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Volumn 17, Issue 10, 1998, Pages 2865-2876

Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin

Author keywords

Chromatin; Heat shock; Histone acetylationl; Nucleosomes; Transcription

Indexed keywords

HEAT SHOCK PROTEIN; HISTONE; HISTONE H1; HISTONE H4; RNA POLYMERASE II;

EID: 0032525139     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.10.2865     Document Type: Article
Times cited : (125)

References (76)
  • 1
    • 0029785841 scopus 로고    scopus 로고
    • Moderate increase in histone acetylation activates the mouse mammary tumor virus promoter and remodels its nucleosome structure
    • Bartsch, J., Truss.M., Bode,J. and Beato.M. (1996) Moderate increase in histone acetylation activates the mouse mammary tumor virus promoter and remodels its nucleosome structure. Proc. Natl Acad. Sci. USA, 93, 10741-10746.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10741-10746
    • Bartsch, J.1
  • 2
    • 0026754072 scopus 로고
    • Cell-free system for assembly of transcriptionally repressed chromatin from Drosophila embryos
    • Becker, P.B. and Wu,C. (1992) Cell-free system for assembly of transcriptionally repressed chromatin from Drosophila embryos. Mot. Cell. Biol., 12, 2241-2249.
    • (1992) Mot. Cell. Biol. , vol.12 , pp. 2241-2249
    • Becker, P.B.1
  • 3
    • 0025735978 scopus 로고
    • Heat shock-regulated transcription m vitro from a chromatin template
    • Becker, P.B., Rabindran.S. and Wu,C. (1991) Heat shock-regulated transcription m vitro from a chromatin template. Proc. Natl Acad. Sci. USA, 88, 4109-4113.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 4109-4113
    • Becker, P.B.1
  • 4
    • 0029085907 scopus 로고
    • Electrostatic mechanism of nucleosome spacing
    • BIank, T.A. and Becker.P.B. (1995) Electrostatic mechanism of nucleosome spacing. J. Mol. Biol, 252, 305-313.
    • (1995) J. Mol. Biol , vol.252 , pp. 305-313
    • Biank, T.A.1
  • 5
    • 0031148774 scopus 로고    scopus 로고
    • Biochemical analysis of chromatin structure and function using Drosophila embryo extracts
    • Blank, T.A., Sandaltzopoulos.R. and Becker.P.B. (1997) Biochemical analysis of chromatin structure and function using Drosophila embryo extracts. Methods, 12, 28-35.
    • (1997) Methods , vol.12 , pp. 28-35
    • Blank, T.A.1
  • 6
    • 0019062866 scopus 로고
    • Modulation of the nucleosome structure by acetylation
    • Bode, J., Henco.K. and Wingender.E. (1980) Modulation of the nucleosome structure by acetylation. Ear. J. Biochem., 110, 143-152.
    • (1980) Ear. J. Biochem. , vol.110 , pp. 143-152
    • Bode, J.1
  • 7
    • 0028009294 scopus 로고
    • Acetylated histone H4 on the male X chromosome is associated with dosage compensation in Drosophita
    • Bone, J.R., Lavender, I., Richman.R., Palmer.MJ., Tumer, B.M. and Kuroda.M.I. (1994) Acetylated histone H4 on the male X chromosome is associated with dosage compensation in Drosophita. Genes Dev., 8, 96-104.
    • (1994) Genes Dev. , vol.8 , pp. 96-104
    • Bone, J.R.1
  • 8
    • 0027192267 scopus 로고
    • Transcriptional silencing in yeast is associated with reduced nucleosome acetylation
    • Braunstein, M., Rose,A.B., Holmes.S.G., AlIis,D.C. and Broach, J.B. (1993) Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev., 7, 592-604.
    • (1993) Genes Dev. , vol.7 , pp. 592-604
  • 9
    • 0030713405 scopus 로고    scopus 로고
    • Disruption of downstream chromatin directed by a transcriptional activator
    • Brown, S.A. and Kingston.R.E. (1997) Disruption of downstream chromatin directed by a transcriptional activator. Genes Dev., 11, 3116-3121.
    • (1997) Genes Dev. , vol.11 , pp. 3116-3121
    • Brown, S.A.1
  • 10
    • 0029759928 scopus 로고    scopus 로고
    • Activator-dependent regulation of transcriptional pausing on nucleosomal templates
    • Brown, S.A., Imbalzano.A.N. and Kingston.R.E. (1996) Activator-dependent regulation of transcriptional pausing on nucleosomal templates. Genes Dev., 10, 1479-1490.
    • (1996) Genes Dev. , vol.10 , pp. 1479-1490
    • Brown, S.A.1
  • 11
    • 0029925512 scopus 로고    scopus 로고
    • Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation
    • Brownell, J.E. and Allis, C.D. (1996) Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation. Curr. Opin. Genet. Dev., 6, 176-184.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 176-184
    • Brownell, J.E.1    Allis, C.D.2
  • 12
    • 0021659613 scopus 로고
    • Psoralen cross-linking of soluble and Hl-depleted soluble rat liver chromatin
    • Conconi, A., Losa.R., KoIler.T. and Sogo.J.M. (1984) Psoralen cross-linking of soluble and Hl-depleted soluble rat liver chromatin. J. Mol. Biol., 178, 920-928.
    • (1984) J. Mol. Biol. , vol.178 , pp. 920-928
    • Conconi, A.1
  • 13
    • 0026599021 scopus 로고
    • Chromatin as an essential part of the transcription mechanism
    • Felsenfeld, G. (1992) Chromatin as an essential part of the transcription mechanism. Nature, 355, 219-224.
    • (1992) Nature , vol.355 , pp. 219-224
    • Felsenfeld, G.1
  • 14
    • 0030581149 scopus 로고    scopus 로고
    • Chromatin unfolds
    • Felsenfeld.G. (1996) Chromatin unfolds. Cell, 86, 13-19.
    • (1996) Cell , vol.86 , pp. 13-19
    • Felsenfeld1
  • 15
    • 0028858566 scopus 로고
    • Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organisation through distinct molecular mechanisms
    • Fletcher, T.M. and HansenJ.C. (1995) Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organisation through distinct molecular mechanisms. J. Biol. Chem., 270, 25359-25362.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25359-25362
    • Fletcher, T.M.1
  • 16
    • 0029815618 scopus 로고    scopus 로고
    • The nucleosomal array: Structure/function relationships
    • Fletcher, T.M. and HansenJ.C. (1996) The nucleosomal array: structure/function relationships. Crit. Rev. Eukaryot. Gene Expr., 6, 149-188.
    • (1996) Crit. Rev. Eukaryot. Gene Expr. , vol.6 , pp. 149-188
    • Fletcher, T.M.1
  • 17
    • 0029046603 scopus 로고
    • Modulation of chromatin folding by histone acetylation
    • Garcia-Ramirez.M., Rocchini.C. and AusioJ. (1995) Modulation of chromatin folding by histone acetylation. J. Biol. Client., 270, 17923-17928.
    • (1995) J. Biol. Client. , vol.270 , pp. 17923-17928
    • Garcia-Ramirez1
  • 18
    • 0023050122 scopus 로고
    • Cohabitation of scaffold binding regions with upstream/enhancer elements of three developmentally regulated genes of D.melanogaster
    • Gasser, S.M. and Laemmli.U.K. (1986) Cohabitation of scaffold binding regions with upstream/enhancer elements of three developmentally regulated genes of D.melanogaster. Cell, 46, 521-530.
    • (1986) Cell , vol.46 , pp. 521-530
    • Gasser, S.M.1
  • 19
    • 0029971350 scopus 로고    scopus 로고
    • The stability of nucleosomes at the replication fork
    • Gasser, R., Koller.T. and Sogo.J.M. (1996) The stability of nucleosomes at the replication fork. J. Mol. Biol, 258, 224-239.
    • (1996) J. Mol. Biol , vol.258 , pp. 224-239
    • Gasser, R.1
  • 20
    • 0027969124 scopus 로고
    • Relationship between core histone acetylation and histone HI gene activity
    • Girardot, V., Rabilloud, T, Yoshida.M., Beppu.T., Lawrence, J. and Khochbin, S. (1994) Relationship between core histone acetylation and histone HI gene activity. Eur. J. Biochem., 224, 885-892.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 885-892
    • Girardot, V.1
  • 21
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. (1997) Histone acetylation in chromatin structure and transcription. Nature, 389, 349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 22
    • 0028799089 scopus 로고
    • The regulation of euchromatin and heterochromatin by histones in yeast
    • Grunstein, M., Hecht, A., Fisher-Adams, G., Wan.J., Mann.R.K., StrahlBolsinger, S., Laroche, T. and Gasser, S. (1995) The regulation of euchromatin and heterochromatin by histones in yeast. J. Cell Sci., 19 Suppl, 29-36.
    • (1995) J. Cell Sci. , vol.19 , pp. 29-36
    • Grunstein, M.1    Hecht, A.2    Fisher-Adams, G.3
  • 23
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W. and Roeder, R.G. (1997) Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell, 90, 595-506.
    • (1997) Cell , vol.90 , pp. 595-1506
    • Gu, W.1    Roeder, R.G.2
  • 24
    • 0030996361 scopus 로고    scopus 로고
    • Synergistic activation of transcription by CBP and p53
    • Gu, W., Shi, X.L. and Roeder, R.G. (1997) Synergistic activation of transcription by CBP and p53. Nature, 387, 819-823.
    • (1997) Nature , vol.387 , pp. 819-823
    • Gu, W.1    Shi, X.L.2    Roeder, R.G.3
  • 25
    • 0027412701 scopus 로고
    • Assembly and structural properties of subsaturated chromatin arrays
    • Hansen, J.C. and Lohr.D. (1993) Assembly and structural properties of subsaturated chromatin arrays. J. Biol. Chem., 268, 5840-5848.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5840-5848
    • Hansen, J.C.1
  • 26
    • 0026644714 scopus 로고
    • Influence of chromatin folding on transcription initiation and elongation by RNA polymerase III
    • Hansen, J.C. and Wolffe, A.P. (1992) Influence of chromatin folding on transcription initiation and elongation by RNA polymerase III. Biochemistry, 31, 7977-7988.
    • (1992) Biochemistry , vol.31 , pp. 7977-7988
    • Hansen, J.C.1    Wolffe, A.P.2
  • 27
    • 0026928709 scopus 로고
    • The interaction of transcription factors with nucleosomal DNA
    • Hayes, J.J. and Wolffe, A.P. (1992) The interaction of transcription factors with nucleosomal DNA. BioEssays, 14, 597-603.
    • (1992) BioEssays , vol.14 , pp. 597-603
    • Hayes, J.J.1    Wolffe, A.P.2
  • 28
    • 0028326787 scopus 로고
    • Core histone acetylation co-maps with generalized DNase I sensitivity in the chicken β-globin chromosomal domain
    • Hebbes, T.R., Clayton, A.L., Thorne, A.W. and Crane-Robinson.C. (1994) Core histone acetylation co-maps with generalized DNase I sensitivity in the chicken β-globin chromosomal domain. EMBO J., 13, 1823-1830.
    • (1994) EMBO J. , vol.13 , pp. 1823-1830
    • Hebbes, T.R.1
  • 29
    • 0031952181 scopus 로고    scopus 로고
    • Nucleosome translational position, not histone deacetylation, determines TFIIIA binding to nucleosomal Xenopus laevis 5S rRNA genes
    • Howe, L. and Ausio, J. (1998) Nucleosome translational position, not histone deacetylation, determines TFIIIA binding to nucleosomal Xenopus laevis 5S rRNA genes. Mol. Cell. Biol., 18, 1156-1162.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1156-1162
    • Howe, L.1    Ausio, J.2
  • 30
    • 0031239891 scopus 로고    scopus 로고
    • Acetylation of general transcription factors by histone acetyl-transferases
    • Imhof, A., Yang, X., Ogryzko, V.V., Nakatani, Y., Wolffe, A.P. and Ge, H. (1997) Acetylation of general transcription factors by histone acetyl-transferases. Curr. Biol., 7, 689-692.
    • (1997) Curr. Biol. , vol.7 , pp. 689-692
    • Imhof, A.1    Yang, X.2    Ogryzko, V.V.3    Nakatani, Y.4    Wolffe, A.P.5    Ge, H.6
  • 31
    • 0025877255 scopus 로고
    • Transcription on nucleosomal templates by RNA polymerase II in vitro: Inhibition of elongation with enhancement of sequence-specific pausing
    • Izban, M.G. and Luse, D.S. (1991) Transcription on nucleosomal templates by RNA polymerase II in vitro: inhibition of elongation with enhancement of sequence-specific pausing. Genes Dev., 5, 683-696.
    • (1991) Genes Dev. , vol.5 , pp. 683-696
    • Izban, M.G.1    Luse, D.S.2
  • 32
    • 0027183088 scopus 로고
    • The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression
    • Jeppesen, P. and Tumer.B.M. (1993) The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression. Cell, 74, 281-289.
    • (1993) Cell , vol.74 , pp. 281-289
    • Jeppesen, P.1
  • 33
    • 0027275194 scopus 로고
    • Potentiation of RNA polymerase II transcription by GaI4-VP16 during but not after DNA replication
    • Kamakaka, R.T, Bulger.M. and KadonagaJ.T. (1993) Potentiation of RNA polymerase II transcription by GaI4-VP16 during but not after DNA replication. Genes Dev., 7, 1779-1795.
    • (1993) Genes Dev. , vol.7 , pp. 1779-1795
    • Kamakaka1
  • 34
    • 0029565873 scopus 로고
    • Equality for X chromosomes
    • Kelley, R.L. and Kuroda.M.I. (1995) Equality for X chromosomes. Science, 270, 1607-1610.
    • (1995) Science , vol.270 , pp. 1607-1610
    • Kelley, R.L.1
  • 35
    • 0032539694 scopus 로고    scopus 로고
    • Reconstitution of hyperacetylated, DNase I sensitive chromatin characterised by high conformational flexibility of nucleosomal DNA
    • Krajewski, W.A. and Becker, P.B. (1998) Reconstitution of hyperacetylated, DNase I sensitive chromatin characterised by high conformational flexibility of nucleosomal DNA. Proc. Nall Acad. Sci. USA, 95, 1540-1545
    • (1998) Proc. Nall Acad. Sci. USA , vol.95 , pp. 1540-1545
    • Krajewski, W.A.1    Becker, P.B.2
  • 36
    • 0032030906 scopus 로고    scopus 로고
    • Histone acetyltransferase activity of GcnSp is required for the activation of target genes m vivo
    • Kuo, M., Zhou, J., Jambeck,P., Churchill, M.E.A. and Allis.C.D. (1998) Histone acetyltransferase activity of GcnSp is required for the activation of target genes m vivo. Genes Dev., 12, 627-639.
    • (1998) Genes Dev. , vol.12 , pp. 627-639
    • Kuo, M.1
  • 37
    • 0027465862 scopus 로고
    • A positive role for histone acetylation in transcription factor access to nucleosomal DNA
    • Lee, D.Y., Hayes, J.J., Pruss.D. and Wolffe, A.P. (1993) A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell, 72, 73-84.
    • (1993) Cell , vol.72 , pp. 73-84
    • Lee, D.Y.1
  • 39
    • 0027335550 scopus 로고
    • n repeats and heat shock elements have distinct roles in chromatin structure and transcriptional activation of the Drosophila hsp26 gene
    • n repeats and heat shock elements have distinct roles in chromatin structure and transcriptional activation of the Drosophila hsp26 gene. Mol. Cell. Biol., 13, 2802-2814.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2802-2814
    • Lu, Q.1
  • 40
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 a resolution
    • Luger, K., Mader, A.W., Richmond, R.K., Sargent, D.F. and Richmond, TJ. (1997) Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature, 389, 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
  • 41
    • 0026705216 scopus 로고
    • Effects of histone acetylation on chromatin topology in vivo
    • Lutter, L.C., Judis,L. and Paretti, R.F. (1992) Effects of histone acetylation on chromatin topology in vivo. Mol. Cell. Biol., 12, 5004-5014.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5004-5014
    • Lutter, L.C.1    Paretti, R.F.2
  • 42
    • 15644384251 scopus 로고    scopus 로고
    • Cooperative and competitive protein interactions at the Itsp70 promoter
    • Mason, P.B. and Lis, J.T. (1997) Cooperative and competitive protein interactions at the Itsp70 promoter. J. Biol. Chem., 272, 33227-33233.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33227-33233
    • Mason, P.B.1    Lis, J.T.2
  • 43
    • 0031306557 scopus 로고    scopus 로고
    • A role of nucleosome remodelling factor NURF in transcriptional activation of chromatin
    • Mizuguchi, G., Tsukiyama, T., Wisniewski, J. and Wu, C. (1998) A role of nucleosome remodelling factor NURF in transcriptional activation of chromatin. Mol. Cell, 1, 141-150.
    • (1998) Mol. Cell , vol.1 , pp. 141-150
    • Mizuguchi, G.1    Tsukiyama, T.2    Wisniewski, J.3    Wu, C.4
  • 44
    • 0030447943 scopus 로고    scopus 로고
    • The TAF(II)250 subunit of TFIID has histone acetyltransferase activity
    • Mizzen, C.A. et al. (1996) The TAF(II)250 subunit of TFIID has histone acetyltransferase activity. Cell, 87, 1261-1270.
    • (1996) Cell , vol.87 , pp. 1261-1270
    • Mizzen, C.A.1
  • 45
    • 0030967242 scopus 로고    scopus 로고
    • The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
    • Ng, K.W., Ridgway.R, Cohen.D.R. and Tremethick.DJ. (1997) The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome. EMBO J., 16, 2072-2085.
    • (1997) EMBO J. , vol.16 , pp. 2072-2085
    • Ng, K.W.1
  • 46
    • 0024503977 scopus 로고
    • Histone acetylation reduces nucleosome core panicle linking number change
    • Norton, V.G., Imai, B.S., Yau, P. and Bradbury, E.M. (1989) Histone acetylation reduces nucleosome core panicle linking number change. Cell, 57, 449-457.
    • (1989) Cell , vol.57 , pp. 449-457
    • Norton, V.G.1    Imai, B.S.2    Yau, P.3    Bradbury, E.M.4
  • 47
    • 0025244999 scopus 로고
    • Nucleosome linking number change controlled by acetylation of histones H3 and H4
    • Norton, V.G., Marvin, K.W., Yau, P. and Bradbury.E.M. (1990) Nucleosome linking number change controlled by acetylation of histones H3 and H4. J. Biol. Chem., 265, 19848-19852.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19848-19852
    • Norton, V.G.1    Marvin, K.W.2    Yau, P.3
  • 48
    • 0029119093 scopus 로고
    • Histone H4 acetylation distinguishes coding regions of the genome from heterochromatin in a differentiation-dependent but transcription-independent manner
    • O'Neill, L.P. and Tumer, B.M. (1995) Histone H4 acetylation distinguishes coding regions of the genome from heterochromatin in a differentiation-dependent but transcription-independent manner. EMBO J., 14, 3946-3957.
    • (1995) EMBO J. , vol.14 , pp. 3946-3957
    • O'Neill, L.P.1    Tumer, B.M.2
  • 49
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coaclivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V.V., Schiltz, R.L., Russanova, V., Howard, B.H. and Nakatani, Y. (1996) The transcriptional coaclivators p300 and CBP are histone acetyltransferases. Cell, 87, 953-959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 51
    • 0025946135 scopus 로고
    • Histone acetylation reduces Himediated nucleosome interactions during chromatin assembly
    • Perry, C.A. and Annunziato, A.T. (1991) Histone acetylation reduces Himediated nucleosome interactions during chromatin assembly. Exp. Cell Res., 196, 337-345.
    • (1991) Exp. Cell Res. , vol.196 , pp. 337-345
    • Perry, C.A.1    Annunziato, A.T.2
  • 52
    • 0028201744 scopus 로고
    • TFIID sequence recognition of the initiator and sequences farther downstream in Drosophila class II genes
    • Pumell, B.A., Emanuel, P.A. and Gilmour, D.S. (1994) TFIID sequence recognition of the initiator and sequences farther downstream in Drosophila class II genes. Genes Dev., 8, 830-842.
    • (1994) Genes Dev. , vol.8 , pp. 830-842
    • Pumell, B.A.1    Emanuel, P.A.2    Gilmour, D.S.3
  • 53
    • 0029075820 scopus 로고
    • Analysis of protein-DNA interaction by solid-phase footprinting
    • Sandaltzopoulos.R. and Becker.P.B. (1995) Analysis of protein-DNA interaction by solid-phase footprinting. Methods Mol. Cell Biol., 5, 176-181.
    • (1995) Methods Mol. Cell Biol. , vol.5 , pp. 176-181
    • Sandaltzopoulos1
  • 54
    • 0031972647 scopus 로고    scopus 로고
    • Heat shock factor increases the reinitiation rate from potentiated chromatin templates
    • Sandaltzopoulos.R. and Becker.P.B. (1998) Heat shock factor increases the reinitiation rate from potentiated chromatin templates. Mol. Cell. Biol., 18, 361-367.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 361-367
    • Sandaltzopoulos1
  • 56
    • 0028157349 scopus 로고
    • Transcriptional repression by nucleosomes but not HI in reconstituted preblastoderm Drosophila chromatin
    • Sandaltzopoulos, R., Blank, T. and Becker, P.B. (1994) Transcriptional repression by nucleosomes but not HI in reconstituted preblastoderm Drosophila chromatin. EMBO J., 13, 373-379.
    • (1994) EMBO J. , vol.13 , pp. 373-379
    • Sandaltzopoulos, R.1    Blank, T.2    Becker, P.B.3
  • 57
    • 0028201770 scopus 로고
    • Gene expression within a chromatin domain: The role of core histone hyperacetylation
    • Schlake, T., Klehr-Wirth, D., Yoshida, M., Beppu, T. and Bode, J. (1994) Gene expression within a chromatin domain: The role of core histone hyperacetylation. Biochemistry, 33, 4197-4206.
    • (1994) Biochemistry , vol.33 , pp. 4197-4206
    • Schlake, T.1    Klehr-Wirth, D.2    Yoshida, M.3    Beppu, T.4    Bode, J.5
  • 58
    • 0031455415 scopus 로고    scopus 로고
    • Histone acetyltransferases regulate HIV-1 enhancer activity in vitro
    • Sheridan, P.L., Mayall, T.P., Verdin.E. and Jones, K.A. (1998) Histone acetyltransferases regulate HIV-1 enhancer activity in vitro. Genes Dev., 11, 3327-3340.
    • (1998) Genes Dev. , vol.11 , pp. 3327-3340
    • Sheridan, P.L.1    Mayall, T.P.2    VerdinE3    Jones, K.A.4
  • 59
    • 0018086146 scopus 로고
    • Structure of chromatin containing extensively acetylated H3 and H4
    • Simpson, R.T. (1978) Structure of chromatin containing extensively acetylated H3 and H4. Cell, 13, 691-699.
    • (1978) Cell , vol.13 , pp. 691-699
    • Simpson, R.T.1
  • 60
    • 0021724904 scopus 로고
    • Psoralen cross-linking of DNA as a probe for the structure of active nucleolar chromatin
    • Sogo, J.M., Ness, PJ., Widmer, R.M., Parish, R.W. and Koller, T. (1984) Psoralen cross-linking of DNA as a probe for the structure of active nucleolar chromatin. J. Mol. Biol., 178, 897-919.
    • (1984) J. Mol. Biol. , vol.178 , pp. 897-919
    • Sogo, J.M.1    Ness, P.J.2    Widmer, R.M.3    Parish, R.W.4    Koller, T.5
  • 62
    • 0025780941 scopus 로고
    • Facilitated binding of Gal4 and heat shock factor to nucleosomal templates: Differential function of DNA binding domains
    • Taylor, I.C.A., WorkmanJ.L., Schuetz, T.J. and Kingston, R.E. (1991) Facilitated binding of Gal4 and heat shock factor to nucleosomal templates: differential function of DNA binding domains. Genes Dev., 5, 1285-1298.
    • (1991) Genes Dev. , vol.5 , pp. 1285-1298
    • Taylor, I.C.A.1    Workman2
  • 63
    • 0029562736 scopus 로고
    • Purification and properties of an ATP-dependent nucleosome remodelling factor
    • Tsukiyama,T. and Wu, C. (1995) Purification and properties of an ATP-dependent nucleosome remodelling factor. Cell, 83, 1011-1020.
    • (1995) Cell , vol.83 , pp. 1011-1020
    • Wu, C.1
  • 64
    • 0029349023 scopus 로고
    • Histone acetylation in chromatin and chromosomes
    • Tumer.B.M. and O'Neill.L.P. (1995) Histone acetylation in chromatin and chromosomes. Sem. Cell Biol., 6, 229-236.
    • (1995) Sem. Cell Biol. , vol.6 , pp. 229-236
    • Tumer1
  • 65
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turaer, B.M., Birley, A.J. and Lavender, J. (1992) Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell, 69, 375-384.
    • (1992) Cell , vol.69 , pp. 375-384
    • Turaer, B.M.1    Birley, A.J.2    Lavender, J.3
  • 66
    • 0027525056 scopus 로고
    • Decoding the nucleosome
    • Turner, B.M. (1993) Decoding the nucleosome. Cell, 75, 5-8.
    • (1993) Cell , vol.75 , pp. 5-8
    • Turner, B.M.1
  • 67
    • 0030998534 scopus 로고    scopus 로고
    • Histone acetylation: Influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression
    • Ura, K., Kurumizaka, H., Dimitrov, S., Almouzni, G. and Wolffe, A.P. (1997) Histone acetylation: influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression. EMBO J., 16, 2096-2107.
    • (1997) EMBO J. , vol.16 , pp. 2096-2107
    • Ura, K.1    Kurumizaka, H.2    Dimitrov, S.3    Almouzni, G.4    Wolffe, A.P.5
  • 69
    • 0029919356 scopus 로고    scopus 로고
    • Transcriptional activation and chromatin remodelling of the HIV-1 promoter in response to histone acetylation
    • Van Lint,C., Emiliani, S., Ott,M. and Verdin.E. (1996a) Transcriptional activation and chromatin remodelling of the HIV-1 promoter in response to histone acetylation. EMBO J., 15, 1112-1120.
    • (1996) EMBO J. , vol.15 , pp. 1112-1120
    • Emiliani, S.1
  • 70
    • 0029693220 scopus 로고    scopus 로고
    • The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation
    • Van Lint, C., Emiliani, S. and Verdin, E. (1996b) The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr., 5, 245-253.
    • (1996) Gene Expr. , vol.5 , pp. 245-253
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 71
    • 0028127762 scopus 로고
    • Role of the histone amino termini in facilitated binding of a transcription factor, GAL4-AH, to nucleosome cores
    • Vettese-Dadey, M., Walter, P., Chen, H., Juan, L.-J. and Workman, J.L. (1994) Role of the histone amino termini in facilitated binding of a transcription factor, GAL4-AH, to nucleosome cores. Mol. Cell. Biol., 14, 970-981.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 970-981
    • Vettese-Dadey, M.1    Walter, P.2    Chen, H.3    Juan, L.-J.4    Workman, J.L.5
  • 72
    • 0029985730 scopus 로고    scopus 로고
    • Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro
    • Vettese-Dadey, M., Grant, P.A., Hebbes, T.R., Crane-Robinson, C., Allis, C.D. and WorkmanJ.L. (1996) Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro. EMBO J., 15, 2508-2518.
    • (1996) EMBO J. , vol.15 , pp. 2508-2518
    • Vettese-Dadey, M.1
  • 73
    • 0021750061 scopus 로고
    • Differential dissociation of histone tails from core chromatin
    • Walker, I.O. (1984) Differential dissociation of histone tails from core chromatin. Biochemistry, 23, 5622-5628.
    • (1984) Biochemistry , vol.23 , pp. 5622-5628
    • Walker, I.O.1
  • 74
    • 0023782238 scopus 로고
    • Analysis of psoralencross-linking pattern in chromatin DNA by exonuclease digestion
    • Widmer, R.M., Koller, T. and Sogo, J.M. (1988) Analysis of psoralencross-linking pattern in chromatin DNA by exonuclease digestion. Nucleic Acids Res., 16, 7013-7024.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7013-7024
    • Widmer, R.M.1    Koller, T.2    Sogo, J.M.3
  • 75
    • 0031132205 scopus 로고    scopus 로고
    • Activators and repressers: Making use of chromatin to regulate transcription
    • Wolffe, A.P., Wong, J. and Pruss.D. (1997) Activators and repressers: Making use of chromatin to regulate transcription. Genes to Cells, 2, 291-302.
    • (1997) Genes to Cells , vol.2 , pp. 291-302
    • Wolffe, A.P.1    Wong, J.2
  • 76
    • 0029294663 scopus 로고
    • Trichostatin a and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function
    • Yoshida, M., Horinouchi, S. and Beppu, T. (1995) Trichostatin A and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structure and function. BioEssays, 17, 423-430.
    • (1995) BioEssays , vol.17 , pp. 423-430
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3


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