Identification of Seven Hydrophobic Clusters in GCN4 Making Redundant Contributions to Transcriptional Activation

REFERENCES

• Arndt, K., S. Ricupero-Hovasse, and F. Winston. 1995. TBP mutants defective in activated transcription in vivo. EMBO J. 14: 1490–1497.
   PubMedGoogle Scholar
• Baniahmad, A., I. Ha, D. Reinberg, S. Tsai, M. Tsai, and B. O’Malley. 1993. Interaction of human thyroid hormone receptor β with transcription factor TFIIB may mediate target gene depression and activation by thyroid hormone. Proc. Natl. Acad. Sci. USA 90: 8832–8836.
   PubMedGoogle Scholar
• Barettino, D., M. D. M. Vivanco Ruiz, and H. G. Stunnenberg. 1994. Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor. EMBO J. 13: 3039–3049.
   PubMed Web of Science ®Google Scholar
• Barlev, N. A., R. Candau, L. Wang, P. Darpino, N. Silverman, and S. L. Berger. 1995. Characterization of physical interactions of the putative transcriptional adaptor, ADA2, with acidic activation domains and TATA-binding protein. J. Biol. Chem. 270: 19337–19344.
   PubMedGoogle Scholar
• Berger, S. L., B. Piña, N. Silverman, G. A. Marcus, J. Agapite, J. L. Regier, S. J. Triezenberg, and L. Guarente. 1992. Genetic isolation of ADA2: a potential transcription adaptor required for function of certain acidic domains. Cell 70: 251–265.
   PubMedGoogle Scholar
• Blair, W. B., H. P. Bogerd, S. J. Madore, and B. R. Cullen. 1994. Mutational analysis of the transcriptional activation domain of RelA: identification of a highly synergistic minimal acidic activation module. Mol. Cell. Biol. 14: 7226–7234.
   PubMedGoogle Scholar
• Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248–254.
   PubMed Web of Science ®Google Scholar
• Buratowski, S. 1994. The basics of basal transcription by RNA polymerase II. Cell 77: 1–3.
   PubMed Web of Science ®Google Scholar
• Cadwell, R. C., and G. F. Joyce. 1992. Randomization of genes by PCR mutagenesis. PCR Methods Applic. 2: 28–33.
   PubMedGoogle Scholar
• Caron, C., R. Rousset, C. Beraud, V. Moncollin, J. Egly, and P. Jalinot. 1993. Functional and biochemical interaction of the HTLV-1 Tax1 transactivator with TBP. EMBO J. 12: 4269–4278.
   PubMedGoogle Scholar
• Chatterjee, S., and K. Struhl. 1995. Connecting a promoter-bound protein to TBP bypasses the need for a transcriptional activation domain. Nature (London) 374: 820–822.
   PubMedGoogle Scholar
• Chen, J.-L., L. Attardi, C. Verrijzer, K. Yokomori, and R. Tjian. 1994. Assembly of recombinant TFIID reveals differential coactivator requirements for distinct transcriptional activators. Cell 79: 93–105.
   PubMed Web of Science ®Google Scholar
• Choy, B., and M. R. Green. 1993. Eukaryotic activators function during multiple steps of preinitiation complex assembly. Nature (London) 366: 531–536.
   PubMedGoogle Scholar
• Cress, W. D., and S. J. Triezenberg. 1991. Critical structural elements of the VP16 transcriptional activation domain. Science 251: 87–90.
   PubMedGoogle Scholar
• Dahlman-Wright, K., H. Baumann, I. McEwan, T. Almlof, A. Wright, J. Gustafsson, and T. Hard. 1995. Structural characterization of a minimal function transactivation domain from the human glucocorticoid receptor. Proc. Natl. Acad. Sci. USA 92: 1699–1703.
   PubMedGoogle Scholar
• Drysdale, C. M., E. Dueñas, B. M. Jackson, U. Reusser, G. H. Braus, and A. G. Hinnebusch. 1995. The transcriptional activator GCN4 contains multiple activation domains that are critically dependent on hydrophobic amino acids. Mol. Cell. Biol. 15: 1220–1233.
   PubMed Web of Science ®Google Scholar
• Ellenberger, T. E., C. J. Brandl, K. Struhl, and S. C. Harrison. 1992. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α helices: crystal structure of the protein-DNA complex. Cell 71: 1223–1237.
   PubMed Web of Science ®Google Scholar
• Ge, H., and R. Roeder. 1994. Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes. Cell 78: 513–523.
   PubMedGoogle Scholar
• Geisberg, J., W. Lee, A. Berk, and R. Ricciardi. 1994. The zinc finger region of the adenovirus E1A transactivating domain complexes with the TATA box binding protein. Proc. Natl. Acad. Sci. USA 91: 2488–2492.
   PubMedGoogle Scholar
• Georgakopoulos, T., N. Gounalaki, and G. Thireos. 1995. Genetic evidence for the interaction of the yeast transcriptional co-activator proteins GCN5 and ADA2. Mol. Gen. Genet. 246: 723–728.
   PubMedGoogle Scholar
• Georgakopoulos, T., and G. Thireos. 1992. Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription. EMBO J. 11: 4145–4152.
   PubMed Web of Science ®Google Scholar
• Gill, G., E. Pascal, Z. H. Tseng, and R. Tjian. 1994. A glutamine-rich hydrophobic patch in transcription factor Sp1 contacts the dTAFII110 component of the Drosophila TFIID complex and mediates transcriptional activation. Proc. Natl. Acad. Sci. USA 91: 192–196.
   PubMed Web of Science ®Google Scholar
• Goodrich, J. A., T. Hoey, C. J. Thut, A. Admon, and R. Tjian. 1993. Drosophila TAFII40 interacts with both a VP16 activation domain and the basal transcription factor TFIIB. Cell 75: 519–530.
   PubMedGoogle Scholar
• Hagemeier, C., A. Cook, and T. Kouzarides. 1993. The retinoblastoma protein binds E2F residues required for activation in vivo and TBP binding in vitro. Nucleic Acids Res. 21: 4998–5004.
   PubMedGoogle Scholar
• Hardwick, J. M., L. Tse, N. Applegren, J. Nicholas, and M. A. Veliuona. 1992. The Epstein-Barr virus R transactivator (Rta) contains a complex, potent activation domain with properties different from those of VP16. J. Virol. 66: 5500–5508.
   PubMedGoogle Scholar
• Hengartner, C., C. Thompson, J. Zhang, D. Chao, S.-M. Liao, A. Koleske, S. Okamura, and R. Young. 1995. Association of an activator with an RNA polymerase II holoenzyme. Genes Dev. 9: 897–910.
   PubMed Web of Science ®Google Scholar
• Hinnebusch, A. G. 1984. Evidence for translational regulation of the activator of general amino acid control in yeast. Proc. Natl. Acad. Sci. USA 81: 6442–6446.
   PubMed Web of Science ®Google Scholar
• Hinnebusch, A. G. 1992. General and pathway-specific regulatory mechanisms controlling the synthesis of amino acid biosynthetic enzymes in Saccharomyces cerevisiae, p. 319–414. In E. W. Jones, J. R. Pringle, and J. R. Broach (ed.), The molecular and cellular biology of the yeast Saccharomyces: gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Hinnebusch, A. G., and G. R. Fink. 1983. Positive regulation in the general amino acid control of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 80: 5374–5378.
   PubMed Web of Science ®Google Scholar
• Hope, I. A., S. Mahadevan, and K. Struhl. 1988. Structural and functional characterization of the short acidic transcriptional activation region of yeast GCN4 protein. Nature (London) 333: 635–640.
   PubMedGoogle Scholar
• Hope, I. A., and K. Struhl. 1985. GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for the general control of amino acid biosynthetic genes in yeast. Cell 43: 177–188.
   PubMed Web of Science ®Google Scholar
• Hope, I. A., and K. Struhl. 1986. Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of yeast. Cell 46: 885–894.
   PubMed Web of Science ®Google Scholar
• Hope, I. A., and K. Struhl. 1987. GCN4, a eukaryotic transcriptional activator protein, binds as a dimer to target DNA. EMBO J. 6: 2781–2784.
   PubMed Web of Science ®Google Scholar
• Ingles, C. J., M. Shales, W. D. Cress, S. J. Triezenberg, and J. Greenblatt. 1991. Reducing binding of TFIID to transcriptionally compromised mutants of VP16. Nature (London) 351: 588–590.
   PubMedGoogle Scholar
• Jacq, X., C. Brou, Y. Lutz, I. Davidson, P. Chambon, and L. Tora. 1994. Human TAFII30 is present in a distinct TFIID complex and is required for transcriptional activation by the estrogen receptor. Cell 79: 107–117.
   PubMedGoogle Scholar
• Kashanchi, F., G. Piras, M. Radonovich, J. Duvall, A. Fattaey, C. Chiang, R. Roeder, and J. Brady. 1994. Direct interaction of human TFIID with the HIV-1 transactivator Tat. Nature (London) 367: 295–300.
   PubMed Web of Science ®Google Scholar
• Kerr, L., L. Ransone, P. Wamsley, M. Schmitt, T. Boyer, Q. Zhou, A. Berk, and I. Verma. 1993. Association between proto-oncoprotein Rel and TATA-binding protein mediates transcriptional activation by NF-KappaB. Nature (London) 365: 412–419.
   PubMedGoogle Scholar
• Kim, T. K., S. Hashimoto, R. J. Kelleher, P. M. Flanagan, R. D. Kornberg, M. Horikoshi, and R. G. Roeder. 1994. Effects of activation-defective TBP mutations on transcription initiation in yeast. Nature (London) 369: 252–255.
   PubMedGoogle Scholar
• Kim, T., and R. Roeder. 1994. Proline-rich activator CTF1 targets the TFIIB assembly step during transcriptional activation. Proc. Natl. Acad. Sci. USA 91: 4170–4174.
   PubMedGoogle Scholar
• Klages, N., and M. Strubin. 1995. Stimulation of RNA polymerase II transcription initiation by recruitment of TBP in vivo. Nature (London) 374: 822–823.
   PubMedGoogle Scholar
• Koleske, A., and R. Young. 1995. The RNA polymerase II holoenzyme and its implications for gene regulation. Trends Biochem. Sci. 20: 113–116.
   PubMedGoogle Scholar
• Lee, M., and K. Struhl. 1995. Mutations on the DNA-binding surface of TATA-binding protein can specifically impair the response to acidic activators in vivo. Mol. Cell. Biol. 15: 5461–5469.
   PubMedGoogle Scholar
• Lee, W., C. Kao, G. Bryant, X. Liu, and A. Berk. 1991. Adenovirus E1A activation domain binds the basic repeat in the TATA box transcription factor. Cell 67: 365–376.
   PubMedGoogle Scholar
• Leuther, K. K., J. M. Salmeron, and S. A. Johnston. 1993. Genetic evidence that an activation domain of GAL4 does not require acidity and may form a β sheet. Cell 72: 575–585.
   PubMed Web of Science ®Google Scholar
• Lienhard Schmitz, M., M. Dos Santos Silva, H. Altmann, M. Czisch, T. Holak, and P. Baeuerle. 1994. Structural and functional analysis of the NF-kB p65 terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation. J. Biol. Chem. 269: 25613–25620.
   PubMedGoogle Scholar
• Lin, J., J. Chen, B. Elenbaas, and A. J. Levine. 1994. Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein. Genes Dev. 8: 1235–1246.
   PubMed Web of Science ®Google Scholar
• Lin, Y., and M. R. Green. 1991. Mechanism of action of an acidic transcriptional activator in vitro. Cell 64: 971–981.
   PubMed Web of Science ®Google Scholar
• Lin, Y., I. Ha, E. Maldonado, D. Reinberg, and M. R. Green. 1991. Binding of general transcription factor TFIIB to an acidic activating region. Nature (London) 353: 569–571.
   PubMed Web of Science ®Google Scholar
• Lu, H., and A. Levine. 1995. Human TAFII31 protein is a transcriptional coactivator of the p53 protein. Proc. Natl. Acad. Sci. USA 92: 5154–5158.
   PubMedGoogle Scholar
• Melcher, K., and S. A. Johnston. 1995. GAL4 interacts with TATA-binding protein and coactivators. Mol. Cell. Biol. 15: 2839–2848.
   PubMedGoogle Scholar
• Metz, R., A. J. Bannister, J. A. Sutherland, C. Hagemeier, E. C. O’Rourke, A. Cook, R. Bravo, and T. Kouzarides. 1994. c-Fos-Induced activation of a TATA-box-containing promoter involves direct contact with TATA-binding protein. Mol. Cell. Biol. 14: 6021–6029.
   PubMedGoogle Scholar
• Metz, R., T. Kouzarides, and R. Bravo. 1994. A C-terminal domain in FosB, absent in FosB/SF and Fra-1, which is able to interact with the TATA binding protein, is required for altered cell growth. EMBO J. 13: 3832–3842.
   PubMedGoogle Scholar
• Moehle, C. M., and A. G. Hinnebusch. 1991. Association of RAP1 binding sites with stringent control of ribosomal protein gene transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 11: 2723–2735.
   Google Scholar
• Narayan, S., S. Widen, W. Beard, and S. Wilson. 1994. RNA polymerase II transcription. Rate of promoter clearance is enhanced by a purified activating transcription factor/cAMP response element-binding protein. J. Biol. Chem. 269: 12755–12763.
   PubMedGoogle Scholar
• Natarajan, K., and A. Hinnebusch. Unpublished observations.
   Google Scholar
• Paluh, J. L., and C. Yanofsky. 1991. Characterization of Neurospora CPC1, a bZIP DNA binding protein that does not require aligned heptad leucines for dimerization. Mol. Cell. Biol. 11: 935–944.
   PubMedGoogle Scholar
• Parent, S. A., C. M. Fenimore, and K. A. Bostian. 1985. Vector systems for the expression, analysis and cloning of DNA sequences in S. cerevisiae. Yeast 1: 83–138.
   PubMedGoogle Scholar
• Peterson, C. L., and J. W. Tamkun. 1995. The SWI-SNF complex: a chromatin remodeling machine? Trends Biochem. Sci. 20: 143–146.
   Google Scholar
• Piña, B., S. Berger, G. Marcus, N. Silverman, J. Agapite, and L. Guarente. 1993. ADA3: a gene, identified by resistance to GAL4-VP16, with properties similar to and different from those of ADA2. Mol. Cell. Biol. 13: 5981–5989.
   Google Scholar
• Regier, J. L., F. Shen, and S. J. Triezenberg. 1993. Pattern of aromatic and hydrophobic amino acids critical for one of two subdomains of the VP16 transcriptional activator. Proc. Natl. Acad. Sci. USA 90: 883–887.
   PubMed Web of Science ®Google Scholar
• Seipel, K., O. Georgiev, and W. Schaffner. 1994. A minimal transcription activation domain consisting of a specific array of aspartic acid and leucine residues. Biol. Chem. Hoppe-Seyler 375: 463–470.
   PubMed Web of Science ®Google Scholar
• Shen, F., S. J. Triezenberg, P. Hensley, D. Porter, and J. R. Knutson. 1996. Critical amino acids in the transcriptional activation domain of the herpesvirus protein VP16 are solvent-exposed in highly mobile protein segments. J. Biol. Chem. 271: 4819–4826.
   PubMedGoogle Scholar
• Shen, F., S. J. Triezenberg, P. Hensley, D. Porter, and J. R. Knutson. 1996. Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. J. Biol. Chem. 271: 4827–4837.
   PubMedGoogle Scholar
• Sherman, F., G. R. Fink, and C. W. Lawrence. 1974. Methods of yeast genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Tanaka, M., and W. Herr. 1994. Reconstitution of transcriptional activation domains by reiteration of short peptide segments reveals the modular organization of a glutamine-rich activation domain. Mol. Cell. Biol. 14: 6056–6067.
   PubMedGoogle Scholar
• Tavernarakis, N., and G. Thireos. 1995. Transcriptional interference caused by GCN4 overexpression reveals multiple interactions mediating transcriptional activation. Mol. Gen. Genet. 247: 571–578.
   PubMedGoogle Scholar
• Thut, C., J.-L. Chen, R. Klemm, and R. Tjian. 1995. P53 Transcriptional activation mediated by coactivators TAFII40 and TAFII60. Science 267: 100–104.
   PubMedGoogle Scholar
• Tong, X., R. Drapkin, D. Reinberg, and E. Kieff. 1995. The 62- and 80-kDa subunits of transcription factor IIH mediate the interaction with Epstein-Barr virus nuclear protein 2. Proc. Natl. Acad. Sci. USA 92: 3259–3263.
   PubMedGoogle Scholar
• Walker, S., R. Greaves, and P. O’Hare. 1993. Transcriptional activation by the acidic domain of Vmw65 requires the integrity of the domain and involves additional determinants distinct from those necessary for TFIIB binding. Mol. Cell. Biol. 13: 5233–5244.
   PubMedGoogle Scholar
• Xiao, H., J. Friesen, and J. Lis. 1995. Recruiting TATA-binding protein to a promoter: transcriptional activation without an upstream activator. Mol. Cell. Biol. 15: 5757–5761.
   PubMedGoogle Scholar
• Xiao, H., J. D. Friesen, and J. T. Lis. 1994. A highly conserved domain of RNA polymerase II shares a functional element with acidic activation domains of upstream transcription factors. Mol. Cell. Biol. 14: 7507–7516.
   PubMedGoogle Scholar
• Xiao, H., A. Pearson, B. Coulombe, R. Truant, S. Zhang, J. Regier, S. Triezenberg, D. Reinberg, O. Flores, C. Ingles, and J. Greenblatt. 1994. Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53. Mol. Cell. Biol. 14: 7013–7024.
   PubMed Web of Science ®Google Scholar
• Xu, X., C. Prorock, H. Ishikawa, E. Maldonado, Y. Ito, and C. Gelinas. 1993. Functional interaction of the v-Rel and c-Rel oncoproteins with the TATA-binding protein and association with transcription factor IIB. Mol. Cell. Biol. 13: 6733–6741.
   PubMedGoogle Scholar
• Yankulov, K., J. Blau, T. Purton, S. Roberts, and D. Bentley. 1994. Transcriptional elongation by RNA polymerase II is stimulated by transactivators. Cell 77: 749–759.
   PubMedGoogle Scholar