a basal hTAF(II)-enhanced repression state to an activator-mediated activated state on a promoter may be mediated in part through activator or coactivator interactions with hTAF(II)135 [37].
  • Therefore, the SNAP190 Myb domain functions both to specifically recognize the proximal sequence element present in the core promoters of human snRNA genes and to stimulate TBP recognition of the neighboring TATA box present in human U6 snRNA promoters [38].
  • Moreover, IFN-stimulated transcription was resistant to poliovirus-targeted degradation by TBP, and continued despite host-cell transcriptional shutoff during poliovirus infection [1].
  • Human U6 small nuclear RNA (snRNA) gene transcription by RNA polymerase III requires cooperative promoter binding involving the snRNA-activating protein complex (SNAP(c)) and the TATA-box binding protein (TBP) [38].

Other interactions of TBP

  • When only TBP, TFIIB, and pol II were present in the reaction, the more negatively supercoiled the IgH template DNA was, the more active the transcription [39].
  • Our findings suggest that targeted histone acetylation at specific promoters by TAF(II)250 may be involved in mechanisms by which TFIID gains access to transcriptionally repressed chromatin [40].
  • Determination of the crystal structure of the human TBP-associated factor (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel histone-like pair in the TFIID complex [41].
  • We report for the first time the cloning of a complete cDNA encoding the human TFIID subunit hTAF(II)135 (hTAF(II)130) [42].
  • Similarly to known TFTC (TBP-free TAF(II)-containing)-type HAT complexes (hTFTC, hPCAF, and hSTAGA), TRRP directly interacted with liganded ER alpha, or other NRs [43].

Analytical, diagnostic and therapeutic context of TBP

  • Using a combination of protein affinity chromatography and cotransfection and immunoprecipitation assays, we have identified a series of in vitro and intracellular interactions among the novel hTAFIIs and between the novel hTAFIIs and hTAFII30 or TBP [44].
  • Using epitope-tagging and immunoprecipitation experiments, we demonstrate that these genes encode bona fide TAF proteins and show that the yeast TBP-TAFII complex is minimally composed of TBP and seven distinct yTAFII proteins ranging in size from M(r) = 150,000 to M(r) = 25,000 [45].
  • Proteolysis significantly stimulated TFIIA-TFIID-TATA binding in both electrophoresis mobility shift assay and DNase I footprinting but had little effect on complexes formed with TBP [46].
  • Chromatin immunoprecipitation experiments suggest that ZNF76 prevents TBP from occupying the endogenous p21 promoter [29].
  • The cAMP/cAMP-dependent protein kinase pathway mediates the effects on CBP and TBP, whereas a cAMP-independent pathway is the major transducer for the effects on p65 nuclear translocation [47].


  1. IFN-Stimulated transcription through a TBP-free acetyltransferase complex escapes viral shutoff. Paulson, M., Press, C., Smith, E., Tanese, N., Levy, D.E. Nat. Cell Biol. (2002) [Pubmed]
  2. The retinoblastoma tumor suppressor protein targets distinct general transcription factors to regulate RNA polymerase III gene expression. Hirsch, H.A., Gu, L., Henry, R.W. Mol. Cell. Biol. (2000) [Pubmed]
  3. Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex. Kashanchi, F., Khleif, S.N., Duvall, J.F., Sadaie, M.R., Radonovich, M.F., Cho, M., Martin, M.A., Chen, S.Y., Weinmann, R., Brady, J.N. J. Virol. (1996) [Pubmed]
  4. No evidence for association of the TATA-box binding protein glutamine repeat sequence or the flanking chromosome 6q27 region with type 1 diabetes. Payne, F., Smyth, D.J., Pask, R., Cooper, J.D., Masters, J., Wang, W.Y., Godfrey, L.M., Bowden, G., Szeszko, J., Smink, L.J., Lam, A.C., Burren, O., Walker, N.M., Nutland, S., Rance, H., Undlien, D.E., Rønningen, K.S., Guja, C., Ionescu-Tîrgovişte, C., Todd, J.A., Twells, R.C. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  5. Assembly of partial TFIID complexes in mammalian cells reveals distinct activities associated with individual TATA box-binding protein-associated factors. Furukawa, T., Tanese, N. J. Biol. Chem. (2000) [Pubmed]
  6. TBP, a polyglutamine tract containing protein, accumulates in Alzheimer's disease. Reid, S.J., van Roon-Mom, W.M., Wood, P.C., Rees, M.I., Owen, M.J., Faull, R.L., Dragunow, M., Snell, R.G. Brain Res. Mol. Brain Res. (2004) [Pubmed]
  7. Huntington's disease-like phenotype due to trinucleotide repeat expansions in the TBP and JPH3 genes. Stevanin, G., Fujigasaki, H., Lebre, A.S., Camuzat, A., Jeannequin, C., Dode, C., Takahashi, J., San, C., Bellance, R., Brice, A., Durr, A. Brain (2003) [Pubmed]
  8. CAG repeat expansion in the TATA box-binding protein gene causes autosomal dominant cerebellar ataxia. Fujigasaki, H., Martin, J.J., De Deyn, P.P., Camuzat, A., Deffond, D., Stevanin, G., Dermaut, B., Van Broeckhoven, C., Dürr, A., Brice, A. Brain (2001) [Pubmed]
  9. Applying the Theory of Planned Behavior to healthy eating behaviors in urban Native American youth. Fila, S.A., Smith, C. The international journal of behavioral nutrition and physical activity [electronic resource]. (2006) [Pubmed]
  10. Small de novo duplication in the repeat region of the TATA-box-binding protein gene manifest with a phenotype similar to variant Creutzfeldt-Jakob disease. Shatunov, A., Fridman, E.A., Pagan, F.I., Leib, J., Singleton, A., Hallett, M., Goldfarb, L.G. Clin. Genet. (2004) [Pubmed]
  11. Biochemistry and structural biology of transcription factor IID (TFIID). Burley, S.K., Roeder, R.G. Annu. Rev. Biochem. (1996) [Pubmed]
  12. A regulated two-step mechanism of TBP binding to DNA: a solvent-exposed surface of TBP inhibits TATA box recognition. Zhao, X., Herr, W. Cell (2002) [Pubmed]
  13. Nucleosome sliding via TBP DNA binding in vivo. Lomvardas, S., Thanos, D. Cell (2001) [Pubmed]
  14. The ability to associate with activation domains in vitro is not required for the TATA box-binding protein to support activated transcription in vivo. Tansey, W.P., Herr, W. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  15. TATA binding protein discriminates between different lesions on DNA, resulting in a transcription decrease. Coin, F., Frit, P., Viollet, B., Salles, B., Egly, J.M. Mol. Cell. Biol. (1998) [Pubmed]
  16. The acidic activation domain of the Epstein-Barr virus transcription factor R interacts in vitro with both TBP and TFIIB and is cell-specifically potentiated by a proline-rich region. Manet, E., Allera, C., Gruffat, H., Mikaelian, I., Rigolet, A., Sergeant, A. Gene Expr. (1993) [Pubmed]
  17. Coordinate regulation of RARgamma2, TBP, and TAFII135 by targeted proteolysis during retinoic acid-induced differentiation of F9 embryonal carcinoma cells. Perletti, L., Kopf, E., Carré, L., Davidson, I. BMC Mol. Biol. (2001) [Pubmed]
  18. Recruitment of TFIIH to the HIV LTR is a rate-limiting step in the emergence of HIV from latency. Kim, Y.K., Bourgeois, C.F., Pearson, R., Tyagi, M., West, M.J., Wong, J., Wu, S.Y., Chiang, C.M., Karn, J. EMBO J. (2006) [Pubmed]
  19. Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation. Ruppert, S., Wang, E.H., Tjian, R. Nature (1993) [Pubmed]
  20. Cisplatin- and UV-damaged DNA lure the basal transcription factor TFIID/TBP. Vichi, P., Coin, F., Renaud, J.P., Vermeulen, W., Hoeijmakers, J.H., Moras, D., Egly, J.M. EMBO J. (1997) [Pubmed]
  21. Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal conserved interactions with other subunits of TFIID. Weinzierl, R.O., Ruppert, S., Dynlacht, B.D., Tanese, N., Tjian, R. EMBO J. (1993) [Pubmed]
  22. A mechanism for repression of class II gene transcription through specific binding of NC2 to TBP-promoter complexes via heterodimeric histone fold domains. Goppelt, A., Stelzer, G., Lottspeich, F., Meisterernst, M. EMBO J. (1996) [Pubmed]
  23. Yeast homologues of higher eukaryotic TFIID subunits. Moqtaderi, Z., Yale, J.D., Struhl, K., Buratowski, S. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  24. Interaction between endothelial differentiation-related factor-1 and calmodulin in vitro and in vivo. Mariotti, M., De Benedictis, L., Avon, E., Maier, J.A. J. Biol. Chem. (2000) [Pubmed]
  25. The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP. Zwilling, S., Annweiler, A., Wirth, T. Nucleic Acids Res. (1994) [Pubmed]
  26. Potential targets for HSF1 within the preinitiation complex. Yuan, C.X., Gurley, W.B. Cell Stress Chaperones (2000) [Pubmed]
  27. Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors. May, M., Mengus, G., Lavigne, A.C., Chambon, P., Davidson, I. EMBO J. (1996) [Pubmed]
  28. Taf(II) 250 phosphorylates human transcription factor IIA on serine residues important for TBP binding and transcription activity. Solow, S., Salunek, M., Ryan, R., Lieberman, P.M. J. Biol. Chem. (2001) [Pubmed]
  29. ZNF76, a novel transcriptional repressor targeting TATA-binding protein, is modulated by sumoylation. Zheng, G., Yang, Y.C. J. Biol. Chem. (2004) [Pubmed]
  30. Induced alpha-helix structure in the aryl hydrocarbon receptor transactivation domain modulates protein-protein interactions. Watt, K., Jess, T.J., Kelly, S.M., Price, N.C., McEwan, I.J. Biochemistry (2005) [Pubmed]
  31. TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain. Kumar, R., Volk, D.E., Li, J., Lee, J.C., Gorenstein, D.G., Thompson, E.B. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  32. Redundant cooperative interactions for assembly of a human U6 transcription initiation complex. Ma, B., Hernandez, N. Mol. Cell. Biol. (2002) [Pubmed]
  33. TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping roles with TAF9. Frontini, M., Soutoglou, E., Argentini, M., Bole-Feysot, C., Jost, B., Scheer, E., Tora, L. Mol. Cell. Biol. (2005) [Pubmed]
  34. The high mobility group protein HMG1 can reversibly inhibit class II gene transcription by interaction with the TATA-binding protein. Ge, H., Roeder, R.G. J. Biol. Chem. (1994) [Pubmed]
  35. Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription. Inostroza, J.A., Mermelstein, F.H., Ha, I., Lane, W.S., Reinberg, D. Cell (1992) [Pubmed]
  36. Cell-cycle-dependent phosphorylation of the basal transcription factor RAP74. Yonaha, M., Tsuchiya, T., Yasukochi, Y. FEBS Lett. (1997) [Pubmed]
  37. Positive and negative TAF(II) functions that suggest a dynamic TFIID structure and elicit synergy with traps in activator-induced transcription. Guermah, M., Tao, Y., Roeder, R.G. Mol. Cell. Biol. (2001) [Pubmed]
  38. The small nuclear RNA-activating protein 190 Myb DNA binding domain stimulates TATA box-binding protein-TATA box recognition. Hinkley, C.S., Hirsch, H.A., Gu, L., LaMere, B., Henry, R.W. J. Biol. Chem. (2003) [Pubmed]
  39. DNA topology and a minimal set of basal factors for transcription by RNA polymerase II. Parvin, J.D., Sharp, P.A. Cell (1993) [Pubmed]
  40. The TAF(II)250 subunit of TFIID has histone acetyltransferase activity. Mizzen, C.A., Yang, X.J., Kokubo, T., Brownell, J.E., Bannister, A.J., Owen-Hughes, T., Workman, J., Wang, L., Berger, S.L., Kouzarides, T., Nakatani, Y., Allis, C.D. Cell (1996) [Pubmed]
  41. Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family. Birck, C., Poch, O., Romier, C., Ruff, M., Mengus, G., Lavigne, A.C., Davidson, I., Moras, D. Cell (1998) [Pubmed]
  42. Human TAF(II)135 potentiates transcriptional activation by the AF-2s of the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian cells. Mengus, G., May, M., Carré, L., Chambon, P., Davidson, I. Genes Dev. (1997) [Pubmed]
  43. Nuclear receptor function requires a TFTC-type histone acetyl transferase complex. Yanagisawa, J., Kitagawa, H., Yanagida, M., Wada, O., Ogawa, S., Nakagomi, M., Oishi, H., Yamamoto, Y., Nagasawa, H., McMahon, S.B., Cole, M.D., Tora, L., Takahashi, N., Kato, S. Mol. Cell (2002) [Pubmed]
  44. Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID. Mengus, G., May, M., Jacq, X., Staub, A., Tora, L., Chambon, P., Davidson, I. EMBO J. (1995) [Pubmed]
  45. Identification and characterization of a TFIID-like multiprotein complex from Saccharomyces cerevisiae. Poon, D., Bai, Y., Campbell, A.M., Bjorklund, S., Kim, Y.J., Zhou, S., Kornberg, R.D., Weil, P.A. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  46. Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding. Ozer, J., Mitsouras, K., Zerby, D., Carey, M., Lieberman, P.M. J. Biol. Chem. (1998) [Pubmed]
  47. Vasoactive intestinal peptide and pituitary adenylate cyclase-activating polypeptide inhibit nuclear factor-kappa B-dependent gene activation at multiple levels in the human monocytic cell line THP-1. Delgado, M., Ganea, D. J. Biol. Chem. (2001) [Pubmed]
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