Gene Therapy & Molecular Biology Volume 7 Issue A

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Spencer and Davie: Dynamic histone acetylation and its involvement in transcription distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains. Mol Cell 4, 715-723. Cervoni N and Szyf M (2001) Demethylase activity is directed by histone acetylation. J Biol Chem 276, 40778-40787. Chen H, Lin RJ, Xie W, Wilpitz D, and Evans RM (1999) Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell 98, 675686. Cheung P, Tanner KG, Cheung WL, Sassone-Corsi P, Denu JM, and Allis CD (2000) Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol Cell 5, 905-915. Cho H, Orphanides G, Sun X, Yang XJ, Ogryzko V, Lees E, Nakatani Y, and Reinberg D (1998). A human RNA polymerase II complex containing factors that modify chromatin structure. Mol Cell Biol 18, 5355-5363. Covault J and Chalkley R (1980) The identification of distinct populations of acetylated histone. J Biol Chem 255, 91109116. Crane-Robinson C, Myers FA, Hebbes TR, Clayton AL, and Thorne AW (1999). Chromatin immunoprecipitation assays in acetylation mapping of higher eukaryotes. Methods Enzymol 304, 533-547. Davie JR (1995) The nuclear matrix and the regulation of chromatin organization and function. Int Rev Cytol 162A, 191-250. Davie JR and Moniwa M (2000) Control of chromatin remodeling. Crit Rev Eukaryot Gene Expr 10, 303-325. Davie JR and Spencer VA (1999) Control of histone modifications. J Cell Biochem Suppl 32-33, 141-148. Davie JR and Spencer VA (2001) Signal transduction pathways and the modification of chromatin structure. Prog Nucleic Acid Res Mol Biol 65, 299-340. De Rubertis F, Kadosh D, Henchoz S, Pauli D, Reuter G, Struhl K, and Spierer P (1996) The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast. Nature 384, 589-591. Downes M, Ordentlich P, Kao HY, Alvarez JG, and Evans RM (2000) Identification of a nuclear domain with deacetylase activity. Proc Natl Acad Sci USA 97, 10330-10335. Fisher AL and Caudy M (1998) Groucho proteins: transcriptional corepressors for specific subsets of DNA-binding transcription factors in vertebrates and invertebrates. Genes Dev 12, 1931-1940. Frye RA (1999) Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADPribosyltransferase activity. Biochem Biophys Res Commun 260, 273-279. Frye RA (2000) Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem Biophys Res Commun 273, 793-798. Garcia-Ramirez M, Rocchini C, and Ausio J (1995) Modulation of chromatin folding by histone acetylation. J Biol Chem 270, 17923-17928. Grant PA, Eberharter A, John S, Cook RG, Turner BM, and Workman JL (1999) Expanded lysine acetylation specificity of Gcn5 in native complexes. J Biol Chem 274, 5895-5900. Gregory PD, Schmid A, Zavari M, Munsterkotter M, and Horz W (1999) Chromatin remodeling at the PHO8 promoter requires SWI-SNF and SAGA at a step subsequent to activator binding. EMBO J 18, 6407-6414.

A recent study mapping the distribution of di-methylated lysine 9 on H3 across the chicken $-globin domain during erythropoiesis showed that regions enriched in methylated lysine 9 were depleted of di-acetylated H3 (K9 and K14). However, H3 acetylation correlated with lysine 4 methylation, suggesting that transcriptional activation is associated with H3 methylated at K4, as well as with acetylated H3 and H4 isoforms (Litt et al, 2001). Likewise, in Tetrahymena, methylated Lys4 of H3 is found only in transcriptionally active macronuclei (Strahl et al, 1999).

Acknowledgments Research supported by grants from the Canadian Institutes of Health Research (CIHR) (MT-9186,RO15183), CancerCare Manitoba, and the U.S. Army Medical and Materiel Command Breast Cancer Research Program (#DAM17-00-1-0319), and the National Cancer Institute of Canada with funds from the Canadian Cancer Society. A CIHR Senior Scientist Award to J.R.D. and a U.S. Army Medical and Materiel Command Fellowship to V.A.S. are gratefully acknowledged.

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