메뉴 건너뛰기




Volumn 2, Issue , 2012, Pages

Histone deacetylase inhibitors globally enhance H3/H4 tail acetylation without affecting H3 lysine 56 acetylation

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84942102316     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep00220     Document Type: Article
Times cited : (71)

References (54)
  • 1
    • 0036307707 scopus 로고    scopus 로고
    • Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 A resolution
    • Davey, C. A., Sargent, D. F., Luger, K, Maeder, A. W. & Richmond, T. J. Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 A resolution. J Mol Biol 319, 1097-1113 (2002).
    • (2002) J Mol Biol , vol.319 , pp. 1097-1113
    • Davey, C.A.1    Sargent, D.F.2    Luger, K.3    Maeder, A.W.4    Richmond, T.J.5
  • 2
    • 33644625997 scopus 로고    scopus 로고
    • Dynamic nucleosomes
    • Luger, K. Dynamic nucleosomes. Chromosome Res 14, 5-16 (2006).
    • (2006) Chromosome Res , vol.14 , pp. 5-16
    • Luger, K.1
  • 3
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. Chromatin modifications and their function. Cell 128, 693-705 (2007).
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 4
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycleregulated histone H3 lysine 56 acétylation in the DNA damage response
    • Masumoto, H., Hawke, D., Kobayashi, R. & Verreault, A. A role for cell-cycleregulated histone H3 lysine 56 acétylation in the DNA damage response. Nature 436, 294-298 (2005).
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 5
    • 0037077178 scopus 로고    scopus 로고
    • Dotlp modulates silencing in yeast by méthylation of the nucleosome core
    • Van Leeuwen, F., Gafken, P. R. & Gottschling, D. E. Dotlp modulates silencing in yeast by méthylation of the nucleosome core. Cell 109, 745-756 (2002).
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 6
    • 15944416371 scopus 로고    scopus 로고
    • Histone H4 lysine 91 acétylation: A core domain modification associated with chromatin assembly
    • Ye, J. et al. Histone H4 lysine 91 acétylation: a core domain modification associated with chromatin assembly. Mol Cell 18, 123-130 (2005).
    • (2005) Mol Cell , vol.18 , pp. 123-130
    • Ye, J.1
  • 7
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D. & Allis, C. D. The language of covalent histone modifications. Nature 403, 41-45 (2000).
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 8
    • 0035680767 scopus 로고    scopus 로고
    • Chromatin structure and dynamics: Functional implications
    • Morales, V. et al. Chromatin structure and dynamics: functional implications. Biochimie 83, 1029-1039 (2001).
    • (2001) Biochimie , vol.83 , pp. 1029-1039
    • Morales, V.1
  • 9
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden, J. E., Peart, M. J. & Johnstone, R. W. Anticancer activities of histone deacetylase inhibitors. Nat Rev Drug Discov 5, 769-784 (2006).
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 10
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida, M., Kijima, M., Akita, M. & Beppu, T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 265, 17174-17179 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 11
    • 1842631408 scopus 로고    scopus 로고
    • Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer
    • Halkidou, K. et al. Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer. Prostate 59, 177-189 (2004).
    • (2004) Prostate , vol.59 , pp. 177-189
    • Halkidou, K.1
  • 12
    • 0035962644 scopus 로고    scopus 로고
    • Histone deacetylases: A common molecular target for differentiation treatment of acute myeloid leukemias?
    • Minucci, S., Nervi, C., Lo Coco, F. & Pelicci, P. G. Histone deacetylases: a common molecular target for differentiation treatment of acute myeloid leukemias? Oncogene 20, 3110-3115 (2001).
    • (2001) Oncogene , vol.20 , pp. 3110-3115
    • Minucci, S.1    Nervi, C.2    Lo Coco, F.3    Pelicci, P.G.4
  • 13
    • 20144388146 scopus 로고    scopus 로고
    • Loss of acetylation at Lysl6 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer
    • Fraga, M. F. et al. Loss of acetylation at Lysl6 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer. Nat Genet 37, 391-400 (2005).
    • (2005) Nat Genet , vol.37 , pp. 391-400
    • Fraga, M.F.1
  • 15
    • 67449127082 scopus 로고    scopus 로고
    • Clinical studies of histone deacetylase inhibitors
    • Prince, H. M., Bishton, M. J. & Harrison, S. J. Clinical studies of histone deacetylase inhibitors. Clin Cancer Res 15, 3958-3969 (2009).
    • (2009) Clin Cancer Res , vol.15 , pp. 3958-3969
    • Prince, H.M.1    Bishton, M.J.2    Harrison, S.J.3
  • 17
    • 67449145358 scopus 로고    scopus 로고
    • Rational combinations using HDAC inhibitors
    • Bots, M. & Johnstone, R. W. Rational combinations using HDAC inhibitors. Clin Cancer Res 15, 3970-3977 (2009).
    • (2009) Clin Cancer Res , vol.15 , pp. 3970-3977
    • Bots, M.1    Johnstone, R.W.2
  • 18
    • 36048958965 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Overview and perspectives
    • Dokmanovic, M., Clarke, C. & Marks, P. A. Histone deacetylase inhibitors: overview and perspectives. Mol Cancer Res 5, 981-989 (2007).
    • (2007) Mol Cancer Res , vol.5 , pp. 981-989
    • Dokmanovic, M.1    Clarke, C.2    Marks, P.A.3
  • 19
    • 36148950997 scopus 로고    scopus 로고
    • FDA approval summary: Vorinostat for treatment of advanced primary cutaneous T-cell lymphoma
    • Mann, B. S., Johnson, J. R., Cohen, M. H., Justice, R. & Pazdur, R. FDA approval summary: vorinostat for treatment of advanced primary cutaneous T-cell lymphoma. Oncologist 12, 1247-1252 (2007).
    • (2007) Oncologist , vol.12 , pp. 1247-1252
    • Mann, B.S.1    Johnson, J.R.2    Cohen, M.H.3    Justice, R.4    Pazdur, R.5
  • 20
    • 77749309291 scopus 로고    scopus 로고
    • Romidepsin for the treatment of cutaneous T-cell lymphoma
    • Campas-Moya, C. Romidepsin for the treatment of cutaneous T-cell lymphoma. Drugs Today (Bare) 45, 787-795 (2009).
    • (2009) Drugs Today (Bare) , vol.45 , pp. 787-795
    • Campas-Moya, C.1
  • 21
    • 34547094822 scopus 로고    scopus 로고
    • Distinct pharmacological properties of second generation HDAC inhibitors with the benzamide or hydroxamate head group
    • Beckers, T. et al. Distinct pharmacological properties of second generation HDAC inhibitors with the benzamide or hydroxamate head group. Int J Cancer 121, 1138-1148 (2007).
    • (2007) Int J Cancer , vol.121 , pp. 1138-1148
    • Beckers, T.1
  • 22
    • 67349157687 scopus 로고    scopus 로고
    • Biomarkers for predicting clinical responses to HDAC inhibitors
    • Stimson, L. & La Thangue, N. B. Biomarkers for predicting clinical responses to HDAC inhibitors. Cancer Lett 280, 177-183 (2009).
    • (2009) Cancer Lett , vol.280 , pp. 177-183
    • Stimson, L.1    La Thangue, N.B.2
  • 23
    • 78649410782 scopus 로고    scopus 로고
    • Intact mass detection, interpretation, and visualization to automate Top-Down proteomics on a large scale
    • Durbin, K. R. et al. Intact mass detection, interpretation, and visualization to automate Top-Down proteomics on a large scale. Proteomics 10, 3589-3597 (2010).
    • (2010) Proteomics , vol.10 , pp. 3589-3597
    • Durbin, K.R.1
  • 24
    • 70449705871 scopus 로고    scopus 로고
    • Efficient readout of posttranslational codes on the 50-residue tail of histone H3 by high-resolution MS/MS
    • Siuti, N. & Kelleher, N. L. Efficient readout of posttranslational codes on the 50-residue tail of histone H3 by high-resolution MS/MS. Anal Biochem 396, 180-187 (2010).
    • (2010) Anal Biochem , vol.396 , pp. 180-187
    • Siuti, N.1    Kelleher, N.L.2
  • 25
    • 51549115454 scopus 로고    scopus 로고
    • Comprehensive profiling of histone modifications using a label-free approach and its applications in determining structure-function relationships
    • Drogaris, P., Wurtele, H., Masumoto, H., Verreault, A. & Thibault, P. Comprehensive profiling of histone modifications using a label-free approach and its applications in determining structure-function relationships. Anal Chem 80, 6698-6707 (2008).
    • (2008) Anal Chem , vol.80 , pp. 6698-6707
    • Drogaris, P.1    Wurtele, H.2    Masumoto, H.3    Verreault, A.4    Thibault, P.5
  • 26
    • 77952094640 scopus 로고    scopus 로고
    • Differential sensitivity of human leukemic cell lines to the histone deacetylase inhibitor trichostatin A
    • Ninios, Y. P., Sekeri-Pataryas, K. E. & Sourlingas, T. G. Differential sensitivity of human leukemic cell lines to the histone deacetylase inhibitor trichostatin A. Leukemia Res 34, 786-792 (2010).
    • (2010) Leukemia Res , vol.34 , pp. 786-792
    • Ninios, Y.P.1    Sekeri-Pataryas, K.E.2    Sourlingas, T.G.3
  • 27
    • 0036527775 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone, R. W. Histone deacetylase inhibitors: novel drugs for the treatment of cancer. Nat Rev Drug Discovery 1, 287-299 (2002).
    • (2002) Nat Rev Drug Discovery , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 28
    • 33646908631 scopus 로고    scopus 로고
    • Modifications of H3 and H4 during chromatin replication, nucleosome assembly, and histone exchange
    • Benson, L. J. et al. Modifications of H3 and H4 during chromatin replication, nucleosome assembly, and histone exchange. JBiol Chem 281, 9287-9296 (2006).
    • (2006) JBiol Chem , vol.281 , pp. 9287-9296
    • Benson, L.J.1
  • 29
    • 33749657892 scopus 로고    scopus 로고
    • PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state
    • Loyola, A., Bonaldi, T., Roche, D., Imhof, A. & Almouzni, G. PTMs on H3 variants before chromatin assembly potentiate their final epigenetic state. Mol Cell 24, 309-316 (2006).
    • (2006) Mol Cell , vol.24 , pp. 309-316
    • Loyola, A.1    Bonaldi, T.2    Roche, D.3    Imhof, A.4    Almouzni, G.5
  • 30
    • 0028847955 scopus 로고
    • Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4
    • Sobel, R. E., Cook, R. G., Perry, C. A., Annunziato, A. T. & Allis, C. D. Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4. Proc Natl Acad Sci USA 92, 1237-1241 (1995).
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1237-1241
    • Sobel, R.E.1    Cook, R.G.2    Perry, C.A.3    Annunziato, A.T.4    Allis, C.D.5
  • 31
    • 0030272047 scopus 로고    scopus 로고
    • Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
    • Verreault, A., Kaufman, P. D., Kobayashi, R. & Stillman, B. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 87, 95-104 (1996).
    • (1996) Cell , vol.87 , pp. 95-104
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 32
    • 27744538093 scopus 로고    scopus 로고
    • Resazurin assay of radiation response in cultured cells
    • Anoopkumar-Dukie, S. et al. Resazurin assay of radiation response in cultured cells. Br J Radiol 78, 945-947 (2005).
    • (2005) Br J Radiol , vol.78 , pp. 945-947
    • Anoopkumar-Dukie, S.1
  • 33
    • 0141755383 scopus 로고    scopus 로고
    • An N-α-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A
    • Song, O. K, Wang, X., Waterborg, J. H. & Sternglanz, R. An N-α-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A. J Biol Chem 278, 38109-38112 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 38109-38112
    • Song, O.K.1    Wang, X.2    Waterborg, J.H.3    Sternglanz, R.4
  • 34
  • 35
    • 70349333702 scopus 로고    scopus 로고
    • Epigenetic and replacement roles of histone variant H3.3 in reproduction and development
    • Orsi, G. A., Couble, P. & Loppin, B. Epigenetic and replacement roles of histone variant H3.3 in reproduction and development. Int J Dev Biol 53, 231-243 (2009).
    • (2009) Int J Dev Biol , vol.53 , pp. 231-243
    • Orsi, G.A.1    Couble, P.2    Loppin, B.3
  • 36
    • 79960590601 scopus 로고    scopus 로고
    • ABRF-PRG07: Advanced quantitative proteomics study
    • Falick, A. M. et al. ABRF-PRG07: advanced quantitative proteomics study. J Biomol Tech 22, 21-26 (2011).
    • (2011) J Biomol Tech , vol.22 , pp. 21-26
    • Falick, A.M.1
  • 37
    • 56149086397 scopus 로고    scopus 로고
    • Decision tree-driven tandem mass spectrometry for shotgun proteomics
    • Swaney, D. L., McAlister, G. C. & Coon, J. J. Decision tree-driven tandem mass spectrometry for shotgun proteomics. Nat Methods 5, 959-964 (2008).
    • (2008) Nat Methods , vol.5 , pp. 959-964
    • Swaney, D.L.1    McAlister, G.C.2    Coon, J.J.3
  • 38
    • 80054062798 scopus 로고    scopus 로고
    • ASF1A and ATM regulate H3K56-mediated cellcycle checkpoint recovery in response to UV irradiation
    • Battu, A., Ray, A. & Wani, A. A. ASF1A and ATM regulate H3K56-mediated cellcycle checkpoint recovery in response to UV irradiation. Nucleic Acids Res 39, 7931-7945 (2011).
    • (2011) Nucleic Acids Res , vol.39 , pp. 7931-7945
    • Battu, A.1    Ray, A.2    Wani, A.A.3
  • 39
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das, C., Lucia, M. S., Hansen, K. C. & Tyler, J. K. CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 459, 113-117 (2009).
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 40
    • 79955773522 scopus 로고    scopus 로고
    • The type III histone deacetylase Sirtl protein suppresses p300-mediated histone H3 lysine 56 acetylation at Bclafl promoter to inhibit T cell activation
    • Kong, S. et al. The type III histone deacetylase Sirtl protein suppresses p300-mediated histone H3 lysine 56 acetylation at Bclafl promoter to inhibit T cell activation. J Biol Chem 286, 16967-16975 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 16967-16975
    • Kong, S.1
  • 41
    • 84945580519 scopus 로고    scopus 로고
    • And-1 is required for the stability of histone acetyltransferase
    • 21987584 Epub ahead of print
    • Li, Y. et al. And-1 is required for the stability of histone acetyltransferase Gcn5. Oncogene [Epub ahead of print] PMID: 21987584 (2011).
    • (2011) Gcn5. Oncogene
    • Li, Y.1
  • 42
    • 79957950591 scopus 로고    scopus 로고
    • Genome-wide profiling of H3K56 acetylation and transcription factor binding sites in human adipocytes
    • Lo, K. A. et al. Genome-wide profiling of H3K56 acetylation and transcription factor binding sites in human adipocytes. PLoS One 6, el9778 (2011).
    • (2011) PLoS One , vol.6 , pp. el9778
    • Lo, K.A.1
  • 43
    • 69249221533 scopus 로고    scopus 로고
    • Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6
    • Michishita, E. et al. Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6. Cell Cycle 8, 2664-2666 (2009).
    • (2009) Cell Cycle , vol.8 , pp. 2664-2666
    • Michishita, E.1
  • 44
    • 77956341931 scopus 로고    scopus 로고
    • Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining
    • Miller, K. M. et al. Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining. Nat Struct Mol Biol 17, 1144-1151 (2010).
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1144-1151
    • Miller, K.M.1
  • 45
    • 78650724968 scopus 로고    scopus 로고
    • Neural sirtuin 6 (Sirt6) ablation attenuates somatic growth and causes obesity
    • Schwer, B. et al. Neural sirtuin 6 (Sirt6) ablation attenuates somatic growth and causes obesity. Proc Natl Acad Sci USA 107, 21790-21794 (2010).
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 21790-21794
    • Schwer, B.1
  • 46
    • 67650409769 scopus 로고    scopus 로고
    • Screen for DNA-damage-responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells
    • Tjeertes, J. V., Miller, K. M. & Jackson, S. P. Screen for DNA-damage-responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells. EMBO J 28, 1878-1889 (2009).
    • (2009) EMBO J , vol.28 , pp. 1878-1889
    • Tjeertes, J.V.1    Miller, K.M.2    Jackson, S.P.3
  • 47
    • 84855200286 scopus 로고    scopus 로고
    • DNA damage in the presence of chemical genotoxic agents induce acetylation of H3K56 and H4K16 but not H3K9 in mammalian cells
    • Vempati, R. K. & Haidar, D. DNA damage in the presence of chemical genotoxic agents induce acetylation of H3K56 and H4K16 but not H3K9 in mammalian cells. Mol Biol Rep 39, 303-308 (2012).
    • (2012) Mol Biol Rep , vol.39 , pp. 303-308
    • Vempati, R.K.1    Haidar, D.2
  • 48
    • 77956553913 scopus 로고    scopus 로고
    • p300-mediated acetylation of histone H3 lysine 56 functions in DNA damage response in mammals
    • Vempati, R. K. et al. p300-mediated acetylation of histone H3 lysine 56 functions in DNA damage response in mammals. J Biol Chem 285, 28553-28564 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 28553-28564
    • Vempati, R.K.1
  • 49
    • 60549111235 scopus 로고    scopus 로고
    • Histone H3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells
    • Xie, W. et al. Histone H3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells. Mol Cell 33, 417-427 (2009).
    • (2009) Mol Cell , vol.33 , pp. 417-427
    • Xie, W.1
  • 50
    • 66749102871 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is important for genomic stability in mammals
    • Yuan, J., Pu, M., Zhang, Z. & Lou, Z. Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle 8, 1747-1753 (2009).
    • (2009) Cell Cycle , vol.8 , pp. 1747-1753
    • Yuan, J.1    Pu, M.2    Zhang, Z.3    Lou, Z.4
  • 51
    • 33745520486 scopus 로고    scopus 로고
    • The sirtuins Hst3 and Hst4p preserve genome integrity by controlling histone H3 lysine 56 deacetylation
    • Celic, I. et al. The sirtuins Hst3 and Hst4p preserve genome integrity by controlling histone H3 lysine 56 deacetylation. Curr Biol 16, 1280-1289 (2006).
    • (2006) Curr Biol , vol.16 , pp. 1280-1289
    • Celic, I.1
  • 52
    • 0035986095 scopus 로고    scopus 로고
    • Dynamics of histone acetylation in vivo. A function for acetylation turnover?
    • Waterborg, J. H. Dynamics of histone acetylation in vivo. A function for acetylation turnover? Biochem Cell Biol 80, 363-378 (2002).
    • (2002) Biochem Cell Biol , vol.80 , pp. 363-378
    • Waterborg, J.H.1
  • 53
    • 80054062798 scopus 로고    scopus 로고
    • ASF1A and ATM regulate H3K56-mediated cellcycle checkpoint recovery in response to UV irradiation
    • Battu, A., Ray, A. & Wani, A. A. ASF1A and ATM regulate H3K56-mediated cellcycle checkpoint recovery in response to UV irradiation. Nucleic Acids Res 39, 7931-7945 (2011).
    • (2011) Nucleic Acids Res , vol.39 , pp. 7931-7945
    • Battu, A.1    Ray, A.2    Wani, A.A.3
  • 54
    • 1542334851 scopus 로고    scopus 로고
    • Reconstitution of nucleosome core particles from recombinant histones and DNA
    • Dyer, P. N. et al. Reconstitution of nucleosome core particles from recombinant histones and DNA. Methods Enzymol 375, 23-44 (2004).
    • (2004) Methods Enzymol , vol.375 , pp. 23-44
    • Dyer, P.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.