REFERENCES
- Aso, T., Vasavada, H. A., Kawaguchi, T., Germino, F. J., Ganguly, S., Kitajima, S., Weissman, S. M., and Yasukochi, Y.. 1992. Characterization of cDNA for the large subunit of the transcription initiation factor TFIIF. Nature 355:461–464
- Attwood, P. V., Mayer, F., and Wallace, J. C.. 1986. Avidin as a probe of the conformational changes induced in pyruvate carboxylase by acetyl-CoA and pyruvate. FEBS Lett. 203:191–196
- Bannister, A. J., and Kouzarides, T.. 1996. The CBP co-activator is a histone acetyltransferase. Nature 384:641–643
- Bohmann, D., and Tjian, R.. 1989. Biochemical analysis of transcriptional activation by Jun: differential activity of c- and v-Jun. Cell 59:709–717
- Boyes, J., Byfield, P., Nakatani, Y., and Ogryzko, V.. 1998. Regulation of activity of the transcription factor GATA-1 by acetylation. Nature 396:594–598
- Brownell, J. E., and Allis, C. D.. 1996. Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation. Curr. Opin. Genet. Dev. 6:176–184
- Brownell, J. E., Zhou, J., Ranalli, T., Kobayashi, R., Edmondson, D. G., Roth, S. Y., and Allis, C. D.. 1996. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84:843–851
- Dignam, J. D., Martin, P. L., Shastry, B. S., and Roeder, R. G.. 1983. Eukaryotic gene transcription with purified components. Methods Enzymol. 101:582–598
- Dutnall, R. N., Tafrov, S. T., Sternglanz, R., and Ramakrishnan, V.. 1998. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell 94:427–438
- Finkelstein, A., Kostrub, C. F., Li, J., Chavez, D. P., Wang, B. Q., Fang, S. M., Greenblatt, J., and Burton, Z. F.. 1992. A cDNA encoding RAP74, a general initiation factor for transcription by RNA polymerase II. Nature 355:464–467
- Flores, O., Lu, H., and Reinberg, D.. 1992. Factors involved in specific transcription initiation by RNA polymerase II: Identification and characterization of factor IIH. J. Biol. Chem. 267:2786–2793
- Goodrich, J. A., Cutler, G., and Tjian, R.. 1996. Contacts in context: promoter specificity and macromolecular interactions in transcription. Cell 84:825–830
- Goodrich, J. A., Hoey, T., Thut, C. J., Admon, A., and Tjian, R.. 1993. Drosophila TAFII40 interacts with both a VP16 activation domain and the basal transcription factor TFIIB. Cell 75:519–530
- Goodrich, J. A., and Tjian, R.. 1994. Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II. Cell 77:145–156
- Gu, W., and Roeder, R. G.. 1997. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90:595–606
- Ha, I., Lane, W. S., and Reinberg, D.. 1991. Cloning of a human gene encoding the general transcription factor IIB. Nature 352:689–695
- Hernandez, N.. 1993. TBP, a universal eukaryotic transcription factor? Genes Dev. 7:1291–1308
- Herrera, J. E., Bergel, M., Yang, X. J., Nakatani, Y., and Bustin, M.. 1997. The histone acetyltransferase activity of human GCN5 and PCAF is stabilized by coenzymes. J. Biol. Chem. 272:27253–27258
- Herrera, J. E., Sakaguchi, K., Bergel, M., Trieschmann, L., Nakatani, Y., and Bustin, M.. 1999. Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes. Mol. Cell. Biol. 19:3466–3473
- Hickman, A. B., Namboodiri, M. A., Klein, M. A., and Dyda, F.. 1999. The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 Å resolution with bisubstrate analog. Cell 97:361–369
- Hoffmann, A., Chiang, C.-M., Oelgeschlager, T., Xie, X., Burley, S. K., Nakatani, Y., and Roeder, R.. 1996. A histone octamer-like structure within TFIID. Nature 380:356–359
- Imhof, A., Yang, X.-J., Ogryzko, V. V., Nakatani, Y., Wolffe, A. P., and Ge, H.. 1997. Acetylation of general transcription factors by histone acetyltransferases. Curr. Biol. 7:689–692
- Kokubo, T., Gond, D.-W., Wootton, J. C., Horikoshi, M., Roeder, R. G., and Nakatani, Y.. 1994. Molecular cloning of Drosophila TFIID subunits. Nature 367:484–487
- Kugel, J. F., and Goodrich, J. A.. 1998. Promoter escape limits the rate of transcription from the adenovirus major late promoter on negatively supercoiled templates. Proc. Natl. Acad. Sci. USA 95:9232–9237
- Lieberman, P. M., and Berk, A. J.. 1994. A mechanism for TAFs in transcriptional activation: activation domain enhancement of TFIID-TFIIA-promoter DNA complex formation. Genes Dev. 8:995–1006
- Lu, H., Flores, O., Weinmann, R., and Reinberg, D.. 1991. The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex. Proc. Natl. Acad. Sci. USA 88:10004–10008
- 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., and Allis, C. D.. 1996. The TAFII250 subunit of TFIID has histone acetyltransferase activity. Cell 87:1261–1270
- Munshi, N., Merika, M., Yie, J., Senger, K., Chen, G., and Thanos, D.. 1998. Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome. Mol. Cell 2:457–467
- Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., and Nakatani, Y.. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953–959
- Ozer, J., Moore, P. A., Bolden, A. H., Lee, A., Rosen, C. A., and Lieberman, P. M.. 1994. Molecular cloning of the small (gamma) subunit of human TFIIA reveals functions critical for activated transcription. Genes Dev. 8:2324–2335
- Pazin, M. J., and Kadonaga, J. T.. 1997. What's up and down with histone deacetylation and transcription? Cell 89:325–328
- Peterson, M. G., Inostroza, J., Maxon, M. E., Flores, O., Admon, A., Reinberg, D., and Tjian, R.. 1991. Structure and functional properties of human general transcription factor IIE. Nature 354:369–373
- Peterson, M. G., Tanese, N., Pugh, B. F., and Tjian, R.. 1990. Functional domains and upstream activation properties of cloned human TATA binding protein. Science 248:1625–1630
- Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., and Appella, E.. 1998. DNA damage activates p53 through a phosphorylation-acetylation cascade. Genes Dev. 12:2831–2841
- Sopta, M., Burton, Z., and Greenblatt, J.. 1989. Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II. Nature 341:410–414
- Sun, X., Ma, D., Sheldon, M., Yeung, K., and Reinberg, D.. 1994. Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription. Genes Dev. 8:2336–2348
- Thut, C. J., Chen, J.-L., Klemm, R., and Tjian, R.. 1995. p53 transcriptional activation mediated by TAFII40 and TAFII60. Science 267:100–104
- Utley, R. T., Ikeda, K., Grant, P. A., Cote, J., Steger, D. J., Eberharter, A., John, S., and Workman, J. L.. 1998. Transcriptional activators direct histone acetyltransferase complexes to nucleosomes. Nature 394:498–502
- Wolffe, A. P.. The nucleosome 1: JAI Press Ltd., Greenwich, Conn
- Workman, J. L., and Kingston, R. E.. 1998. 1995. Alterations of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 67:545–579
- Xie, X., Kokubo, T., Cohen, S. L., Mirza, U. A., Hoffmann, A., Chait, B. T., Roeder, R. G., Nakatani, Y., and Burley, S. K.. 1996. Structural similarity between TAFs and the heterotetrameric core of the histone octamer. Nature 380:316–322
- Yang, X.-J., Ogryzko, V. V., Nishikawa, J., Howard, B. H., and Nakatani, Y.. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319–324
- Yoshinaga, T.. 1976. Phosphoenolpyruvate carboxylase of Escherichia coli. Studies on multiple conformational states elicited by allosteric effectors with fluorescent probe, 1-anilinonaphthalene-8-sulfonate. Biochim. Biophys. Acta 452:566–579
- Zhang, W., and Bieker, J. J.. 1998. Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases. Proc. Natl. Acad. Sci. USA 95:9855–9860