Skip to main content
PMC home page
The EMBO Journal logoLink to The EMBO Journal
. 1994 Jan 15;13(2):435–445. doi: 10.1002/j.1460-2075.1994.tb06278.x

A TATA sequence-dependent transcriptional repressor activity associated with mammalian transcription factor IIA.

T Aso 1, H Serizawa 1, R C Conaway 1, J W Conaway 1
PMCID: PMC394826  PMID: 8313889

Abstract

In the process of characterizing cellular proteins that modulate basal transcription by RNA polymerase II, we identified a novel repressor activity specific for promoters containing consensus TATA boxes. This activity strongly represses TATA-binding protein (TBP)-dependent transcription initiation from core promoter elements containing a consensus TATA sequence, but activates TBP-dependent transcription from core promoter elements lacking a consensus TATA sequence. Purification of this activity to near homogeneity from rat liver nuclear extracts led to the surprising discovery that it co-purifies closely with mammalian transcription factor IIA (TFIIA). The close association of TATA sequence-dependent transcriptional repressor activity with TFIIA adds a new and unexpected dimension to the already complex picture of this factor's function in transcription by RNA polymerase II.

Full text

PDF

Images in this article

436Image
on p.436
437Image
on p.437
438Image
on p.438
439Image
on p.439
440Image
on p.440
441Image
on p.441
441Image
on p.441

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aso T., Vasavada H. A., Kawaguchi T., Germino F. J., Ganguly S., Kitajima S., Weissman S. M., Yasukochi Y. Characterization of cDNA for the large subunit of the transcription initiation factor TFIIF. Nature. 1992 Jan 30;355(6359):461–464. doi: 10.1038/355461a0. [DOI] [PubMed] [Google Scholar]
  2. Berger S. L., Cress W. D., Cress A., Triezenberg S. J., Guarente L. Selective inhibition of activated but not basal transcription by the acidic activation domain of VP16: evidence for transcriptional adaptors. Cell. 1990 Jun 29;61(7):1199–1208. doi: 10.1016/0092-8674(90)90684-7. [DOI] [PubMed] [Google Scholar]
  3. Brou C., Chaudhary S., Davidson I., Lutz Y., Wu J., Egly J. M., Tora L., Chambon P. Distinct TFIID complexes mediate the effect of different transcriptional activators. EMBO J. 1993 Feb;12(2):489–499. doi: 10.1002/j.1460-2075.1993.tb05681.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Buratowski S., Hahn S., Guarente L., Sharp P. A. Five intermediate complexes in transcription initiation by RNA polymerase II. Cell. 1989 Feb 24;56(4):549–561. doi: 10.1016/0092-8674(89)90578-3. [DOI] [PubMed] [Google Scholar]
  5. Buratowski S., Hahn S., Sharp P. A., Guarente L. Function of a yeast TATA element-binding protein in a mammalian transcription system. Nature. 1988 Jul 7;334(6177):37–42. doi: 10.1038/334037a0. [DOI] [PubMed] [Google Scholar]
  6. Buratowski S., Zhou H. Transcription factor IID mutants defective for interaction with transcription factor IIA. Science. 1992 Feb 28;255(5048):1130–1132. doi: 10.1126/science.1546314. [DOI] [PubMed] [Google Scholar]
  7. Carthew R. W., Chodosh L. A., Sharp P. A. An RNA polymerase II transcription factor binds to an upstream element in the adenovirus major late promoter. Cell. 1985 Dec;43(2 Pt 1):439–448. doi: 10.1016/0092-8674(85)90174-6. [DOI] [PubMed] [Google Scholar]
  8. Cavallini B., Faus I., Matthes H., Chipoulet J. M., Winsor B., Egly J. M., Chambon P. Cloning of the gene encoding the yeast protein BTF1Y, which can substitute for the human TATA box-binding factor. Proc Natl Acad Sci U S A. 1989 Dec;86(24):9803–9807. doi: 10.1073/pnas.86.24.9803. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Conaway J. W., Bond M. W., Conaway R. C. An RNA polymerase II transcription system from rat liver. Purification of an essential component. J Biol Chem. 1987 Jun 15;262(17):8293–8297. [PubMed] [Google Scholar]
  10. Conaway J. W., Bradsher J. N., Conaway R. C. Mechanism of assembly of the RNA polymerase II preinitiation complex. Transcription factors delta and epsilon promote stable binding of the transcription apparatus to the initiator element. J Biol Chem. 1992 May 15;267(14):10142–10148. [PubMed] [Google Scholar]
  11. Conaway J. W., Conaway R. C. A multisubunit transcription factor essential for accurate initiation by RNA polymerase II. J Biol Chem. 1989 Feb 5;264(4):2357–2362. [PubMed] [Google Scholar]
  12. Conaway J. W., Hanley J. P., Garrett K. P., Conaway R. C. Transcription initiated by RNA polymerase II and transcription factors from liver. Structure and action of transcription factors epsilon and tau. J Biol Chem. 1991 Apr 25;266(12):7804–7811. [PubMed] [Google Scholar]
  13. Conaway J. W., Reines D., Conaway R. C. Transcription initiated by RNA polymerase II and purified transcription factors from liver. Cooperative action of transcription factors tau and epsilon in initial complex formation. J Biol Chem. 1990 May 5;265(13):7552–7558. [PMC free article] [PubMed] [Google Scholar]
  14. Conaway J. W., Travis E., Conaway R. C. Transcription initiated by RNA polymerase II and purified transcription factors from liver. A complex set of promoter sequences governs formation of the initial complex. J Biol Chem. 1990 May 5;265(13):7564–7569. [PubMed] [Google Scholar]
  15. Conaway R. C., Conaway J. W. General initiation factors for RNA polymerase II. Annu Rev Biochem. 1993;62:161–190. doi: 10.1146/annurev.bi.62.070193.001113. [DOI] [PubMed] [Google Scholar]
  16. Conaway R. C., Conaway J. W. Transcription initiated by RNA polymerase II and purified transcription factors from liver. Transcription factors alpha, beta gamma, and delta promote formation of intermediates in assembly of the functional preinitiation complex. J Biol Chem. 1990 May 5;265(13):7559–7563. [PubMed] [Google Scholar]
  17. Cortes P., Flores O., Reinberg D. Factors involved in specific transcription by mammalian RNA polymerase II: purification and analysis of transcription factor IIA and identification of transcription factor IIJ. Mol Cell Biol. 1992 Jan;12(1):413–421. doi: 10.1128/mcb.12.1.413. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Coulombe B., Killeen M., Liljelund P., Honda B., Xiao H., Ingles C. J., Greenblatt J. Identification of three mammalian proteins that bind to the yeast TATA box protein TFIID. Gene Expr. 1992;2(2):99–110. [PMC free article] [PubMed] [Google Scholar]
  19. Davison B. L., Egly J. M., Mulvihill E. R., Chambon P. Formation of stable preinitiation complexes between eukaryotic class B transcription factors and promoter sequences. Nature. 1983 Feb 24;301(5902):680–686. doi: 10.1038/301680a0. [DOI] [PubMed] [Google Scholar]
  20. Dynlacht B. D., Hoey T., Tjian R. Isolation of coactivators associated with the TATA-binding protein that mediate transcriptional activation. Cell. 1991 Aug 9;66(3):563–576. doi: 10.1016/0092-8674(81)90019-2. [DOI] [PubMed] [Google Scholar]
  21. Egly J. M., Miyamoto N. G., Moncollin V., Chambon P. Is actin a transcription initiation factor for RNA polymerase B? EMBO J. 1984 Oct;3(10):2363–2371. doi: 10.1002/j.1460-2075.1984.tb02141.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Finkelstein A., Kostrub C. F., Li J., Chavez D. P., Wang B. Q., Fang S. M., Greenblatt J., Burton Z. F. A cDNA encoding RAP74, a general initiation factor for transcription by RNA polymerase II. Nature. 1992 Jan 30;355(6359):464–467. doi: 10.1038/355464a0. [DOI] [PubMed] [Google Scholar]
  23. Flanagan P. M., Kelleher R. J., 3rd, Sayre M. H., Tschochner H., Kornberg R. D. A mediator required for activation of RNA polymerase II transcription in vitro. Nature. 1991 Apr 4;350(6317):436–438. doi: 10.1038/350436a0. [DOI] [PubMed] [Google Scholar]
  24. Garrett K. P., Serizawa H., Hanley J. P., Bradsher J. N., Tsuboi A., Arai N., Yokota T., Arai K., Conaway R. C., Conaway J. W. The carboxyl terminus of RAP30 is similar in sequence to region 4 of bacterial sigma factors and is required for function. J Biol Chem. 1992 Nov 25;267(33):23942–23949. [PubMed] [Google Scholar]
  25. Hahn S., Buratowski S., Sharp P. A., Guarente L. Identification of a yeast protein homologous in function to the mammalian general transcription factor, TFIIA. EMBO J. 1989 Nov;8(11):3379–3382. doi: 10.1002/j.1460-2075.1989.tb08501.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Hahn S., Buratowski S., Sharp P. A., Guarente L. Isolation of the gene encoding the yeast TATA binding protein TFIID: a gene identical to the SPT15 suppressor of Ty element insertions. Cell. 1989 Sep 22;58(6):1173–1181. doi: 10.1016/0092-8674(89)90515-1. [DOI] [PubMed] [Google Scholar]
  27. Hahn S., Buratowski S., Sharp P. A., Guarente L. Yeast TATA-binding protein TFIID binds to TATA elements with both consensus and nonconsensus DNA sequences. Proc Natl Acad Sci U S A. 1989 Aug;86(15):5718–5722. doi: 10.1073/pnas.86.15.5718. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Hahn S. Structure(?) and function of acidic transcription activators. Cell. 1993 Feb 26;72(4):481–483. doi: 10.1016/0092-8674(93)90064-w. [DOI] [PubMed] [Google Scholar]
  29. Hoey T., Dynlacht B. D., Peterson M. G., Pugh B. F., Tjian R. Isolation and characterization of the Drosophila gene encoding the TATA box binding protein, TFIID. Cell. 1990 Jun 29;61(7):1179–1186. doi: 10.1016/0092-8674(90)90682-5. [DOI] [PubMed] [Google Scholar]
  30. Horikoshi M., Wang C. K., Fujii H., Cromlish J. A., Weil P. A., Roeder R. G. Cloning and structure of a yeast gene encoding a general transcription initiation factor TFIID that binds to the TATA box. Nature. 1989 Sep 28;341(6240):299–303. doi: 10.1038/341299a0. [DOI] [PubMed] [Google Scholar]
  31. Horikoshi M., Wang C. K., Fujii H., Cromlish J. A., Weil P. A., Roeder R. G. Purification of a yeast TATA box-binding protein that exhibits human transcription factor IID activity. Proc Natl Acad Sci U S A. 1989 Jul;86(13):4843–4847. doi: 10.1073/pnas.86.13.4843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Inostroza J. A., Mermelstein F. H., Ha I., Lane W. S., Reinberg D. Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription. Cell. 1992 Aug 7;70(3):477–489. doi: 10.1016/0092-8674(92)90172-9. [DOI] [PubMed] [Google Scholar]
  33. Johnson P. F., McKnight S. L. Eukaryotic transcriptional regulatory proteins. Annu Rev Biochem. 1989;58:799–839. doi: 10.1146/annurev.bi.58.070189.004055. [DOI] [PubMed] [Google Scholar]
  34. Kao C. C., Lieberman P. M., Schmidt M. C., Zhou Q., Pei R., Berk A. J. Cloning of a transcriptionally active human TATA binding factor. Science. 1990 Jun 29;248(4963):1646–1650. doi: 10.1126/science.2194289. [DOI] [PubMed] [Google Scholar]
  35. Kelleher R. J., 3rd, Flanagan P. M., Kornberg R. D. A novel mediator between activator proteins and the RNA polymerase II transcription apparatus. Cell. 1990 Jun 29;61(7):1209–1215. doi: 10.1016/0092-8674(90)90685-8. [DOI] [PubMed] [Google Scholar]
  36. Kokubo T., Gong D. W., Yamashita S., Horikoshi M., Roeder R. G., Nakatani Y. Drosophila 230-kD TFIID subunit, a functional homolog of the human cell cycle gene product, negatively regulates DNA binding of the TATA box-binding subunit of TFIID. Genes Dev. 1993 Jun;7(6):1033–1046. doi: 10.1101/gad.7.6.1033. [DOI] [PubMed] [Google Scholar]
  37. Lee D. K., DeJong J., Hashimoto S., Horikoshi M., Roeder R. G. TFIIA induces conformational changes in TFIID via interactions with the basic repeat. Mol Cell Biol. 1992 Nov;12(11):5189–5196. doi: 10.1128/mcb.12.11.5189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Lorch Y., LaPointe J. W., Kornberg R. D. Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones. Cell. 1987 Apr 24;49(2):203–210. doi: 10.1016/0092-8674(87)90561-7. [DOI] [PubMed] [Google Scholar]
  39. Maldonado E., Ha I., Cortes P., Weis L., Reinberg D. Factors involved in specific transcription by mammalian RNA polymerase II: role of transcription factors IIA, IID, and IIB during formation of a transcription-competent complex. Mol Cell Biol. 1990 Dec;10(12):6335–6347. doi: 10.1128/mcb.10.12.6335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Matsui T., Segall J., Weil P. A., Roeder R. G. Multiple factors required for accurate initiation of transcription by purified RNA polymerase II. J Biol Chem. 1980 Dec 25;255(24):11992–11996. [PubMed] [Google Scholar]
  41. Meisterernst M., Horikoshi M., Roeder R. G. Recombinant yeast TFIID, a general transcription factor, mediates activation by the gene-specific factor USF in a chromatin assembly assay. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9153–9157. doi: 10.1073/pnas.87.23.9153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Meisterernst M., Roeder R. G. Family of proteins that interact with TFIID and regulate promoter activity. Cell. 1991 Nov 1;67(3):557–567. doi: 10.1016/0092-8674(91)90530-c. [DOI] [PubMed] [Google Scholar]
  43. Meisterernst M., Roy A. L., Lieu H. M., Roeder R. G. Activation of class II gene transcription by regulatory factors is potentiated by a novel activity. Cell. 1991 Sep 6;66(5):981–993. doi: 10.1016/0092-8674(91)90443-3. [DOI] [PubMed] [Google Scholar]
  44. Mitchell P. J., Tjian R. Transcriptional regulation in mammalian cells by sequence-specific DNA binding proteins. Science. 1989 Jul 28;245(4916):371–378. doi: 10.1126/science.2667136. [DOI] [PubMed] [Google Scholar]
  45. Miyamoto N. G., Moncollin V., Egly J. M., Chambon P. Specific interaction between a transcription factor and the upstream element of the adenovirus-2 major late promoter. EMBO J. 1985 Dec 16;4(13A):3563–3570. doi: 10.1002/j.1460-2075.1985.tb04118.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Moncollin V., Fischer L., Cavallini B., Egly J. M., Chambon P. Class II (B) general transcription factor (TFIIB) that binds to the template-committed preinitiation complex is different from general transcription factor BTF3. Proc Natl Acad Sci U S A. 1992 Jan 1;89(1):397–401. doi: 10.1073/pnas.89.1.397. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Moncollin V., Miyamoto N. G., Zheng X. M., Egly J. M. Purification of a factor specific for the upstream element of the adenovirus-2 major late promoter. EMBO J. 1986 Oct;5(10):2577–2584. doi: 10.1002/j.1460-2075.1986.tb04537.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Muhich M. L., Iida C. T., Horikoshi M., Roeder R. G., Parker C. S. cDNA clone encoding Drosophila transcription factor TFIID. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9148–9152. doi: 10.1073/pnas.87.23.9148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Nakatani Y., Horikoshi M., Brenner M., Yamamoto T., Besnard F., Roeder R. G., Freese E. A downstream initiation element required for efficient TATA box binding and in vitro function of TFIID. Nature. 1990 Nov 1;348(6296):86–88. doi: 10.1038/348086a0. [DOI] [PubMed] [Google Scholar]
  50. Ohkuma Y., Sumimoto H., Hoffmann A., Shimasaki S., Horikoshi M., Roeder R. G. Structural motifs and potential sigma homologies in the large subunit of human general transcription factor TFIIE. Nature. 1991 Dec 5;354(6352):398–401. doi: 10.1038/354398a0. [DOI] [PubMed] [Google Scholar]
  51. Peterson M. G., Inostroza J., Maxon M. E., Flores O., Admon A., Reinberg D., Tjian R. Structure and functional properties of human general transcription factor IIE. Nature. 1991 Dec 5;354(6352):369–373. doi: 10.1038/354369a0. [DOI] [PubMed] [Google Scholar]
  52. Pugh B. F., Tjian R. Diverse transcriptional functions of the multisubunit eukaryotic TFIID complex. J Biol Chem. 1992 Jan 15;267(2):679–682. [PubMed] [Google Scholar]
  53. Pugh B. F., Tjian R. Mechanism of transcriptional activation by Sp1: evidence for coactivators. Cell. 1990 Jun 29;61(7):1187–1197. doi: 10.1016/0092-8674(90)90683-6. [DOI] [PubMed] [Google Scholar]
  54. Pugh B. F., Tjian R. Transcription from a TATA-less promoter requires a multisubunit TFIID complex. Genes Dev. 1991 Nov;5(11):1935–1945. doi: 10.1101/gad.5.11.1935. [DOI] [PubMed] [Google Scholar]
  55. Ranish J. A., Hahn S. The yeast general transcription factor TFIIA is composed of two polypeptide subunits. J Biol Chem. 1991 Oct 15;266(29):19320–19327. [PubMed] [Google Scholar]
  56. Ranish J. A., Lane W. S., Hahn S. Isolation of two genes that encode subunits of the yeast transcription factor IIA. Science. 1992 Feb 28;255(5048):1127–1129. doi: 10.1126/science.1546313. [DOI] [PubMed] [Google Scholar]
  57. Roy A. L., Malik S., Meisterernst M., Roeder R. G. An alternative pathway for transcription initiation involving TFII-I. Nature. 1993 Sep 23;365(6444):355–359. doi: 10.1038/365355a0. [DOI] [PubMed] [Google Scholar]
  58. Samuels M., Fire A., Sharp P. A. Separation and characterization of factors mediating accurate transcription by RNA polymerase II. J Biol Chem. 1982 Dec 10;257(23):14419–14427. [PubMed] [Google Scholar]
  59. Samuels M., Sharp P. A. Purification and characterization of a specific RNA polymerase II transcription factor. J Biol Chem. 1986 Feb 15;261(5):2003–2013. [PubMed] [Google Scholar]
  60. Sawadogo M., Roeder R. G. Interaction of a gene-specific transcription factor with the adenovirus major late promoter upstream of the TATA box region. Cell. 1985 Nov;43(1):165–175. doi: 10.1016/0092-8674(85)90021-2. [DOI] [PubMed] [Google Scholar]
  61. Sawadogo M., Sentenac A. RNA polymerase B (II) and general transcription factors. Annu Rev Biochem. 1990;59:711–754. doi: 10.1146/annurev.bi.59.070190.003431. [DOI] [PubMed] [Google Scholar]
  62. Sayre M. H., Tschochner H., Kornberg R. D. Reconstitution of transcription with five purified initiation factors and RNA polymerase II from Saccharomyces cerevisiae. J Biol Chem. 1992 Nov 15;267(32):23376–23382. [PubMed] [Google Scholar]
  63. Serizawa H., Conaway R. C., Conaway J. W. A carboxyl-terminal-domain kinase associated with RNA polymerase II transcription factor delta from rat liver. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7476–7480. doi: 10.1073/pnas.89.16.7476. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Struhl K. Molecular mechanisms of transcriptional regulation in yeast. Annu Rev Biochem. 1989;58:1051–1077. doi: 10.1146/annurev.bi.58.070189.005155. [DOI] [PubMed] [Google Scholar]
  65. Sumimoto H., Ohkuma Y., Sinn E., Kato H., Shimasaki S., Horikoshi M., Roeder R. G. Conserved sequence motifs in the small subunit of human general transcription factor TFIIE. Nature. 1991 Dec 5;354(6352):401–404. doi: 10.1038/354401a0. [DOI] [PubMed] [Google Scholar]
  66. Tanese N., Pugh B. F., Tjian R. Coactivators for a proline-rich activator purified from the multisubunit human TFIID complex. Genes Dev. 1991 Dec;5(12A):2212–2224. doi: 10.1101/gad.5.12a.2212. [DOI] [PubMed] [Google Scholar]
  67. Usuda Y., Kubota A., Berk A. J., Handa H. Affinity purification of transcription factor IIA from HeLa cell nuclear extracts. EMBO J. 1991 Aug;10(8):2305–2310. doi: 10.1002/j.1460-2075.1991.tb07767.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Waldschmidt R., Seifart K. H. TFIIA is required for in vitro transcription of mammalian U6 genes by RNA polymerase III. J Biol Chem. 1992 Aug 15;267(23):16359–16364. [PubMed] [Google Scholar]
  69. Weinzierl R. O., Dynlacht B. D., Tjian R. Largest subunit of Drosophila transcription factor IID directs assembly of a complex containing TBP and a coactivator. Nature. 1993 Apr 8;362(6420):511–517. doi: 10.1038/362511a0. [DOI] [PubMed] [Google Scholar]
  70. White J. H., Brou C., Wu J., Burton N., Egly J. M., Chambon P. Evidence for a factor required for transcriptional stimulation by the chimeric acidic activator GAL-VP16 in HeLa cell extracts. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7674–7678. doi: 10.1073/pnas.88.17.7674. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. White J., Brou C., Wu J., Lutz Y., Moncollin V., Chambon P. The acidic transcriptional activator GAL-VP16 acts on preformed template-committed complexes. EMBO J. 1992 Jun;11(6):2229–2240. doi: 10.1002/j.1460-2075.1992.tb05282.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Wiley S. R., Kraus R. J., Mertz J. E. Functional binding of the "TATA" box binding component of transcription factor TFIID to the -30 region of TATA-less promoters. Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):5814–5818. doi: 10.1073/pnas.89.13.5814. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. Wobbe C. R., Struhl K. Yeast and human TATA-binding proteins have nearly identical DNA sequence requirements for transcription in vitro. Mol Cell Biol. 1990 Aug;10(8):3859–3867. doi: 10.1128/mcb.10.8.3859. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Zawel L., Reinberg D. Initiation of transcription by RNA polymerase II: a multi-step process. Prog Nucleic Acid Res Mol Biol. 1993;44:67–108. doi: 10.1016/s0079-6603(08)60217-2. [DOI] [PubMed] [Google Scholar]
  75. Zhou Q., Boyer T. G., Berk A. J. Factors (TAFs) required for activated transcription interact with TATA box-binding protein conserved core domain. Genes Dev. 1993 Feb;7(2):180–187. doi: 10.1101/gad.7.2.180. [DOI] [PubMed] [Google Scholar]
  76. Zhou Q., Lieberman P. M., Boyer T. G., Berk A. J. Holo-TFIID supports transcriptional stimulation by diverse activators and from a TATA-less promoter. Genes Dev. 1992 Oct;6(10):1964–1974. doi: 10.1101/gad.6.10.1964. [DOI] [PubMed] [Google Scholar]
  77. Zhu H., Pyrwes R. Identification of a coactivator that increases activation of transcription by serum response factor and GAL4-VP16 in vitro. Proc Natl Acad Sci U S A. 1992 Jun 15;89(12):5291–5295. doi: 10.1073/pnas.89.12.5291. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The EMBO Journal are provided here courtesy of Nature Publishing Group

RESOURCES