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Gene Review

GTF2B  -  general transcription factor IIB

Homo sapiens

Synonyms: General transcription factor TFIIB, S300-II, TF2B, TFIIB, Transcription initiation factor IIB
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Disease relevance of GTF2B

  • The N-terminal domain of RAP74 (minimally aa 1 to 172) is sufficient to deliver pol II into a complex formed on the adenovirus major late promoter with the TATA-binding protein, TFIIB, and RAP30 [1].
  • Antibodies to basal transcription factors TATA-binding protein and TFIIB, but not TFIIIC, inhibited HTLV-I OTU transcription [2].
  • Transcriptional activators such as the herpes simplex virus VP16 facilitate this complex formation through conformational activation of TFIIB, a focal molecule of transcriptional initiation and activation [3].
  • When the general transcription factors (GTFs) were added in the assay, NC enhances NF-kappaB, Sp1, and TFIIB-induced HIV-1 LTR-directed RNA transcription [4].
  • In P19 embryonal carcinoma cells cotransfection of VDR and TFIIB cooperatively activated reporter transcription, while each factor alone gave very low to no activation [5].

High impact information on GTF2B

  • Mapping the location of TFIIB within the RNA polymerase II transcription preinitiation complex: a model for the structure of the PIC [6].
  • 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 [7].
  • Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein [8].
  • Abortive initiation assays revealed that TATA-binding protein, transcription factors TFIIB and TFIIF, and pol II were necessary and sufficient to form functional initiation complexes on both linear and supercoiled templates [9].
  • We have identified previously two transcription factors, COUP (chicken ovalbumin upstream promoter) and S300-II, from HeLa cell nuclear extracts [10].

Chemical compound and disease context of GTF2B

  • 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 [11].
  • Human transcription factor IIB (TFIIB) was discovered to be decreased on the 3rd day after the cells had been treated with retinoic acid and increased by phorbol 12-myristate 13-acetate, which stimulated the proliferation of human hepatocellular carcinoma cells [12].

Biological context of GTF2B

  • TFIIB contains a region with amino acid sequence similarity to a highly conserved region of prokaryotic sigma factors [13].
  • This "synthetic lethal" effect is not observed with E188A, suggesting that the previously described role of L189 in transcriptional activation may be related to its location on the DNA-binding surface and not to its interaction with TFIIB [14].
  • Furthermore, we demonstrate interaction of TFIIB with Sp1/Sp3 at the Sp1(I) site besides its association with EAR3 and the TATA-less core promoter region [15].
  • Conversely, the L189A mutation, which has the mildest effect on the interaction with TFIIB (10-fold), can abolish transcriptional activation and cell viability when combined with mutations on the DNA-binding surface [14].
  • According to solution and mutagenesis studies, the multiple domains of RAP30 and RAP74 bind PolII, TFIIB, TAF250 and DNA in interactions that are essential for transcription initiation and elongation [16].

Anatomical context of GTF2B

  • One serum, which strongly inhibited transcription in a cell-free system, was shown to contain antibodies directed against human TFIIB [17].
  • TFIIB-directed transcriptional activation by the orphan nuclear receptor hepatocyte nuclear factor 4 [18].
  • Likewise, GST-E2TA bound TFIID and TFIIB present in a nuclear extract from the human cervical cancer-derived cell line, HeLa [19].
  • In contrast, transfection of NIH 3T3 cells generated strong reporter activation by 1,25(OH)2D3 in the presence of VDR alone, and cotransfection of TFIIB led to specific dose-dependent repression of reporter activity [5].
  • Expressing amino acids 1-124 of human TFIIB (N-TFIIB) in COS-7 cells or in osteoblastic ROS17/2.8 cells effectively suppressed 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3)-induced transcription, but had no effect on basal or glucocorticoid-activated transcription [20].

Associations of GTF2B with chemical compounds

  • Purified S300-II is also required for steroid receptor-activated transcription [21].
  • Our findings suggest that there is a regulatory pathway controlling acetylation of TFIIB, and they link acetyl-CoA with basal gene transcription [22].
  • The first step involves AF-2-independent recruitment of TFIIB to the promoter complex; the second step is AF-2 dependent and entails entry of preinitiation complex components acting downstream of TFIIB [18].
  • We have shown that the human general transcriptional factor IB (TFIIB) auto-acetylates specifically at lysine 238 in the presence of acetyl coenzyme A in vitro [23].
  • The sugar residues protected from hydroxyl-radical cleavage by the TFIIB-TBP complex were mapped on the crystal-structure model of the TBP-DNA complex [24].

Physical interactions of GTF2B

  • Second, unlike yeast TBP, human TBP can use a shared surface to interact with two different TFIIB family members--TFIIB and Brf2--to initiate transcription by different RNA polymerases [25].
  • In vitro protein-protein interaction assays reveal that as observed with Drosophila TAFII40, hTAFII32 interacts with the C-terminal 39-amino acid activation domain of the acidic transactivator viral protein 16 (VP16) as well as with the general transcription factor TFIIB [26].
  • TFIIB binds to an overlapping region of RAP30, localized to amino acids 1-176 (amino acids 27-152 comprise a minimal binding region) [27].
  • The C-terminal region of RAP74 (amino acids 358-517) binds directly and independently to TFIIB [27].
  • RNA polymerase II-associated protein (RAP) 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding [27].

Regulatory relationships of GTF2B


Other interactions of GTF2B

  • 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 [30].
  • Mutants were tested for accurate transcriptional activity, RAP74 binding, and TFIIB binding [27].
  • Although S300-II does not bind DNA selectively, it stabilizes the binding of COUP-TF to its ciselement (Tsai, S. Y., Sagami, I., Wang, H., Tsai, M.-J., and O'Malley, B. W. (1987) Cell 50, 701-709) [21].
  • Interestingly, a truncated estrogen receptor construct containing only the N-terminal transcription activation function 1 did not interact with S300-II/TFIIB in our assay, revealing that individual transcription activation functions of a single steroid hormone receptor may contact different targets [21].
  • However, in the reverse titration, with very high mole ratios of HMG-1 present, TFIIB is not dissociated off and a complex is formed that contains all factors [31].

Analytical, diagnostic and therapeutic context of GTF2B


  1. Functions of the N- and C-terminal domains of human RAP74 in transcriptional initiation, elongation, and recycling of RNA polymerase II. Lei, L., Ren, D., Finkelstein, A., Burton, Z.F. Mol. Cell. Biol. (1998) [Pubmed]
  2. Transcription of the human T-cell lymphotropic virus type I promoter by an alpha-amanitin-resistant polymerase. Piras, G., Kashanchi, F., Radonovich, M.F., Duvall, J.F., Brady, J.N. J. Virol. (1994) [Pubmed]
  3. FRET evidence for a conformational change in TFIIB upon TBP-DNA binding. Zheng, L., Hoeflich, K.P., Elsby, L.M., Ghosh, M., Roberts, S.G., Ikura, M. Eur. J. Biochem. (2004) [Pubmed]
  4. Enhancement of the basal-level activity of HIV-1 long terminal repeat by HIV-1 nucleocapsid protein. Zhang, J.L., Sharma, P.L., Crumpacker, C.S. Virology (2000) [Pubmed]
  5. Transcription factor TFIIB and the vitamin D receptor cooperatively activate ligand-dependent transcription. Blanco, J.C., Wang, I.M., Tsai, S.Y., Tsai, M.J., O'Malley, B.W., Jurutka, P.W., Haussler, M.R., Ozato, K. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  6. Mapping the location of TFIIB within the RNA polymerase II transcription preinitiation complex: a model for the structure of the PIC. Chen, H.T., Hahn, S. Cell (2004) [Pubmed]
  7. 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]
  8. Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein. Bagby, S., Kim, S., Maldonado, E., Tong, K.I., Reinberg, D., Ikura, M. Cell (1995) [Pubmed]
  9. Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II. Goodrich, J.A., Tjian, R. Cell (1994) [Pubmed]
  10. Interactions between a DNA-binding transcription factor (COUP) and a non-DNA binding factor (S300-II). Tsai, S.Y., Sagami, I., Wang, H., Tsai, M.J., O'Malley, B.W. Cell (1987) [Pubmed]
  11. 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]
  12. Transcriptional regulation of human transcription factor IIB in SMMC-7721 human hepatocellular carcinoma cells by all-trans-retinoic acid and phorbol 12-myristate 13-acetate. Chen, C., Yin, X., Zhou, D., Shen, Z., Chi, C., Gu, J. J. Cancer Res. Clin. Oncol. (1998) [Pubmed]
  13. Sequence of general transcription factor TFIIB and relationships to other initiation factors. Malik, S., Hisatake, K., Sumimoto, H., Horikoshi, M., Roeder, R.G. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  14. A severely defective TATA-binding protein-TFIIB interaction does not preclude transcriptional activation in vivo. Lee, M., Struhl, K. Mol. Cell. Biol. (1997) [Pubmed]
  15. Repression of the luteinizing hormone receptor gene promoter by cross talk among EAR3/COUP-TFI, Sp1/Sp3, and TFIIB. Zhang, Y., Dufau, M.L. Mol. Cell. Biol. (2003) [Pubmed]
  16. Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution. Gaiser, F., Tan, S., Richmond, T.J. J. Mol. Biol. (2000) [Pubmed]
  17. Identification of human autoantibodies to transcription factor IIB. Abendroth, F.D., Peterson, S.R., Galman, M., Suwa, A., Hardin, J.A., Dynan, W.S. Nucleic Acids Res. (1995) [Pubmed]
  18. TFIIB-directed transcriptional activation by the orphan nuclear receptor hepatocyte nuclear factor 4. Malik, S., Karathanasis, S.K. Mol. Cell. Biol. (1996) [Pubmed]
  19. Bovine papillomavirus type 1 E2 transcriptional regulators directly bind two cellular transcription factors, TFIID and TFIIB. Rank, N.M., Lambert, P.F. J. Virol. (1995) [Pubmed]
  20. The N-terminal domain of transcription factor IIB is required for direct interaction with the vitamin D receptor and participates in vitamin D-mediated transcription. Masuyama, H., Jefcoat, S.C., MacDonald, P.N. Mol. Endocrinol. (1997) [Pubmed]
  21. Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II). Ing, N.H., Beekman, J.M., Tsai, S.Y., Tsai, M.J., O'Malley, B.W. J. Biol. Chem. (1992) [Pubmed]
  22. Transcription factor IIB acetylates itself to regulate transcription. Choi, C.H., Hiromura, M., Usheva, A. Nature (2003) [Pubmed]
  23. Auto-acetylation of transcription factors as a control mechanism in gene expression. Choi, C.H., Burton, Z.F., Usheva, A. Cell Cycle (2004) [Pubmed]
  24. Model for binding of transcription factor TFIIB to the TBP-DNA complex. Lee, S., Hahn, S. Nature (1995) [Pubmed]
  25. A shared surface of TBP directs RNA polymerase II and III transcription via association with different TFIIB family members. Zhao, X., Schramm, L., Hernandez, N., Herr, W. Mol. Cell (2003) [Pubmed]
  26. Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. Klemm, R.D., Goodrich, J.A., Zhou, S., Tjian, R. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  27. RNA polymerase II-associated protein (RAP) 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding. Fang, S.M., Burton, Z.F. J. Biol. Chem. (1996) [Pubmed]
  28. Proline-rich activator CTF1 targets the TFIIB assembly step during transcriptional activation. Kim, T.K., Roeder, R.G. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  29. Simian virus 40 large T antigen interacts with human TFIIB-related factor and small nuclear RNA-activating protein complex for transcriptional activation of TATA-containing polymerase III promoters. Damania, B., Mital, R., Alwine, J.C. Mol. Cell. Biol. (1998) [Pubmed]
  30. DNA topology and a minimal set of basal factors for transcription by RNA polymerase II. Parvin, J.D., Sharp, P.A. Cell (1993) [Pubmed]
  31. Influence of HMG-1 and adenovirus oncoprotein E1A on early stages of transcriptional preinitiation complex assembly. Lu, W., Peterson, R., Dasgupta, A., Scovell, W.M. J. Biol. Chem. (2000) [Pubmed]
  32. Functional dissection of TFIIB domains required for TFIIB-TFIID-promoter complex formation and basal transcription activity. Hisatake, K., Roeder, R.G., Horikoshi, M. Nature (1993) [Pubmed]
  33. Oestrogen receptor facilitates the formation of preinitiation complex assembly: involvement of the general transcription factor TFIIB. Sabbah, M., Kang, K.I., Tora, L., Redeuilh, G. Biochem. J. (1998) [Pubmed]
  34. Evidence that the Tfg1/Tfg2 dimer interface of TFIIF lies near the active center of the RNA polymerase II initiation complex. Freire-Picos, M.A., Krishnamurthy, S., Sun, Z.W., Hampsey, M. Nucleic Acids Res. (2005) [Pubmed]
  35. Eukaryotic activators function during multiple steps of preinitiation complex assembly. Choy, B., Green, M.R. Nature (1993) [Pubmed]
  36. Assembly of the isomerized TFIIA--TFIID--TATA ternary complex is necessary and sufficient for gene activation. Chi, T., Carey, M. Genes Dev. (1996) [Pubmed]
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