Abstract
It has recently been demonstrated that bromodomains — motifs found in several eukaryotic transcription factors — bind to acetyl-lysine, a modification of histones that is important for transcription. This finding suggests that the regulatory effects of histone acetylation may be exerted by bromodomain-containing proteins.
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References
Jeanmougin, F., Wurtz, J.-M., Le Douarin, B., Chambon, P. & Losson, R. Trends in Biochemical Sciences 22, 151–153 (1997).
Dhalluin, C. et al. Nature 399, 491–496 (1999).
Tamkun, J.W. et al. Cell 68, 561–572 (1992).
Hanes, S.R. et al. Nucleic Acids Res. 20, 2603–'(1992).
Struhl, K. Genes Dev 12, 599–606 (1998).
Workman, J.L. & Kingston, R.E. Annu. Rev. Biochem. 67, 545–579 (1998).
Dutnall, R.N., Tafrov, S.T., Sternglanz, R. & Ramakrishnan, V. Cell 94, 427–438 (1998).
Ornaghi, P., Ballario, P., Lena, A.M., Gonzalez, A. & Filetici, P. J. Mol. Biol. 287, 1–7 (1999).
Schiltz, R.L. et al. J. Biol. Chem. 274, 1189–1192 (1999).
Pawson, T. Nature 373, 573–580 (1995).
Sudol, M. Oncogene 17, 1469–1474 (1998).
Sterner, D.E. et al. Mol. Cell. Biol. 19, 86–98 (1999).
Gansheroff, L.J., Dollard, C., Tan, P. & Winston, F. Genetics 139, 523–536 (1995).
Laurent, B.C., Treich, I. & Carlson, M. Genes Dev. 7, 583–591 (1993).
Elfring, L.K. et al. Genetics 148, 251–65 (1998).
Hampsey, M. Microbiol. Mol. Biol. Rev. 62, 465–503 (1998).
Muchardt, C. & Yaniv, M. EMBO J. 12, 4279–4290 (1993).
Chua, P. & Roeder, G.S. Mol. Cell. Biol. 15, 3685–3696 (1995).
Cairns, B.R. et al. Cell 87, 1249–1260 (1996).
Du, J., Nasir, I., Benton, B.K., Kladde, M.P. & Laurent, B.C. Genetics 150, 987–1005 (1998).
Travers, A. Cell 96, 311–314 (1999).
Gu, W. & Roeder, R.G. Cell 90, 595–606 (1997).
Imhof, A. et al. Curr. Biol. 7, 689–692 (1997).
Pollard, K.J. & Peterson, C.L. Mol. Cell Biol. 17, 6212–6222 (1997).
Liu, L. et al. Mol. Cell. Biol. 19, 1202–1209 (1999).
Lin, R., Leone, J.W., Cook, R.G. & Allis, C.D. J. Cell Biol. 108, 1577–1588 (1989).
Turner, B.M., Birley, A.J. & Lavender, J. Cell 69, 375–384 (1992).
Barlev, N.A., et al. Mol Cell. Biol. 18, 1349–58 (1998).
Cosma, M.P., Tanaka, T. & Nasmyth, K. Cell 97, 299–311 (1999).
Natarajan, K., Jackson, B.M., Rhee, E. & Hinnebusch, A.G. Mol. Cell 2, 683–692 (1998).
Lin, Y., Fletcher, C.M., Zhou, J., Allis, C.D. & Wagner, G. Nature, in the press (1999).
Trievel, R.C. et al. Proc. Natl. Acad. Sci. USA, in the press (1999).
Herrera, J.E., Bergei, M., Yang, X.-J., Nakatani, Y. & Bustin, M. J. Biol. Chem. 272, 27253–27258 (1997).
Koonin, E.V., Zhou, S. & Lucchesi, J.C. Nucleic Acids Res. 23, 4229–4233 (1995).
Cavalli, G. & Paro, R. Curr. Opin. Cell. Biol. 10, 354–360 (1998).
Ball, L.J. et al. EMBO J. 16, 2473–2481 (1997).
Braunstein, M., Sobel, R.E., Allis, C.D., Turner, B.M. & Broach, J.R. Mol. Cell. Biol. 16, 4349–4356 (1996).
Paro, R. & Hogness, D.S. Proc. Natl. Acad. Sci. USA 88, 263–267 (1991).
Hilfiker, A., Hilfiker-Kleiner, D., Pannuti, A. & Lucchesi, J.C. EMBO J. 16, 2054–2060 (1997).
Brownell, J.E. & Allis, C.D. Curr. Opin. Genet. Dev. 6, 176–184 (1996).
Wolffe, A.P. & Hayes, J.J. Nucleic. Acids. Res. 27, 711–720 (1999).
Wei, Y., Yu, L., Bowen, J., Gorovsky, M.A. & Allis, C.D. Cell 97, 99–109 (1999).
Hirano, T. Genes Dev. 13, 11–19 (1999).
Acknowledgements
We apologize to the many colleagues whose work could not be referenced because of space limitations. We thank M.-H. Kuo for providing Fig. 2. Work in our labs is supported by grants from the National Institutes of Health.
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Winston, F., Allis, C. The bromodomain: a chromatin-targeting module?. Nat Struct Mol Biol 6, 601–604 (1999). https://doi.org/10.1038/10640
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DOI: https://doi.org/10.1038/10640
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