메뉴 건너뛰기




Volumn 15, Issue 10, 1996, Pages 2508-2518

Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro

Author keywords

Chromatin; Histone acetylation; Nucleosomes; Transcription factors

Indexed keywords

ANTIBODY; DNA; DNA BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; HISTONE H3; HISTONE H4; TRANSCRIPTION FACTOR;

EID: 0029985730     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00608.x     Document Type: Article
Times cited : (394)

References (80)
  • 1
    • 0028872728 scopus 로고
    • The binding of disparate transcription factors to nucleosomal DNA is inherently cooperative
    • Adams,C.C. and Workman,J.L. (1995) The binding of disparate transcription factors to nucleosomal DNA is inherently cooperative. Mol. Cell. Biol., 15, 1405-1421.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1405-1421
    • Adams, C.C.1    Workman, J.L.2
  • 2
    • 0020131558 scopus 로고
    • Participation of the core histone 'tails' in the stabilization of the chromatin solenoid
    • Allan,J., Harborne,N., Rau,D.C. and Gould,H. (1982) Participation of the core histone 'tails' in the stabilization of the chromatin solenoid. J. Cell Biol., 93, 285-297.
    • (1982) J. Cell Biol. , vol.93 , pp. 285-297
    • Allan, J.1    Harborne, N.2    Rau, D.C.3    Gould, H.4
  • 3
    • 0023660740 scopus 로고
    • Affinity Chromatographic purification of nucleosomes containing transcriptionally active DNA sequences
    • Allegra,P., Sterner,R., Clayton,D.F. and Allfrey,V.G. (1987) Affinity Chromatographic purification of nucleosomes containing transcriptionally active DNA sequences. J. Mol. Biol., 196, 379-388.
    • (1987) J. Mol. Biol. , vol.196 , pp. 379-388
    • Allegra, P.1    Sterner, R.2    Clayton, D.F.3    Allfrey, V.G.4
  • 4
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey,V.G., Faulkner,R. and Mirsky,A.E. (1964) Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl Acad. Sci. USA, 51, 786-794.
    • (1964) Proc. Natl Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 5
    • 0021112684 scopus 로고
    • Histone deacetylation is required for the maturation of newly replicated chromatin
    • Annunziato,A.T. and Seale,R.L. (1983) Histone deacetylation is required for the maturation of newly replicated chromatin. J. Biol. Chem., 258, 12675-12684.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12675-12684
    • Annunziato, A.T.1    Seale, R.L.2
  • 7
    • 0028484563 scopus 로고
    • The establishment of active promoters in chromatin
    • Becker,P.B. (1994) The establishment of active promoters in chromatin. BioEssays, 16, 541-547.
    • (1994) BioEssays , vol.16 , pp. 541-547
    • Becker, P.B.1
  • 8
    • 0025606725 scopus 로고
    • Factors affecting nucleosome structure in transcriptionally active chromatin: Histone acetylation, nascent RNA and inhibitors of RNA synthesis
    • Boffa,L.C., Walker,J., Chen,T.A., Sterner,R., Mariani,M.R. and Allfrey,V.G. (1990) Factors affecting nucleosome structure in transcriptionally active chromatin: histone acetylation, nascent RNA and inhibitors of RNA synthesis. Eur. J. Biochem., 194, 811-823.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 811-823
    • Boffa, L.C.1    Walker, J.2    Chen, T.A.3    Sterner, R.4    Mariani, M.R.5    Allfrey, V.G.6
  • 9
    • 0028009294 scopus 로고
    • Acetylated histone H4 on the male X chromosome is associated with dosage compensation in Drosophila
    • Bone,J.R., Lavender,J., Richman,R., Palmer,M.J., Turner,B.M. and Kuroda,M.I. (1994) Acetylated histone H4 on the male X chromosome is associated with dosage compensation in Drosophila. Genes Dev., 8, 96-104.
    • (1994) Genes Dev. , vol.8 , pp. 96-104
    • Bone, J.R.1    Lavender, J.2    Richman, R.3    Palmer, M.J.4    Turner, B.M.5    Kuroda, M.I.6
  • 10
    • 0027192267 scopus 로고
    • Transcriplional silencing in yeast is associated with reduced nucleosome acetylation
    • Braunstein,M., Rose,A.B., Holmes,S.G., Allis,C.D. and Broach,J.R. (1993) Transcriplional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev., 7, 592-604.
    • (1993) Genes Dev. , vol.7 , pp. 592-604
    • Braunstein, M.1    Rose, A.B.2    Holmes, S.G.3    Allis, C.D.4    Broach, J.R.5
  • 11
    • 0029925512 scopus 로고    scopus 로고
    • Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation
    • in press
    • 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., in press.
    • (1996) Curr. Opin. Genet. Dev.
    • Brownell, J.E.1    Allis, C.D.2
  • 12
    • 0343427290 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A transcriptional co-activator linking gene expression to histone acetylation
    • in press
    • Brownell,J.E., Zhou,J., Ranalli,T., Kobayashi,R., Edmonson,D.G., Rothe,S.Y. and Allis,C.D. (1996) Tetrahymena histone acetyltransferase A: a transcriptional co-activator linking gene expression to histone acetylation. Cell, in press.
    • (1996) Cell
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmonson, D.G.5    Rothe, S.Y.6    Allis, C.D.7
  • 13
    • 0023448190 scopus 로고
    • The major late transcription factor binds to and activates the mouse metallothionein I promoter
    • Carthew,R.W., Chodosh,L.A. and Sharp,P.A. (1987) The major late transcription factor binds to and activates the mouse metallothionein I promoter. Genes Dev., 1, 973-980.
    • (1987) Genes Dev. , vol.1 , pp. 973-980
    • Carthew, R.W.1    Chodosh, L.A.2    Sharp, P.A.3
  • 14
    • 0025239866 scopus 로고
    • A yeast protein that influences chromatin structure of UASG and functions as a powerful auxiliary activator
    • Chasman,D.I., Lue,N.F., Buchman,A.R., LaPointe,J.W., Lorch,Y. and Kornberg,R.D. (1990) A yeast protein that influences chromatin structure of UASG and functions as a powerful auxiliary activator. Genes Dev., 4, 503-514.
    • (1990) Genes Dev. , vol.4 , pp. 503-514
    • Chasman, D.I.1    Lue, N.F.2    Buchman, A.R.3    LaPointe, J.W.4    Lorch, Y.5    Kornberg, R.D.6
  • 15
    • 0023619655 scopus 로고
    • The major late transcription factor activates the rat gamma-fibrinogen promoter
    • Cnodosh,L.A., Carthew,R.W., Morgan,J.G., Crabtree,G.R. and Sharp,P.A. (1987) The major late transcription factor activates the rat gamma-fibrinogen promoter. Science, 238, 684-688.
    • (1987) Science , vol.238 , pp. 684-688
    • Cnodosh, L.A.1    Carthew, R.W.2    Morgan, J.G.3    Crabtree, G.R.4    Sharp, P.A.5
  • 16
    • 0025108413 scopus 로고
    • Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus
    • Churehill,M.E., Tullius,T.D. and Klug,A. (1990) Mode of interaction of the zinc finger protein TFIIIA with a 5S RNA gene of Xenopus. Proc. Natl Acad. Sci. USA, 87m, 5528-5532.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 M , pp. 5528-5532
    • Churehill, M.E.1    Tullius, T.D.2    Klug, A.3
  • 18
    • 77957027468 scopus 로고
    • Basic analysis of transcription factor binding to nucleosomes
    • Côté,J., Utley,R.T. and Workman,J.L. (1995) Basic analysis of transcription factor binding to nucleosomes. Methods Mol. Genet., 6, 108-129.
    • (1995) Methods Mol. Genet. , vol.6 , pp. 108-129
    • Côté, J.1    Utley, R.T.2    Workman, J.L.3
  • 19
    • 0025122175 scopus 로고
    • On the biological role of histone acetylation
    • Csordas,A. (1990) On the biological role of histone acetylation. Biochem. J., 265, 23-38.
    • (1990) Biochem. J. , vol.265 , pp. 23-38
    • Csordas, A.1
  • 20
    • 0027476430 scopus 로고
    • Identification and analysis of all components of a gel retardation assay by combination with immunoblotting
    • Demczuk,S., Harbers,M. and Vennström,B. (1993) Identification and analysis of all components of a gel retardation assay by combination with immunoblotting. Proc. Natl. Acad. Sci. USA, 90, 2574-2578.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2574-2578
    • Demczuk, S.1    Harbers, M.2    Vennström, B.3
  • 21
    • 0025736044 scopus 로고
    • Yeast histone H4 N-terminal sequence is required for promoter activation in vivo
    • Durrin,L.K., Mann,R.K., Kayne,P.S. and Grunstein,M. (1991) Yeast histone H4 N-terminal sequence is required for promoter activation in vivo. Cell. 65, 1023-1031.
    • (1991) Cell. , vol.65 , pp. 1023-1031
    • Durrin, L.K.1    Mann, R.K.2    Kayne, P.S.3    Grunstein, M.4
  • 22
    • 0024261880 scopus 로고
    • Statistical positioning of nucleosomes by specific protein binding to upstream activating sequence in yeast
    • Fedor,M.J., Lue,N.F. and Kornberg,R.D. (1988) Statistical positioning of nucleosomes by specific protein binding to upstream activating sequence in yeast. J. Mol. Biol., 204, 109-127.
    • (1988) J. Mol. Biol. , vol.204 , pp. 109-127
    • Fedor, M.J.1    Lue, N.F.2    Kornberg, R.D.3
  • 24
    • 0028933783 scopus 로고
    • Yeast histone H4 and H3 N-termini have different effects on the chromatin structure of the GAL1 promoter
    • Fisher-Adams,G. and Grunstein,M. (1995) Yeast histone H4 and H3 N-termini have different effects on the chromatin structure of the GAL1 promoter. EMBO J., 14, 1468-1477.
    • (1995) EMBO J. , vol.14 , pp. 1468-1477
    • Fisher-Adams, G.1    Grunstein, M.2
  • 25
    • 0015785691 scopus 로고
    • Studies of histone fraction F2A1 in macro- and micronuclei of Tetrahymena pyriformis
    • Gorovsky,M.A., Pleger,G.L., Keevert,J.B. and Johmann,C.A. (1973) Studies of histone fraction F2A1 in macro- and micronuclei of Tetrahymena pyriformis. J. Cell Biol. 57, 773-781.
    • (1973) J. Cell Biol. , vol.57 , pp. 773-781
    • Gorovsky, M.A.1    Pleger, G.L.2    Keevert, J.B.3    Johmann, C.A.4
  • 26
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow,E. and Lane,D. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 27
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes,T.R., Thorne,A.W. and Crane-Robinson,C. (1988) A direct link between core histone acetylation and transcriptionally active chromatin EMBO J., 7, 1395-1402.
    • (1988) EMBO J. , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 28
    • 0024417448 scopus 로고
    • A 'minimal epitope' anti-protein antibody that recognizes a single modified amino acid
    • Hebbes,T.R., Turner,C.H., Thorne,A.W. and Crane-Robinson,C. (1989) A 'minimal epitope' anti-protein antibody that recognizes a single modified amino acid. Mol. Immunol., 6, 865-873.
    • (1989) Mol. Immunol. , vol.6 , pp. 865-873
    • Hebbes, T.R.1    Turner, C.H.2    Thorne, A.W.3    Crane-Robinson, C.4
  • 29
    • 0028326787 scopus 로고
    • Core histone hyperacetylation 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 hyperacetylation 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    Clayton, A.L.2    Thorne, A.W.3    Crane-Robinson, C.4
  • 30
    • 0028919756 scopus 로고
    • Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
    • Hecht,A., Laroche,T., Strahl-Bolsinger,S., Gasser,S.M. and Grunstein,M. (1995) Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeast. Cell, 80, 583-592.
    • (1995) Cell , vol.80 , pp. 583-592
    • Hecht, A.1    Laroche, T.2    Strahl-Bolsinger, S.3    Gasser, S.M.4    Grunstein, M.5
  • 31
    • 0027525970 scopus 로고
    • Studies of the DNA binding properties of the histone H4 amino terminus
    • Hong,L., Schroth,G.P., Matthews,H.R., Yau,P. and Bradbury,E.M. (1993) Studies of the DNA binding properties of the histone H4 amino terminus. J. Biol. Chem., 268, 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
  • 32
    • 0023785164 scopus 로고
    • The separation of transcriptionally engaged genes
    • Ip,Y.T., Jackson,V., Meier,J. and Chalkley,R. (1988) The separation of transcriptionally engaged genes. J. Biol. Chem., 263, 14044-14052.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14044-14052
    • Ip, Y.T.1    Jackson, V.2    Meier, J.3    Chalkley, R.4
  • 33
    • 0027183088 scopus 로고
    • The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenic marker for gene expression
    • Jeppesen,P. and Turner,B.M. (1993) The inactive X chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenic marker for gene expression. Cell, 74, 281-289.
    • (1993) Cell , vol.74 , pp. 281-289
    • Jeppesen, P.1    Turner, B.M.2
  • 34
    • 0025002966 scopus 로고
    • Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae
    • Johnson,L.M., Kayne,P.S., Kahn,E.S. and Grunstein,M. (1990) Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA, 87, 6286-6290.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 6286-6290
    • Johnson, L.M.1    Kayne, P.S.2    Kahn, E.S.3    Grunstein, M.4
  • 35
    • 0028559510 scopus 로고
    • Differential repression of transcription factor binding by histone HI is regulated by the core histone amino termini
    • Juan,L.-J., Utley,R.T., Adams,C.C., Vettese-Dadey,M. and Workman,J.L. (1994) Differential repression of transcription factor binding by histone HI is regulated by the core histone amino termini. EMBO J., 13, 6031-6040.
    • (1994) EMBO J. , vol.13 , pp. 6031-6040
    • Juan, L.-J.1    Utley, R.T.2    Adams, C.C.3    Vettese-Dadey, M.4    Workman, J.L.5
  • 36
    • 0024280881 scopus 로고
    • Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast
    • Kayne,P.S., Kim,U.-J., Han,M., Mullen,J.R., Yoshizaki,F. and Grunstein,M. (1988) Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast. Cell, 55, 27-39.
    • (1988) Cell , vol.55 , pp. 27-39
    • Kayne, P.S.1    Kim, U.-J.2    Han, M.3    Mullen, J.R.4    Yoshizaki, F.5    Grunstein, M.6
  • 37
    • 0028885077 scopus 로고
    • Identification of a gene encoding a yeast histone H4 acetyltransferase
    • Kleff,S., Andrulis,E.D., Anderson,C.W. and Sternglanz,R. (1995) Identification of a gene encoding a yeast histone H4 acetyltransferase. J. Biol. Chem., 270, 24674-24677.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24674-24677
    • Kleff, S.1    Andrulis, E.D.2    Anderson, C.W.3    Sternglanz, R.4
  • 38
    • 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    Hayes, J.J.2    Pruss, D.3    Wolffe, A.P.4
  • 39
    • 0024544492 scopus 로고
    • Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena
    • Lin,R., Leone,J.W., Cook,R.G. and Allis,C.D. (1989) Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena. J. Cell Biol., 108, 1577-1588.
    • (1989) J. Cell Biol. , vol.108 , pp. 1577-1588
    • Lin, R.1    Leone, J.W.2    Cook, R.G.3    Allis, C.D.4
  • 40
    • 0023742799 scopus 로고
    • How different eukaryotic transcriptional activators can cooperate promiscuously
    • Lin,Y.-S., Carey,M., Ptashne,M. and Green,M.R. (1988) How different eukaryotic transcriptional activators can cooperate promiscuously. Cell, 54, 659-664.
    • (1988) Cell , vol.54 , pp. 659-664
    • Lin, Y.-S.1    Carey, M.2    Ptashne, M.3    Green, M.R.4
  • 41
    • 0028608018 scopus 로고
    • Histone acetylation: Facts and questions
    • Loidl,P. (1994) Histone acetylation: facts and questions. Chromosoma, 103, 441-449.
    • (1994) Chromosoma , vol.103 , pp. 441-449
    • Loidl, P.1
  • 42
    • 0026697659 scopus 로고
    • Histone H3 N-terminal mutations allow hyperactivation of the yeast GAL1 gene in vivo
    • Mann,R.K. and Grunstein,M. (1992) Histone H3 N-terminal mutations allow hyperactivation of the yeast GAL1 gene in vivo. EMBO J., 11, 3297-3306.
    • (1992) EMBO J. , vol.11 , pp. 3297-3306
    • Mann, R.K.1    Grunstein, M.2
  • 43
    • 0026547747 scopus 로고
    • DNA recognition by GAL4: Structure of a protein-DNA complex
    • Marmorstein,R., Carey,M., Ptashne,M. and Harrison,S.C. (1992) DNA recognition by GAL4: structure of a protein-DNA complex. Nature, 356, 408-414.
    • (1992) Nature , vol.356 , pp. 408-414
    • Marmorstein, R.1    Carey, M.2    Ptashne, M.3    Harrison, S.C.4
  • 45
    • 0021112111 scopus 로고
    • Histone hyperacetylation has little effect on the higher order folding of chromatin
    • McGee,J.D., Nickol,J.M., Felsenfeld,G. and Rau,D.C. (1983) Histone hyperacetylation has little effect on the higher order folding of chromatin. Nucleic Acids Res., 11, 4065-4075.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 4065-4075
    • McGee, J.D.1    Nickol, J.M.2    Felsenfeld, G.3    Rau, D.C.4
  • 46
    • 0040215628 scopus 로고
    • Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes
    • Miller,J., McLachlan,A.D. and Klug,A. (1985) Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J., 4, 1609-1614.
    • (1985) EMBO J. , vol.4 , pp. 1609-1614
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 47
    • 0027742525 scopus 로고
    • Nucleosome disruption by transcription factor binding in yeast
    • Morse,R.H. (1993) Nucleosome disruption by transcription factor binding in yeast. Science, 262, 1563-1566.
    • (1993) Science , vol.262 , pp. 1563-1566
    • Morse, R.H.1
  • 48
    • 0023986832 scopus 로고
    • Constitutive and metal-inducible protein:DNA interactions at the mouse metallothionein I promoter examined by in vivo and in vitro footprinting
    • Mueller,P.R., Salser,S.J. and Wold,B. (1988) Constitutive and metal-inducible protein:DNA interactions at the mouse metallothionein I promoter examined by in vivo and in vitro footprinting. Genes Dev., 2, 412-427.
    • (1988) Genes Dev. , vol.2 , pp. 412-427
    • Mueller, P.R.1    Salser, S.J.2    Wold, B.3
  • 49
    • 0028152490 scopus 로고
    • The basic helix-loop-helix protein upstream stimulating factor regulates cardiac ventricular myosin light-chain 2 gene via independent cis regulatory elements
    • Navankasattusas,S., Sawadogo,M., van Bilsen,M., Dang,C.V. and Chien,K. (1994) The basic helix-loop-helix protein upstream stimulating factor regulates cardiac ventricular myosin light-chain 2 gene via independent cis regulatory elements. Mol. Cell. Biol., 14, 7331-7339.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7331-7339
    • Navankasattusas, S.1    Sawadogo, M.2    Van Bilsen, M.3    Dang, C.V.4    Chien, K.5
  • 50
    • 0024503977 scopus 로고
    • Histone acetylation reduces nucleosome core particle linking number change
    • Norton,V.G., Imai,B.S., Yau,P. and Bradbury,E.M. (1989) Histone acetylation reduces nucleosome core particle 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
  • 51
    • 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    Bradbury, E.M.4
  • 52
    • 0029119093 scopus 로고
    • Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner
    • O'Neill,L.P. and Turner,B.M. (1995) Histone H4 acetylation distinguishes coding regions of the human 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    Turner, B.M.2
  • 53
  • 54
    • 0025110835 scopus 로고
    • Point mutations in the yeast histone H4 gene prevent silencing of the silent mating type locus HML
    • Park,E.-C. and Szostak,J.W. (1990) Point mutations in the yeast histone H4 gene prevent silencing of the silent mating type locus HML. Mol. Cell. Biol., 10, 4932-4934.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4932-4934
    • Park, E.-C.1    Szostak, J.W.2
  • 55
    • 0024323875 scopus 로고
    • Influence of histone acetylation on the solubility, HI content and DNase I sensitivity of newly assembled chromatin
    • Perry,C.A. and Annunziato,A.T. (1989) Influence of histone acetylation on the solubility, HI content and DNase I sensitivity of newly assembled chromatin. Nucleic Acids Res., 17, 4275-4291.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4275-4291
    • Perry, C.A.1    Annunziato, A.T.2
  • 56
    • 0025946135 scopus 로고
    • Histone acetylation reduces H1-mediated nucleosome interactions during chromatin assembly
    • Perry,C.A. and Annunziato,A.T. (1991) Histone acetylation reduces H1-mediated 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
  • 57
    • 0027743318 scopus 로고
    • Analysis of nucleosome assembly and histone exchange using antibodies specific for acetylated H4
    • Perry,C.A., Dadd,C.A., Allis,C.D. and Annunziato,A.T. (1993) Analysis of nucleosome assembly and histone exchange using antibodies specific for acetylated H4. Biochemistry, 32, 13605-13614.
    • (1993) Biochemistry , vol.32 , pp. 13605-13614
    • Perry, C.A.1    Dadd, C.A.2    Allis, C.D.3    Annunziato, A.T.4
  • 58
    • 0026057808 scopus 로고
    • Histone acetylation: Recent approaches to a basic mechanism of genome organization
    • Pfeffer,U. and Vidali,G. (1991) Histone acetylation: recent approaches to a basic mechanism of genome organization. Int. J. Biochem., 23, 277-285.
    • (1991) Int. J. Biochem. , vol.23 , pp. 277-285
    • Pfeffer, U.1    Vidali, G.2
  • 59
    • 0025989240 scopus 로고
    • Recombinant 43-kDa USF binds to DNA and activates transcription in a manner indistinguishable from that of natural 43/44-kDa USF
    • Pognonec,P. and Roeder,R.G. (1991) Recombinant 43-kDa USF binds to DNA and activates transcription in a manner indistinguishable from that of natural 43/44-kDa USF. Mol. Cell. Biol., 11, 5125-5136.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5125-5136
    • Pognonec, P.1    Roeder, R.G.2
  • 60
    • 0026410043 scopus 로고
    • A quick procedure for purification of functional recombinant proteins overexpressed in E.coli
    • Pognonec,P., Kato,H., Sumimoto,H., Kretzschmar,M. and Roeder,R.G. (1991) A quick procedure for purification of functional recombinant proteins overexpressed in E.coli. Nucleic Acids Res., 19, 6650.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6650
    • Pognonec, P.1    Kato, H.2    Sumimoto, H.3    Kretzschmar, M.4    Roeder, R.G.5
  • 61
    • 0023123748 scopus 로고
    • Chicken erythrocyte polynucleosomes which are soluble at physiological ionic strength and contain linker histones are highly enriched in beta-globin gene sequences
    • Ridsdale,J.A. and Davie,J.R. (1987) Chicken erythrocyte polynucleosomes which are soluble at physiological ionic strength and contain linker histones are highly enriched in beta-globin gene sequences. Nucleic Acids Res., 15, 1081-1096.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 1081-1096
    • Ridsdale, J.A.1    Davie, J.R.2
  • 62
    • 0025217826 scopus 로고
    • Histone acetylation alters the capacity of the HI histones to condense transcriptionally active/competent chromatin
    • Ridsdale,J.A., Henzdel,M.J., Decluve,G.P. and Davie,J.R. (1990) Histone acetylation alters the capacity of the HI histones to condense transcriptionally active/competent chromatin. J. Biol. Chem., 265, 5150-5156.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5150-5156
    • Ridsdale, J.A.1    Henzdel, M.J.2    Decluve, G.P.3    Davie, J.R.4
  • 63
    • 0026552385 scopus 로고
    • Stable nucleosome positioning and complete repression by the yeast α2 represser are disrupted by amino-terminal mutations in histone H4
    • Roth,S.Y., Shimizu,M. Johnson,L., Grunstein,M. and Simpson,R.T. (1992) Stable nucleosome positioning and complete repression by the yeast α2 represser are disrupted by amino-terminal mutations in histone H4. Genes Dev., 6, 411-425.
    • (1992) Genes Dev. , vol.6 , pp. 411-425
    • Roth, S.Y.1    Shimizu, M.2    Johnson, L.3    Grunstein, M.4    Simpson, R.T.5
  • 64
    • 0022374891 scopus 로고
    • Interaction of a gene-specific transcription factor with the adenovirus major late promoter upstream of the TATA box region
    • Sawadogo,M. and Roeder,R.G. (1985) Interaction of a gene-specific transcription factor with the adenovirus major late promoter upstream of the TATA box region. Cell, 43, 165-175.
    • (1985) Cell , vol.43 , pp. 165-175
    • Sawadogo, M.1    Roeder, R.G.2
  • 65
    • 0023752096 scopus 로고
    • Multiple forms of the gene-specific transcription factor USF I: Complete purification and identification of USF from HeLa cell nuclei
    • Sawadogo,M., Van Dyke,M.W., Gregor,P.D. and Roeder,R.G. (1988) Multiple forms of the gene-specific transcription factor USF I: complete purification and identification of USF from HeLa cell nuclei. J. Biol. Chem., 263, 11985-11993.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11985-11993
    • Sawadogo, M.1    Van Dyke, M.W.2    Gregor, P.D.3    Roeder, R.G.4
  • 66
    • 23444453049 scopus 로고
    • Ubiquitous expression of the 43- and 44-kDa forms of transcription factor USF in mammalian cells
    • Sirito,M., Lin,Q., Maity,T. and Sawadogo,M. (1994) Ubiquitous expression of the 43- and 44-kDa forms of transcription factor USF in mammalian cells. Nucleic Acids. Res., 22, 427-433.
    • (1994) Nucleic Acids. Res. , vol.22 , pp. 427-433
    • Sirito, M.1    Lin, Q.2    Maity, T.3    Sawadogo, M.4
  • 67
    • 0027413988 scopus 로고
    • Histones, nucleosomes and transcription
    • Svaren,J. and Horz,W. (1993) Histones, nucleosomes and transcription. Curr. Opin. Genet. Dev., 3, 219-225.
    • (1993) Curr. Opin. Genet. Dev. , vol.3 , pp. 219-225
    • Svaren, J.1    Horz, W.2
  • 68
    • 0025266610 scopus 로고
    • Alternative chromatin structure at CpG islands
    • Tazi,J. and Bird,A. (1990) Alternative chromatin structure at CpG islands. Cell, 60, 909-920.
    • (1990) Cell , vol.60 , pp. 909-920
    • Tazi, J.1    Bird, A.2
  • 69
    • 0025779831 scopus 로고
    • Histone acetylation and control of gene expression
    • Turner,B.M. (1991) Histone acetylation and control of gene expression. J. Cell Sci., 99, 13-20.
    • (1991) J. Cell Sci. , vol.99 , pp. 13-20
    • Turner, B.M.1
  • 70
    • 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
  • 71
    • 0029349023 scopus 로고
    • Hislone acetylation in chromatin and chromosomes
    • Turner,B.M. and O'Neill,L.P. (1995) Hislone acetylation in chromatin and chromosomes. Semin. Cell Biol., 6, 229-236.
    • (1995) Semin. Cell Biol. , vol.6 , pp. 229-236
    • Turner, B.M.1    O'Neill, L.P.2
  • 72
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner,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
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 73
    • 0020478758 scopus 로고
    • Regulation of histone acetylation in Tetrahymena macro- and micronuclei
    • Vavra,K.J., Allis,C.D. and Gorovsky,M.A. (1982) Regulation of histone acetylation in Tetrahymena macro- and micronuclei. J. Biol. Chem., 257, 2591-2598.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2591-2598
    • Vavra, K.J.1    Allis, C.D.2    Gorovsky, M.A.3
  • 74
    • 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
  • 77
    • 0029015717 scopus 로고
    • Yeast histone H3 and H4 N termini function through different GAL1 regulatory elements to repress and activate transcription
    • Wan,J.S., Mann,R.K. and Grunstein,M. (1995) Yeast histone H3 and H4 N termini function through different GAL1 regulatory elements to repress and activate transcription. Proc. Natl Acad. Sci. USA, 92, 5664-5668.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5664-5668
    • Wan, J.S.1    Mann, R.K.2    Grunstein, M.3
  • 78
    • 0026641776 scopus 로고
    • Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection
    • Winston,F. and Carlson,M. (1992) Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection. Trends Genet., 8, 387-391.
    • (1992) Trends Genet. , vol.8 , pp. 387-391
    • Winston, F.1    Carlson, M.2
  • 79
    • 0028176808 scopus 로고
    • Nucleosome positioning and modification: Chromatin structures that potentiate transcription
    • Wolffe,A.P. (1994) Nucleosome positioning and modification: chromatin structures that potentiate transcription. Trends Biochem. Sci., 19, 240-244.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 240-244
    • Wolffe, A.P.1
  • 80
    • 0027096119 scopus 로고
    • Nucleosome core displacement in vitro via a metastable transcription factor:nucleosome complex
    • Workman,J.L. and Kingston,R.E. (1992) Nucleosome core displacement in vitro via a metastable transcription factor:nucleosome complex. Science, 258, 1780-1784.
    • (1992) Science , vol.258 , pp. 1780-1784
    • Workman, J.L.1    Kingston, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.