Interaction between Acetylated MyoD and the Bromodomain of CBP and/or p300

REFERENCES

• Ait-Si-Ali, S., S. Ramirez, F. X. Barre, F. Dkhissi, L. Magnaghi-Jaulin, J. A. Girault, P. Robin, M. Knibiehler, L. L. Pritchard, B. Ducommun, D. Trouche, and A. Harel-Bellan. 1998. Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A. Nature 396:184–186.
   PubMedGoogle Scholar
• Ait-Si-Ali, S., S. Ramirez, P. Robin, D. Trouche, and A. Harel-Bellan. 1998. A rapid and sensitive assay for histone acetyl-transferase activity. Nucleic Acids Res. 26:3869–3870.
   PubMed Web of Science ®Google Scholar
• Bannister, A. J., and T. Kouzarides. 1996. The CBP co-activator is a histone acetyltransferase. Nature 384:641–643.
   PubMed Web of Science ®Google Scholar
• Bayle, J. H., and G. R. Crabtree. 1997. Protein acetylation: more than chromatin modification to regulate transcription. Chem. Biol. 4:885–888.
   PubMedGoogle Scholar
• Boyes, J., P. Byfield, Y. Nakatani, and V. Ogryzko. 1998. Regulation of activity of the transcription factor GATA-1 by acetylation. Nature 396:594–598.
   PubMed Web of Science ®Google Scholar
• Breitschopf, K., E. Bengal, T. Ziv, A. Admon, and A. Ciechanover. 1998. A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein. EMBO J. 17:5964–5973.
   PubMed Web of Science ®Google Scholar
• Brownell, J. E., J. Zhou, T. Ranalli, R. Kobayashi, D. G. Edmondson, S. Y. Roth, and C. D. Allis. 1996. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84:843–851.
   PubMed Web of Science ®Google Scholar
• Buckingham, M.. 1992. Making muscle in mammals. Trends Genet. 8:144–148.
   PubMed Web of Science ®Google Scholar
• Chrivia, J. C., R. P. S. Kwok, N. Lamb, M. Hagiwara, M. R. Montminy, and R. H. Goodman. 1993. Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 265:855–859.
   Google Scholar
• Davis, R. L., H. Weintraub, and A. B. Lassar. 1987. Expression of a single transfected cDNA converts fibroblasts to myoblasts. Cell 51:987–1000.
   PubMed Web of Science ®Google Scholar
• Dhalluin, C., J. E. Carlson, L. Zeng, C. He, A. K. Aggarwal, and M. M. Zhou. 1999. Structure and ligand of a histone acetyltransferase bromodomain. Nature 399:491–496.
   PubMed Web of Science ®Google Scholar
• Gu, W., and R. G. Roeder. 1997. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90:595–606.
   PubMed Web of Science ®Google Scholar
• Haynes, S. R., C. Dollard, F. Winston, S. Beck, J. Trowsdale, and I. B. Dawid. 1992. The bromodomain: a conserved sequence found in human, Drosophila and yeast proteins. Nucleic Acids Res. 20:2603
   PubMed Web of Science ®Google Scholar
• Imhof, A., X. J. Yang, V. V. Ogryzko, Y. Nakatani, A. P. Wolffe, and H. Ge. 1997. Acetylation of general transcription factors by histone acetyltransferases. Curr. Biol. 7:689–692.
   PubMed Web of Science ®Google Scholar
• Jackson, V., A. Shires, R. Chalkley, and D. K. Granner. 1975. Studies on highly metabolically active acetylation and phosphorylation of histones. J. Biol. Chem. 250:4856–4863.
   PubMed Web of Science ®Google Scholar
• Kamei, Y., L. Xu, T. Heinzel, J. Torchia, R. Kurokawa, B. Gloss, S.-K. Lin, R. A. Heyman, D. W. Rose, C. K. Glass, and M. G. Rosenfeld. 1996. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 85:403–414.
   PubMed Web of Science ®Google Scholar
• Kiernan, R. E., C. Vanhulle, L. Schiltz, E. Adam, H. Xiao, F. Maudoux, C. Calomme, A. Burny, Y. Nakatani, K. T. Jeang, M. Benkirane, and C. van Lint. 1999. HIV-1 tat transcriptional activity is regulated by acetylation. EMBO J. 18:6106–6118.
   PubMed Web of Science ®Google Scholar
• Kraus, W. L., E. T. Manning, and J. T. Kadonaga. 1999. Biochemical analysis of distinct activation functions in p300 that enhance transcription initiation with chromatin templates. Mol. Cell. Biol. 19:8123–8135.
   PubMed Web of Science ®Google Scholar
• Kuo, M. H., and C. D. Allis. 1998. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 20:615–626.
   PubMed Web of Science ®Google Scholar
• Lassar, A. B., R. L. Davis, W. E. Wright, T. Kadesch, C. Murre, A. Voronova, D. Baltimore, and H. Weintraub. 1991. Functional activity of myogenic HLH proteins requires hetero-oligomerisation with E12–E47 like proteins in vivo. Cell 66:305–315.
   PubMed Web of Science ®Google Scholar
• Martinez-Balbas, M. A., U. M. Bauer, S. J. Nielsen, A. Brehm, and T. Kouzarides. 2000. Regulation of E2F1 activity by acetylation. EMBO J. 19:662–671.
   PubMed Web of Science ®Google Scholar
• Murre, C., P. S. McCaw, H. Vaessin, M. Caudy, L. Y. Jan, Y. N. Jan, C. V. Cabrera, J. N. Buskin, S. D. Hauschka, A. B. Lassar, et al.. 1989. Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence. Cell 58:537–544.
   PubMed Web of Science ®Google Scholar
• Ogryzko, V. V., R. L. Schiltz, V. Russanova, B. H. Howard, and Y. Nakatani. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953–959.
   PubMed Web of Science ®Google Scholar
• Petrij, F., R. H. Giles, H. G. Dauwerse, J. J. Saris, R. C. Hennekam, M. Masuno, N. Tommerup, G. J. van Ommen, R. H. Goodman, D. J. Peters, et al.. 1995. Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature 376:348–351.
   PubMed Web of Science ®Google Scholar
• Polesskaya, A., A. Duquet, I. Naguibneva, C. Weise, A. Vervisch, E. Bengal, F. Hucho, P. Robin, and A. Harel-Bellan. 2000. CREB-binding protein/p300 activates MyoD by acetylation. J. Biol. Chem. 275:34359–34364.
   PubMed Web of Science ®Google Scholar
• Puri, P. L., V. Sartorelli, X. J. Yang, Y. Hamamori, V. V. Ogryzko, B. H. Howard, L. Kedes, J. Y. Wang, A. Graessmann, Y. Nakatani, and M. Levrero. 1997. Differential roles of p300 and PCAF acetyltransferases in muscle differentiation. Mol. Cell 1:35–45.
   PubMed Web of Science ®Google Scholar
• Ramirez, S., S. Ait-Si-Ali, P. Robin, D. Trouche, and A. Harel-Bellan. 1997. The CREB-binding protein (CBP) cooperates with the serum response factor for transactivation of the c-fos serum response element. J. Biol. Chem. 272:31016–31021.
   PubMed Web of Science ®Google Scholar
• Sartorelli, V., J. Huang, Y. Hamamori, and L. Kedes. 1997. Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2C. Mol. Cell. Biol. 17:1010–1026.
   PubMed Web of Science ®Google Scholar
• Sartorelli, V., P. L. Puri, Y. Hamamori, V. Ogryzko, G. Chung, Y. Nakatani, J. Y. Wang, and L. Kedes. 1999. Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program. Mol. Cell 4:725–734.
   PubMed Web of Science ®Google Scholar
• Soutoglou, E., N. Katrakili, and I. Talianidis. 2000. Acetylation regulated transcription factor activity at multiple levels. Mol. Cell 5:745–751.
   PubMed Web of Science ®Google Scholar
• Thayer, M. J., and H. Weintraub. 1993. A cellular factor stimulates the DNA-binding activity of MyoD and E47. Proc. Natl. Acad. Sci. USA 90:6483–6487.
   PubMedGoogle Scholar
• Tomita, A., M. Towatari, S. Tsuzuki, F. Hayakawa, H. Kosugi, K. Tamai, T. Miyazaki, T. Kinoshita, and H. Saito. 2000. c-Myb acetylation at the carboxyl-terminal conserved domain by transcriptional co-activator p300. Oncogene 19:444–451.
   PubMed Web of Science ®Google Scholar
• Trouche, D., M. Grigoriev, J. L. Lenormand, P. Robin, S. A. Leibovitch, P. Sassone-Corsi, and A. Harel-Bellan. 1993. Repression of c-fos promoter by MyoD on muscle cell differentiation. Nature 363:79–82.
   PubMed Web of Science ®Google Scholar
• Turner, B. M.. 1998. Histone acetylation as an epigenetic determinant of long-term transcriptional competence. Cell Mol. Life Sci. 54:21–31.
   PubMed Web of Science ®Google Scholar
• Utley, R. T., K. Ikeda, P. A. Grant, J. Cote, D. J. Steger, A. Eberharter, S. John, and J. L. Workman. 1998. Transcriptional activators direct histone acetyltransferase complexes to nucleosomes. Nature 394:498–502.
   PubMed Web of Science ®Google Scholar
• Webster, G. A., and N. D. Perkins. 1999. Transcriptional cross talk between NF-κB and p53. Mol. Cell. Biol. 19:3485–3495.
   PubMed Web of Science ®Google Scholar
• Weintraub, H., V. J. Dwarki, I. Verma, R. Davis, S. Hollenberg, L. Snider, A. Lassar, and S. J. Tapscott. 1991. Muscle-specific transcriptional activation by MyoD. Genes Dev. 5:1377–1386.
   PubMed Web of Science ®Google Scholar
• Winston, F., and C. D. Allis. 1999. The bromodomain: a chromatin-targeting module?. Nat. Struct. Biol. 6:601–604.
   PubMedGoogle Scholar
• Wolffe, A. P.. 1994. Transcriptional activation. Switched-on chromatin. Curr. Biol. 4:525–528.
   PubMedGoogle Scholar
• Wolffe, A. P., and D. Pruss. 1996. Targeting chromatin disruption: transcription regulators that acetylate histones. Cell 84:817–819.
   PubMed Web of Science ®Google Scholar
• Yang, X. J., V. V. Ogryzko, J. Nishikawa, B. H. Howard, and Y. Nakatani. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319–324.
   PubMed Web of Science ®Google Scholar
• Yao, T. P., S. P. Oh, M. Fuchs, N. D. Zhou, L. E. Ch'ng, D. Newsome, R. T. Bronson, E. Li, D. M. Livingston, and R. Eckner. 1998. Gene dosage-dependent embryonic development and proliferation defects in mice lacking the transcriptional integrator p300. Cell 93:361–372.
   PubMed Web of Science ®Google Scholar
• Yuan, W., G. Condorelli, M. Caruso, A. Felsani, and A. Giordano. 1996. Human p300 protein is a coactivator for the transcription factor MyoD. J. Biol. Chem. 271:9009–9013.
   PubMed Web of Science ®Google Scholar