메뉴 건너뛰기




Volumn 6, Issue 2, 1996, Pages 176-184

Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; HISTONE ACETYLTRANSFERASE;

EID: 0029925512     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(96)80048-7     Document Type: Article
Times cited : (486)

References (83)
  • 2
    • 0026441880 scopus 로고
    • Reversible histone modifications and the chromosome cell cycle
    • Bradbury EM: Reversible histone modifications and the chromosome cell cycle. Bioessays 1992, 14:9-16.
    • (1992) Bioessays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 3
    • 0025122175 scopus 로고
    • On the biological role of histone acetylation
    • Csordas A: On the biological role of histone acetylation. Biochem J 1990, 265:23-38.
    • (1990) Biochem J , vol.265 , pp. 23-38
    • Csordas, A.1
  • 4
    • 0028608018 scopus 로고
    • Histone acetylation: Facts and questions
    • Loidl P: Histone acetylation: facts and questions. Chromosoma 1994, 103:441-449.
    • (1994) Chromosoma , vol.103 , pp. 441-449
    • Loidl, P.1
  • 5
    • 0029349023 scopus 로고
    • Histone acetylation in chromatin and chromosomes
    • Turner BM, O'Neill LP: Histone acetylation in chromatin and chromosomes. Semin Cell Biol 1995, 6:229-236.
    • (1995) Semin Cell Biol , vol.6 , pp. 229-236
    • Turner, B.M.1    O'Neill, L.P.2
  • 6
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey VG, Faulkner R, Mirsky AE: Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci USA 1964, 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
  • 7
    • 0028236523 scopus 로고
    • Transcription: In tune with the histones
    • Wolffe AP: Transcription: in tune with the histones. Cell 1994, 77:13-16.
    • (1994) Cell , vol.77 , pp. 13-16
    • Wolffe, A.P.1
  • 8
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes TR, Thorne AW, Crane-Robinson C: A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J 1988, 7:1395-1403.
    • (1988) EMBO J , vol.7 , pp. 1395-1403
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 10
    • 0029119093 scopus 로고
    • Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner
    • ••] an anti-acetyllysine antibody was used to directly demonstrate enrichment of acetylated H4 in transcriptionally 'poised' chromatin versus bulk chromatin in a region that coincided with a region of increased DNase I sensitivity (the chicken β-globin locus), thus fitting with the idea that acetylation is related to gene activation. In this paper, immunoprecipitation experiments using antibodies directed against H4 acetylated at specific sites failed to show enrichment of acetylated histone in active versus bulk chromatin, although H4 associated with pericentric heterochromatin was underacetylated. In similar studies ([14]; M Braunstein, CD Allis, BM Turner, JR Broach, unpublished data) using both antibodies directed towards acetylated and unacetylated forms of H3 and H4 demonstrate that inactive loci are enriched in hypoacetylated histones, although some specific acetylated sites may predominate (i.e. H4.Ac12).
    • (1995) EMBO J , vol.14 , pp. 3946-3957
    • O'Neill, L.P.1    Turner, B.M.2
  • 11
    • 0024280881 scopus 로고
    • Extremely conserved histone H4 N-terminus is dispensible for growth but essential for repressing the silent mating loci in yeast
    • Kayne PS, Kim UJ, Han M, Mullen JR, Yoshizaki F, Grunstein M: Extremely conserved histone H4 N-terminus is dispensible for growth but essential for repressing the silent mating loci in yeast. Cell 1988, 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
  • 12
    • 0025736044 scopus 로고
    • Yeast histone H4 N-terminal sequence is required for promoter activation in vivo
    • Durrin LK, Mann RK, Kayne PS, Grunstein M: Yeast histone H4 N-terminal sequence is required for promoter activation in vivo. Cell 1991, 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
  • 14
    • 0027192267 scopus 로고
    • Transcriptional silencing in yeast is associated with reduced nucleosome acetylation
    • Braunstein M, Rose AB, Holmes SG, Allis CD, Broach JR: Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev 1993, 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
  • 16
    • 0028559510 scopus 로고
    • Differential repression of transcription factor binding by histone H1 is regulated by the core histone amino termini
    • Juan L-J, Utley RT, Adams CC, Vettesse-Dadey M, Workman JL: Differential repression of transcription factor binding by histone H1 is regulated by the core histone amino termini. EMBO J 1994, 13:6031-6040.
    • (1994) EMBO J , vol.13 , pp. 6031-6040
    • Juan, L.-J.1    Utley, R.T.2    Adams, C.C.3    Vettesse-Dadey, M.4    Workman, J.L.5
  • 17
    • 0028127302 scopus 로고
    • Core histone acetylation does not block linker histone binding to a nucleosome including a Xenopus borealis 5 S rRNA gene
    • Ura K, Wolffe AP, Hayes JJ: Core histone acetylation does not block linker histone binding to a nucleosome including a Xenopus borealis 5 S rRNA gene. J Biol Chem 1994, 269:27171-27174.
    • (1994) J Biol Chem , vol.269 , pp. 27171-27174
    • Ura, K.1    Wolffe, A.P.2    Hayes, J.J.3
  • 18
    • 0027429520 scopus 로고
    • Chromatin transitions during early Xenopus embryogenesis: Changes in histone H4 acetylation and in linker histone type
    • Dimitrov S, Almouzni G, Dasso M, Wolffe AP: Chromatin transitions during early Xenopus embryogenesis: changes in histone H4 acetylation and in linker histone type. Dev Biol 1993, 160:214-227.
    • (1993) Dev Biol , vol.160 , pp. 214-227
    • Dimitrov, S.1    Almouzni, G.2    Dasso, M.3    Wolffe, A.P.4
  • 19
    • 0029091306 scopus 로고
    • A positive role for nucleosome mobility in the transcriptional activity of chromatin templates: Restriction by linker histones
    • Ura K, Hayes JJ, Wolffe AP: A positive role for nucleosome mobility in the transcriptional activity of chromatin templates: restriction by linker histones. EMBO J 1995, 14:3752-3765.
    • (1995) EMBO J , vol.14 , pp. 3752-3765
    • Ura, K.1    Hayes, J.J.2    Wolffe, A.P.3
  • 20
    • 0027465862 scopus 로고
    • A positive role for histone acetylation in transcription factor access to nucleosomal DNA
    • Lee DY, Hayes JJ, Pruss D, Wolffe AP: A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell 1993, 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
  • 21
    • 0028127762 scopus 로고
    • Role of the histone amino termini in faciliated binding of a transcription factor, GAL4-AH, to nucleosome cores
    • Vettesse-Dadey M, Walter P, Chen H, Juan L-J, Workman JL: Role of the histone amino termini in faciliated binding of a transcription factor, GAL4-AH, to nucleosome cores. Mol Cell Biol 1994, 14:970-981.
    • (1994) Mol Cell Biol , vol.14 , pp. 970-981
    • Vettesse-Dadey, M.1    Walter, P.2    Chen, H.3    Juan, L.-J.4    Workman, J.L.5
  • 22
    • 0028933783 scopus 로고
    • Yeast histone H4 and H3 N-termini have different effects on the chromatin structure of the GAL1 promoter
    • Fisher-Adams G, Grunstein M: Yeast histone H4 and H3 N-termini have different effects on the chromatin structure of the GAL1 promoter. EMBO J 1995, 14:1468-1477.
    • (1995) EMBO J , vol.14 , pp. 1468-1477
    • Fisher-Adams, G.1    Grunstein, M.2
  • 23
    • 0028906077 scopus 로고
    • Chromatin-mediated transcriptional repression in yeast
    • Roth SY: Chromatin-mediated transcriptional repression in yeast. Curr Opin Genet Dev 1995, 5:168-173.
    • (1995) Curr Opin Genet Dev , vol.5 , pp. 168-173
    • Roth, S.Y.1
  • 24
    • 0026556122 scopus 로고
    • Identification of a non-basic domain in the histone H4 N-terminus required for repression of the yeast silent mating loci
    • Johnson LM, Fisher-Adams G, Grunstein M: Identification of a non-basic domain in the histone H4 N-terminus required for repression of the yeast silent mating loci. EMBO J 1992, 11:2201-2209.
    • (1992) EMBO J , vol.11 , pp. 2201-2209
    • Johnson, L.M.1    Fisher-Adams, G.2    Grunstein, M.3
  • 25
    • 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
    • •], biochemical and genetic evidence for the interaction of Sir3 and Sir4 with the amino termini of H3 and H4 is shown to be dependent on specific histone silencing domains. Combined with data from genetic analyses and immunofluorescence studies with anti-RAP1 and Sir3 antibodies, a model is presented for the formation of heterochromatin-mediated transcriptional silencing in yeast.
    • (1995) Cell , vol.80 , pp. 583-592
    • Hecht, A.1    Laroche, T.2    Strahl-Bolsinger, S.3    Gasser, S.M.4    Grunstein, M.5
  • 26
    • 0028265920 scopus 로고
    • Assembly of nucleosomes: Do multiple assembly factors mean multiple mechanisms?
    • Kaufman PD, Botchan MR: Assembly of nucleosomes: do multiple assembly factors mean multiple mechanisms? Curr Opin Genet Dev 1995, 4:229-235.
    • (1995) Curr Opin Genet Dev , vol.4 , pp. 229-235
    • Kaufman, P.D.1    Botchan, M.R.2
  • 27
    • 0028888181 scopus 로고
    • Chromatin and nuclear assembly: Experimental approaches towards the reconstitution of transcriptionally active and silent states
    • Dimitrov S, Wolffe AP: Chromatin and nuclear assembly: experimental approaches towards the reconstitution of transcriptionally active and silent states. Biochim Biophys Acta 1995, 1260:1-13.
    • (1995) Biochim Biophys Acta , vol.1260 , pp. 1-13
    • Dimitrov, S.1    Wolffe, A.P.2
  • 28
    • 0029397731 scopus 로고
    • Nucleosome assembly during DNA replication
    • Krude T: Nucleosome assembly during DNA replication. Curr Biol 1995, 5:1232-1234.
    • (1995) Curr Biol , vol.5 , pp. 1232-1234
    • Krude, T.1
  • 29
    • 0002216824 scopus 로고
    • Histone acetylation during chromatin replication and nucleosome assembly
    • Annunziato AT: Histone acetylation during chromatin replication and nucleosome assembly. The Nucleus 1995, 1:31-56.
    • (1995) The Nucleus , vol.1 , pp. 31-56
    • Annunziato, A.T.1
  • 30
    • 0022365083 scopus 로고
    • Deposition-related histone acetylation in micronuclei of conjugating Tetrahymena
    • Allis CD, Chicoine LG, Richman R, Schulman IG: Deposition-related histone acetylation in micronuclei of conjugating Tetrahymena. Proc Natl Acad Sci USA 1985, 82:8048-8052.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8048-8052
    • Allis, C.D.1    Chicoine, L.G.2    Richman, R.3    Schulman, I.G.4
  • 32
    • 0022650761 scopus 로고
    • Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena
    • Chicoine LG, Schulman IG, Richman R, Cook RG, Allis CD: Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena. J Biol Chem 1986, 261:1071-1076.
    • (1986) J Biol Chem , vol.261 , pp. 1071-1076
    • Chicoine, L.G.1    Schulman, I.G.2    Richman, R.3    Cook, R.G.4    Allis, C.D.5
  • 33
    • 0028356458 scopus 로고
    • Non-random acetylation of histone H4 by a cytoplasmic histone acetyltransferase as determined by novel methodology
    • Sobel RE, Cook RG, Allis CD: Non-random acetylation of histone H4 by a cytoplasmic histone acetyltransferase as determined by novel methodology. J Biol Chem 1994, 269:18576-18582. This paper describes the first application of a protein deblocking procedure that allows the identification of acetyllysine residues in otherwise amino-terminally blocked H4s.
    • (1994) J Biol Chem , vol.269 , pp. 18576-18582
    • Sobel, R.E.1    Cook, R.G.2    Allis, C.D.3
  • 34
    • 0028847955 scopus 로고
    • Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4
    • Sobel RE, Cook RG, Perry CA, Annunziato AT, Allis CD: Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4. Proc Natl Acad Sci USA 1995, 92:1237-1241.
    • (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
  • 35
    • 0019876888 scopus 로고
    • Histone acetylase from Drosophila melanogaster specific for H4
    • Weingand RC, Brutlag DL: Histone acetylase from Drosophila melanogaster specific for H4. J Biol Chem 1981, 256:4578-4583.
    • (1981) J Biol Chem , vol.256 , pp. 4578-4583
    • Weingand, R.C.1    Brutlag, D.L.2
  • 36
    • 0023944270 scopus 로고
    • Micronuclei and the cytoplasm of growing Tetrahymena contain a histone acetylase activity which Is highly specific for free histone H4
    • Richman R, Chicoine LG, Collini MP, Cook RG, Allis CD: Micronuclei and the cytoplasm of growing Tetrahymena contain a histone acetylase activity which Is highly specific for free histone H4. J Cell Biol 1988, 106:1017-1026.
    • (1988) J Cell Biol , vol.106 , pp. 1017-1026
    • Richman, R.1    Chicoine, L.G.2    Collini, M.P.3    Cook, R.G.4    Allis, C.D.5
  • 37
    • 0027493762 scopus 로고
    • Site specificity of pea histone acetyltransferase B in vitro
    • Mingarro I, Sendra R, Salvador ML, Franco L: Site specificity of pea histone acetyltransferase B in vitro. J Biol Chem 1993, 268:13248-13252.
    • (1993) J Biol Chem , vol.268 , pp. 13248-13252
    • Mingarro, I.1    Sendra, R.2    Salvador, M.L.3    Franco, L.4
  • 39
    • 0024372060 scopus 로고
    • Purification and characterization of CAF1, a human cell factor required for chromatin assembly during DNA replication in vitro
    • Smith S, Stillman B: Purification and characterization of CAF1, a human cell factor required for chromatin assembly during DNA replication in vitro. Cell 1989, 58:15-25.
    • (1989) Cell , vol.58 , pp. 15-25
    • Smith, S.1    Stillman, B.2
  • 42
    • 0019321908 scopus 로고
    • Extensive purification of histone acetylase A, the major histone N-acetyl transferase activity detected in mammalian cell nuclei
    • Belikoff E, Wong L-J, Alberts BM: Extensive purification of histone acetylase A, the major histone N-acetyl transferase activity detected in mammalian cell nuclei. J Biol Chem 1980, 255:11448-11453.
    • (1980) J Biol Chem , vol.255 , pp. 11448-11453
    • Belikoff, E.1    Wong, L.-J.2    Alberts, B.M.3
  • 43
    • 0020479720 scopus 로고
    • Studies on histone acetyltransferase; partial purification and basic properties
    • Wiktorowicz JE, Bonner J: Studies on histone acetyltransferase; partial purification and basic properties. J Biol Chem 1982, 257:12893-12900.
    • (1982) J Biol Chem , vol.257 , pp. 12893-12900
    • Wiktorowicz, J.E.1    Bonner, J.2
  • 44
    • 0021715521 scopus 로고
    • Extensive purification and characterization of chromatin-bound histone acetyltransferase from Saccharomyces cerevisiae
    • Travis GH, Colavito-Shepanski M, Grunstein M: Extensive purification and characterization of chromatin-bound histone acetyltransferase from Saccharomyces cerevisiae. J Biol Chem 1984, 259:14406-14412.
    • (1984) J Biol Chem , vol.259 , pp. 14406-14412
    • Travis, G.H.1    Colavito-Shepanski, M.2    Grunstein, M.3
  • 45
    • 0021367196 scopus 로고
    • Porcine liver nuclear histone acetyltransferase; partial purification and basic properties
    • Kelner DN, McCarty KS: Porcine liver nuclear histone acetyltransferase; partial purification and basic properties. J Biol Chem 1984, 259:3413-3418.
    • (1984) J Biol Chem , vol.259 , pp. 3413-3418
    • Kelner, D.N.1    McCarty, K.S.2
  • 46
    • 0021254356 scopus 로고
    • Two species of histone acetyltransferase in rat liver nuclei
    • Yukioka M, Sasaki S, Qi S-L, Inoue A: Two species of histone acetyltransferase in rat liver nuclei. J Biol Chem 1984, 259:8372-8377.
    • (1984) J Biol Chem , vol.259 , pp. 8372-8377
    • Yukioka, M.1    Sasaki, S.2    Qi, S.-L.3    Inoue, A.4
  • 48
    • 0025259430 scopus 로고
    • Purification and characterization of two porcine liver nuclear histone acetyltransferases
    • Attisano L, Lewis PN: Purification and characterization of two porcine liver nuclear histone acetyltransferases. J Biol Chem 1990, 265:3949-3955.
    • (1990) J Biol Chem , vol.265 , pp. 3949-3955
    • Attisano, L.1    Lewis, P.N.2
  • 49
    • 0025824384 scopus 로고
    • Subcellular localization and nucleosome specificity of yeast histone acetyltransferases
    • López-Rodas G, Tordera V, Sánchez del Pino MM, Franco L: Subcellular localization and nucleosome specificity of yeast histone acetyltransferases. Biochemistry 1991, 30:3728-3732.
    • (1991) Biochemistry , vol.30 , pp. 3728-3732
    • López-Rodas, G.1    Tordera, V.2    Sánchez Del Pino, M.M.3    Franco, L.4
  • 50
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast GCN5 linking histone acetylation to gene activation
    • in press
    • •] describe the identification and subsequent cloning of the gene that encodes p55: a catalytically active HAT from Tetrahymena macronuclei, Analysis of the derived sequence of p55 revealed extensive homology to Gcn5p, a yeast transcription co-adaptor, thus establishing a direct link between acetyltransferases and gene activation.
    • (1996) Cell
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Roth, S.Y.5    Allis, C.D.6
  • 51
    • 0026783834 scopus 로고
    • Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription
    • Georgakopoulos T, Thireos G: Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription. EMBO J 1992, 11:4145-4152.
    • (1992) EMBO J , vol.11 , pp. 4145-4152
    • Georgakopoulos, T.1    Thireos, G.2
  • 53
    • 0028876860 scopus 로고
    • ADA3, a putative transcriptional adaptor, consists of two separable domains and interacts with ADA2 and GCN5 in a trimeric complex
    • ••], provides an immediate mechanism for targeting HAT A to chromatin for transcriptional activation.
    • (1995) Mol Cell Biol , vol.15 , pp. 1203-1209
    • Horiuchi, J.1    Silverman, N.2    Marcus, G.A.3    Guarente, L.4
  • 57
    • 0028840419 scopus 로고
    • Transcriptional coactivators in yeast and beyond
    • Guarente L: Transcriptional coactivators in yeast and beyond. Trends Biochem Sci 1995, 20:516-521.
    • (1995) Trends Biochem Sci , vol.20 , pp. 516-521
    • Guarente, L.1
  • 58
    • 0030030611 scopus 로고    scopus 로고
    • Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5
    • Candau R, Moore PA, Wand L, Barlev N, Ying CY, Rosen CA, Berger SL: Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5. Mol Cell Biol 1996, 16:593-602.
    • (1996) Mol Cell Biol , vol.16 , pp. 593-602
    • Candau, R.1    Moore, P.A.2    Wand, L.3    Barlev, N.4    Ying, C.Y.5    Rosen, C.A.6    Berger, S.L.7
  • 60
    • 0014321608 scopus 로고
    • Evidence for histidine in the active site of papain
    • Husain SS, Lowe G: Evidence for histidine in the active site of papain. Biochem J 1968, 108:855-859.
    • (1968) Biochem J , vol.108 , pp. 855-859
    • Husain, S.S.1    Lowe, G.2
  • 61
    • 0027097978 scopus 로고
    • Peroxisomal acetoacetyl-CoA thiolase of an n-alkane-utilizing yeast, Canadida tropicalis
    • Kurihara T, Ueda M, Kanayama N, Kondo J, Ternishi Y, Tanaka A: Peroxisomal acetoacetyl-CoA thiolase of an n-alkane-utilizing yeast, Canadida tropicalis. Eur J Biochem 1992, 210:999-1005.
    • (1992) Eur J Biochem , vol.210 , pp. 999-1005
    • Kurihara, T.1    Ueda, M.2    Kanayama, N.3    Kondo, J.4    Ternishi, Y.5    Tanaka, A.6
  • 62
    • 0026637547 scopus 로고
    • 3-Hydroxy-3-methylglutaryl coenzyme A lyase: Affinity labeling of the Pseudomonas mevalonii enzyme and assignment of cysteine-237 to the active site
    • Hruz PW, Narasimhan C, Miziorko HM: 3-Hydroxy-3-methylglutaryl coenzyme A lyase: affinity labeling of the Pseudomonas mevalonii enzyme and assignment of cysteine-237 to the active site. Biochemistry 1992, 31:6842-6847.
    • (1992) Biochemistry , vol.31 , pp. 6842-6847
    • Hruz, P.W.1    Narasimhan, C.2    Miziorko, H.M.3
  • 65
    • 0029848521 scopus 로고    scopus 로고
    • Histone modifications, chromatin structure and the nuclear matrix
    • in press
    • Davie JR: Histone modifications, chromatin structure and the nuclear matrix. J Cell Biochem 1996, in press.
    • (1996) J Cell Biochem
    • Davie, J.R.1
  • 67
    • 0022551258 scopus 로고
    • Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of yeast
    • Hope IA, Struhl K: Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of yeast Cell 1986, 46:885-894.
    • (1986) Cell , vol.46 , pp. 885-894
    • Hope, I.A.1    Struhl, K.2
  • 68
    • 0025600929 scopus 로고
    • Mutation in a heterochromatin-specific chromosomal protein is associated with suppression of position-effect variegation in Drosophila melanogaster
    • Eissenberg JC, James TC, Foster-Hartnett DM, Hartnett T, Ngan V, Elgin SCR: Mutation in a heterochromatin-specific chromosomal protein is associated with suppression of position-effect variegation in Drosophila melanogaster. Proc Natl Acad Sci USA 1990, 87:9923-9927.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9923-9927
    • Eissenberg, J.C.1    James, T.C.2    Foster-Hartnett, D.M.3    Hartnett, T.4    Ngan, V.5    Elgin, S.C.R.6
  • 69
    • 0025202707 scopus 로고
    • Imprinting a determined state into the chromatin of Drosophila
    • Paro R: Imprinting a determined state into the chromatin of Drosophila. Trends Genet 1990, 6:416-421.
    • (1990) Trends Genet , vol.6 , pp. 416-421
    • Paro, R.1
  • 70
    • 0026701037 scopus 로고
    • Analysis of the functional role of the Polycomb chromodomain in Drosophila melanogaster
    • Messmer S, Franke A, Paro R: Analysis of the functional role of the Polycomb chromodomain in Drosophila melanogaster, Genes Dev 1992, 6:1241-1254.
    • (1992) Genes Dev , vol.6 , pp. 1241-1254
    • Messmer, S.1    Franke, A.2    Paro, R.3
  • 71
    • 0027497501 scopus 로고
    • Overlapping domains of the heterochromatin associated protein HP1 mediate nuclear localization and heterochromatin binding
    • Powers J, Eissenberg JC: Overlapping domains of the heterochromatin associated protein HP1 mediate nuclear localization and heterochromatin binding. J Cell Biol 1993, 120:291-299.
    • (1993) J Cell Biol , vol.120 , pp. 291-299
    • Powers, J.1    Eissenberg, J.C.2
  • 72
    • 0029645289 scopus 로고
    • Functional analysis of the chromodomain of HP1
    • Platero JS, Hartnett T, Eissenberg JC: Functional analysis of the chromodomain of HP1, EMBO J 1995, 14:3977-3986.
    • (1995) EMBO J , vol.14 , pp. 3977-3986
    • Platero, J.S.1    Hartnett, T.2    Eissenberg, J.C.3
  • 73
    • 0028943705 scopus 로고
    • A new class of histone H2A mutations in Saccharomyces cerevisiae causes specific transcriptional defects
    • Hirschorn JN, Bortvin AL, Ricupero-Hovasse SL, Winston F: A new class of histone H2A mutations in Saccharomyces cerevisiae causes specific transcriptional defects. Mol Cell Biol 1992, 15:1999-2009.
    • (1992) Mol Cell Biol , vol.15 , pp. 1999-2009
    • Hirschorn, J.N.1    Bortvin, A.L.2    Ricupero-Hovasse, S.L.3    Winston, F.4
  • 74
    • 0027295019 scopus 로고
    • The yeast SNF2/SWI2 protein has DNA-stimulated ATPase activity required for transcriptional activation
    • Laurent BC, Treich I, Carlson M: The yeast SNF2/SWI2 protein has DNA-stimulated ATPase activity required for transcriptional activation. Genes Dev 1993, 7:583-591.
    • (1993) Genes Dev , vol.7 , pp. 583-591
    • Laurent, B.C.1    Treich, I.2    Carlson, M.3
  • 75
    • 0026641776 scopus 로고
    • Yeast SNF/SWI transcriptional activators and SPT/SIN chromatin connection
    • Winston F, Carlson M: Yeast SNF/SWI transcriptional activators and SPT/SIN chromatin connection. Trends Genet 1992, 8:387-391.
    • (1992) Trends Genet , vol.8 , pp. 387-391
    • Winston, F.1    Carlson, M.2
  • 76
    • 0028292448 scopus 로고
    • The SNF/SWI family of global transcriptional activators
    • Carlson M, Laurent BC: The SNF/SWI family of global transcriptional activators. Curr Opin Cell Biol 1994, 6:396-402.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 396-402
    • Carlson, M.1    Laurent, B.C.2
  • 79
    • 0028987268 scopus 로고
    • The SWI-SNF complex: A chromatin remodeling machine?
    • Peterson CL, Tamkun JW: The SWI-SNF complex: a chromatin remodeling machine? Trends Biochem Sci 1995, 20:143-146.
    • (1995) Trends Biochem Sci , vol.20 , pp. 143-146
    • Peterson, C.L.1    Tamkun, J.W.2
  • 81
    • 0028904453 scopus 로고
    • The RNA polymerase II holoenzyme and its implications for gene regulation
    • Koleske AJ, Young RA: The RNA polymerase II holoenzyme and its implications for gene regulation. Trends Biochem Sci 1995, 20:113-116.
    • (1995) Trends Biochem Sci , vol.20 , pp. 113-116
    • Koleske, A.J.1    Young, R.A.2
  • 83
    • 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, Beppu T: Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function. Bioessays 1995, 17:423-430.
    • (1995) Bioessays , vol.17 , pp. 423-430
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.