Abstract
Histones acetylation and deacetylation constitute part of the so-called “histone code” and work in concert with other posttranslational modifications to determine the activity of genes. Deacetylation of histone is carried out by a class of enzymes, known as histone deacetylases (HDACs). The action of HDAC is countered by histone acetyltransferases. Although histone is the best characterized substrate of HDACs, increasing evidence also indicates that non-histone proteins are equally important subtract of HDACs. Since HDACs play an important role in normal physiological and pathophysiological conditions, a sensitive and flexible deacetylation assay that can reliably detect HDAC activity and identify potential novel targets of HDACs is critical.
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References
Strahl BD, Allis CD (2000) The language of covalent histone modifications. Nature 403:41–45
Leipe DD, Landsman D (1997) Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily. Nucleic Acids Res 25:3693–3697
Gregoretti IV, Lee YM, Goodson HV (2004) Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J Mol Biol 338:17–31
Taunton J, Hassig CA, Schreiber SL (1996) A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272:408–411
de Ruijter AJ, van Gennip AH, Caron HN, Kemp S, van Kuilenburg AB (2003) Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem J 370:737–749
Takami Y, Nakayama T (2000) N-terminal region, C-terminal region, nuclear export signal, and deacetylation activity of histone deacetylase-3 are essential for the viability of the DT40 chicken B cell line. J Biol Chem 275:16191–16201
Yang WM, Tsai SC, Wen YD, Fejer G, Seto E (2002) Functional domains of histone deacetylase-3. J Biol Chem 277:9447–9454
Witt O, Deubzer HE, Milde T, Oehme I (2009) HDAC family: what are the cancer relevant targets? Cancer Lett 277:8–21
Haigis MC, Guarente LP (2006) Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction. Genes Dev 20:2913–2921
Gao L, Cueto MA, Asselbergs F, Atadja P (2002) Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J Biol Chem 277:25748–25755
Senese S, Zaragoza K, Minardi S, Muradore I, Ronzoni S, Passafaro A, Bernard L, Draetta GF, Alcalay M, Seiser C, Chiocca S (2007) Role for histone deacetylase 1 in human tumor cell proliferation. Mol Cell Biol 27:4784–4795
Zupkovitz G, Grausenburger R, Brunmeir R, Senese S, Tischler J, Jurkin J, Rembold M, Meunier D, Egger G, Lagger S, Chiocca S, Propst F, Weitzer G, Seiser C (2010) The cyclin-dependent kinase inhibitor p21 is a crucial target for histone deacetylase 1 as a regulator of cellular proliferation. Mol Cell Biol 30:1171–1181
Haberland M, Montgomery RL, Olson EN (2009) The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat Rev Genet 10:32–42
Lagger G, O'Carroll D, Rembold M, Khier H, Tischler J, Weitzer G, Schuettengruber B, Hauser C, Brunmeir R, Jenuwein T, Seiser C (2002) Essential function of histone deacetylase 1 in proliferation control and CDK inhibitor repression. EMBO J 21:2672–2681
Karwowska-Desaulniers P, Ketko A, Kamath N, Pflum MK (2007) Histone deacetylase 1 phosphorylation at S421 and S423 is constitutive in vivo, but dispensable in vitro. Biochem Biophys Res Commun 361:349–355
Pflum MK, Tong JK, Lane WS, Schreiber SL (2001) Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation. J Biol Chem 276:47733–47741
Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005) Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol 23:94–101
Sun JM, Chen HY, Davie JR (2007) Differential distribution of unmodified and phosphorylated histone deacetylase 2 in chromatin. J Biol Chem 282:33227–33236
Tsai SC, Seto E (2002) Regulation of histone deacetylase 2 by protein kinase CK2. J Biol Chem 277:31826–31833
Wu MY, Fu J, Xiao X, Wu J, Wu RC (2014) MiR-34a regulates therapy resistance by targeting HDAC1 and HDAC7 in breast cancer. Cancer Lett 354:311–319
Acknowledgements
Work in the authors’ laboratory is supported by grants CA187857 and CA188471 from National Cancer Institute, and McCormick Genomic and Proteomic Center at the George Washington University.
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Wu, MY., Wu, RC. (2016). A Sensitive and Flexible Assay for Determining Histone Deacetylase 1 (HDAC1) Activity. In: Sarkar, S. (eds) Histone Deacetylases. Methods in Molecular Biology, vol 1436. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-3667-0_1
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DOI: https://doi.org/10.1007/978-1-4939-3667-0_1
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