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Volumn 326, Issue 4, 2005, Pages 811-816

Histone acetylation regulates both transcription initiation and elongation of hsp22 gene in Drosophila

Author keywords

Drosophila melanogaster; Heat shock factor; Histone acetylation; Histone deacetylase inhibitors; hsp22; RNA polymerase II; Transcription regulation

Indexed keywords

BUTYRIC ACID; HEAT SHOCK PROTEIN; HISTONE; HISTONE H3; RNA POLYMERASE II; TRICHOSTATIN A;

EID: 10644242733     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.11.118     Document Type: Article
Times cited : (19)

References (34)
  • 1
    • 0034254857 scopus 로고    scopus 로고
    • NuRD and SIN3: Histone deacetylase complexes in development
    • J. Ahringer NuRD and SIN3: histone deacetylase complexes in development Trends Genet. 16 2000 351 356
    • (2000) Trends Genet. , vol.16 , pp. 351-356
    • Ahringer, J.1
  • 2
    • 0343416249 scopus 로고    scopus 로고
    • Histone deacetylases: Silencers for hire
    • H.H. Ng, and A. Bird Histone deacetylases: silencers for hire Trends Biochem. Sci. 25 2000 121 126
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 121-126
    • Ng, H.H.1    Bird, A.2
  • 3
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 angstrom resolution
    • K. Luger, A.W. Mader, R.K. Richmond, D.F. Sargent, and T.J. Richmond Crystal structure of the nucleosome core particle at 2.8 angstrom resolution Nature 389 1997 251 260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 4
    • 0027525970 scopus 로고
    • Studies of the DNA binding properties of histone H4 amino acid terminus: Thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 tail to DNA
    • L. Hong, G.P. Schroth, H.R. Matthews, P. Yau, and E.M. Bradbury Studies of the DNA binding properties of histone H4 amino acid terminus: thermal denaturation studies reveal that acetylation markedly reduces the binding constant of the H4 tail to DNA J. Biol. Chem. 268 1993 305 314
    • (1993) J. Biol. Chem. , vol.268 , pp. 305-314
    • Hong, L.1    Schroth, G.P.2    Matthews, H.R.3    Yau, P.4    Bradbury, E.M.5
  • 5
    • 0033153358 scopus 로고    scopus 로고
    • Gene activation by histone and factor acetyltransferases
    • S.L. Berger Gene activation by histone and factor acetyltransferases Curr. Opin. Cell Biol. 11 1999 336 341
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 336-341
    • Berger, S.L.1
  • 6
    • 0033523203 scopus 로고    scopus 로고
    • Chromatin remodeling and transcriptional regulation
    • R.X. Luo, and D.C. Dean Chromatin remodeling and transcriptional regulation J. Natl. Cancer Inst. 91 1999 1288 1293
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 1288-1293
    • Luo, R.X.1    Dean, D.C.2
  • 7
    • 0032459466 scopus 로고    scopus 로고
    • Promoter-associated pausing in promoter architecture and postinitiation transcriptional regulation
    • J.T. Lis Promoter-associated pausing in promoter architecture and postinitiation transcriptional regulation Cold Spring Harbor Symp. Quant. Biol. 63 1998 347 356
    • (1998) Cold Spring Harbor Symp. Quant. Biol. , vol.63 , pp. 347-356
    • Lis, J.T.1
  • 8
    • 0028055116 scopus 로고
    • ATP-dependent nucleosome disruption at a heat-shock promoter mediated by binding of GAGA transcription factor
    • T. Tsukiyama, P.B. Becker, and C. Wu ATP-dependent nucleosome disruption at a heat-shock promoter mediated by binding of GAGA transcription factor Nature 367 1994 525 532
    • (1994) Nature , vol.367 , pp. 525-532
    • Tsukiyama, T.1    Becker, P.B.2    Wu, C.3
  • 9
    • 0028822276 scopus 로고
    • HSF access to heat shock elements in vivo depends critically on promoter architecture defined by GAGA factor, TFIID, and RNA polymerase II binding sites
    • L.S. Shopland, K. Hirayoshi, M. Fernandes, and J.T. Lis HSF access to heat shock elements in vivo depends critically on promoter architecture defined by GAGA factor, TFIID, and RNA polymerase II binding sites Genes Dev. 9 1995 2756 2769
    • (1995) Genes Dev. , vol.9 , pp. 2756-2769
    • Shopland, L.S.1    Hirayoshi, K.2    Fernandes, M.3    Lis, J.T.4
  • 10
    • 0036340406 scopus 로고    scopus 로고
    • GAGA factor and the TFIID complex collaborate in generating an open chromatin structure at the Drosophila melanogaster hsp26 promoter
    • B.A. Leibovtch, Q. Lu, L.R. Benjamin, Y. Liu, D.S. Gilmour, and S.C.R. Elgin GAGA factor and the TFIID complex collaborate in generating an open chromatin structure at the Drosophila melanogaster hsp26 promoter Mol. Cell. Biol. 22 2002 6148 6157
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6148-6157
    • Leibovtch, B.A.1    Lu, Q.2    Benjamin, L.R.3    Liu, Y.4    Gilmour, D.S.5    Elgin, S.C.R.6
  • 11
    • 0022725530 scopus 로고
    • Sequence requirement for expression of Drosophila melanogaster heat shock protein hsp22 gene during heat shock and normal development
    • R. Klemenz, and W.J. Gehring Sequence requirement for expression of Drosophila melanogaster heat shock protein hsp22 gene during heat shock and normal development Mol. Cell. Biol. 6 1986 2011 2119
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2011-2119
    • Klemenz, R.1    Gehring, W.J.2
  • 12
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • R.I. Morimoto Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators Genes Dev. 12 1998 3788 3796
    • (1998) Genes Dev. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 13
    • 0036919737 scopus 로고    scopus 로고
    • Histone acetylation is involved in hsp70 gene transcription regulation in Drosophila melanogaster
    • T. Chen, H. Sun, J. Lu, Y. Zhao, D. Tao, X. Li, and B. Huang Histone acetylation is involved in hsp70 gene transcription regulation in Drosophila melanogaster Arch. Biochem. Biophys. 408 2002 171 176
    • (2002) Arch. Biochem. Biophys. , vol.408 , pp. 171-176
    • Chen, T.1    Sun, H.2    Lu, J.3    Zhao, Y.4    Tao, D.5    Li, X.6    Huang, B.7
  • 14
    • 10344221614 scopus 로고    scopus 로고
    • Trichostatin a extends the lifespan of Drosophila melanogaster by elevating hsp22 expression
    • D. Tao, J. Lu, H. Sun, Y. Zhao, Z. Yuan, X. Li, and B. Huang Trichostatin A extends the lifespan of Drosophila melanogaster by elevating hsp22 expression Acta Biochim. Biophys. Sin. 36 2004 618 622
    • (2004) Acta Biochim. Biophys. Sin. , vol.36 , pp. 618-622
    • Tao, D.1    Lu, J.2    Sun, H.3    Zhao, Y.4    Yuan, Z.5    Li, X.6    Huang, B.7
  • 15
    • 0032476596 scopus 로고    scopus 로고
    • Xenopus NF-Y pre-sets chromatin to potentiate p300 and acetylation-responsive transcription from the Xenopus hsp70 promoter in vivo
    • Q. Li, M. Herrler, N. Landsberger, N. Kaludov, V.V. Ogryzko, Y. Nakatani, and A.P. Wolffe Xenopus NF-Y pre-sets chromatin to potentiate p300 and acetylation-responsive transcription from the Xenopus hsp70 promoter in vivo EMBO J. 17 1998 6300 6315
    • (1998) EMBO J. , vol.17 , pp. 6300-6315
    • Li, Q.1    Herrler, M.2    Landsberger, N.3    Kaludov, N.4    Ogryzko, V.V.5    Nakatani, Y.6    Wolffe, A.P.7
  • 16
    • 0038692918 scopus 로고    scopus 로고
    • Effect of histone deacetylase inhibitors on heat shock protein gene expression during Xenopus development
    • D.H. Ovakim, and J.J. Heikkila Effect of histone deacetylase inhibitors on heat shock protein gene expression during Xenopus development Genetics 36 2003 88 96
    • (2003) Genetics , vol.36 , pp. 88-96
    • Ovakim, D.H.1    Heikkila, J.J.2
  • 19
    • 0034667949 scopus 로고    scopus 로고
    • High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: Roles in promoter proximal pausing and transcription elongation
    • E.D. Andrulis, E. Guzman, P. Doring, J. Werner, and J.T. Lis High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: roles in promoter proximal pausing and transcription elongation Genes Dev. 14 2000 2635 2649
    • (2000) Genes Dev. , vol.14 , pp. 2635-2649
    • Andrulis, E.D.1    Guzman, E.2    Doring, P.3    Werner, J.4    Lis, J.T.5
  • 20
    • 0020709947 scopus 로고
    • Developmental regulation of Drosophila imaginal proteins: Synthesis of a heat shock protein under non-heat shock conditions
    • C.M. Cheney, and A. Shearn Developmental regulation of Drosophila imaginal proteins: synthesis of a heat shock protein under non-heat shock conditions Dev. Biol. 95 1983 325 330
    • (1983) Dev. Biol. , vol.95 , pp. 325-330
    • Cheney, C.M.1    Shearn, A.2
  • 21
    • 0025364688 scopus 로고
    • Developmental expression of Drosophila melanogaster small heat-shock proteins
    • C. Haass, U. Klein, and P.M. Kloetzel Developmental expression of Drosophila melanogaster small heat-shock proteins J. Cell Sci. 96 1990 413 418
    • (1990) J. Cell Sci. , vol.96 , pp. 413-418
    • Haass, C.1    Klein, U.2    Kloetzel, P.M.3
  • 22
    • 0002024938 scopus 로고
    • The expression of heat shock genes during normal development in Drosophila melanogaster
    • P.J. Mason, L.M.C. Hall, and J. Gausz The expression of heat shock genes during normal development in Drosophila melanogaster Mol. Gen. Genet. 194 1984 73 78
    • (1984) Mol. Gen. Genet. , vol.194 , pp. 73-78
    • Mason, P.J.1    Hall, L.M.C.2    Gausz, J.3
  • 23
    • 0030821356 scopus 로고    scopus 로고
    • Regulation of heat shock gene induction and expression during Drosophila development
    • S. Michaud, R. Marin, and R.M. Tanguay Regulation of heat shock gene induction and expression during Drosophila development Cell Mol. Life Sci. 53 1997 104 113
    • (1997) Cell Mol. Life Sci. , vol.53 , pp. 104-113
    • Michaud, S.1    Marin, R.2    Tanguay, R.M.3
  • 24
    • 0033104457 scopus 로고    scopus 로고
    • Aging-specific expression of Drosophila hsp22
    • V. King, and J. Tower Aging-specific expression of Drosophila hsp22 Dev. Biol. 207 1999 107 118
    • (1999) Dev. Biol. , vol.207 , pp. 107-118
    • King, V.1    Tower, J.2
  • 25
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin a
    • M. Yoshida, M. Kijima, M. Akita, and T. Beppu Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A J. Biol. Chem. 265 1990 17174 17179
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 26
    • 0041854193 scopus 로고    scopus 로고
    • Phosphorylation at serine 28 and acetylation at lysine 9 of histone H3 induced by trichostatin a
    • S. Zhong, H. Goto, M. Inagaki, and Z. Dong Phosphorylation at serine 28 and acetylation at lysine 9 of histone H3 induced by trichostatin A Oncogene 22 2003 5291 9297
    • (2003) Oncogene , vol.22 , pp. 5291-9297
    • Zhong, S.1    Goto, H.2    Inagaki, M.3    Dong, Z.4
  • 27
    • 0017864644 scopus 로고
    • The effect of sodium butyrate on histone modification
    • L. Sealy, and R. Chalkley The effect of sodium butyrate on histone modification Cell 14 1978 115 121
    • (1978) Cell , vol.14 , pp. 115-121
    • Sealy, L.1    Chalkley, R.2
  • 28
    • 0034071282 scopus 로고    scopus 로고
    • The intracellular target of butyrate's actions: HDAC or HDON'T?
    • P.R. Gibson The intracellular target of butyrate's actions: HDAC or HDON'T? Gut 46 2000 447 451
    • (2000) Gut , vol.46 , pp. 447-451
    • Gibson, P.R.1
  • 29
    • 0032525139 scopus 로고    scopus 로고
    • Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin
    • K.P. Nightingale, R.E. Wellinger, J.M. Sogo, and P.B. Becker Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin EMBO J. 17 1998 2865 2876
    • (1998) EMBO J. , vol.17 , pp. 2865-2876
    • Nightingale, K.P.1    Wellinger, R.E.2    Sogo, J.M.3    Becker, P.B.4
  • 30
    • 0026513698 scopus 로고
    • DNA sequence requirements for generating paused polymerase at the start of hsp70
    • H. Lee, K.W. Kraus, M.F. Wolfner, and J.T. Lis DNA sequence requirements for generating paused polymerase at the start of hsp70 Genes Dev. 6 1992 284 295
    • (1992) Genes Dev. , vol.6 , pp. 284-295
    • Lee, H.1    Kraus, K.W.2    Wolfner, M.F.3    Lis, J.T.4
  • 31
    • 0030982769 scopus 로고    scopus 로고
    • Molecular architecture of the hsp70 promoter after deletion of the TATA box or the upstream regulation region
    • J.A. Weber, D.J. Taxman, Q. Lu, and D.S. Gilmour Molecular architecture of the hsp70 promoter after deletion of the TATA box or the upstream regulation region Mol. Cell. Biol. 17 1997 3799 3808
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3799-3808
    • Weber, J.A.1    Taxman, D.J.2    Lu, Q.3    Gilmour, D.S.4
  • 32
    • 0027157980 scopus 로고
    • Rapid changes in Drosophila transcription after an instantaneous heat shock
    • T. O'Brien, and J.T. Lis Rapid changes in Drosophila transcription after an instantaneous heat shock Mol. Cell. Biol. 13 1993 3456 3463
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3456-3463
    • O'Brien, T.1    Lis, J.T.2
  • 33
    • 0027166316 scopus 로고
    • In vivo transcriptional pausing and cap formation on three Drosophila heat shock genes
    • E.B. Rasmussen, and J.T. Lis In vivo transcriptional pausing and cap formation on three Drosophila heat shock genes Proc. Natl. Acad. Sci. USA 90 1993 7923 7927
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7923-7927
    • Rasmussen, E.B.1    Lis, J.T.2


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