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Volumn 19, Issue 6, 2003, Pages 321-329

The diverse functions of histone acetyltransferase complexes

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE ACETYLTRANSFERASE;

EID: 0038204415     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9525(03)00115-X     Document Type: Review
Times cited : (479)

References (70)
  • 1
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey V.G., et al. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. U. S. A. 51:1964;786-794.
    • (1964) Proc. Natl. Acad. Sci. U. S. A. , vol.51 , pp. 786-794
    • Allfrey, V.G.1
  • 2
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell J.E., et al. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell. 84:1996;843-851.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1
  • 3
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman J.L., et al. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 67:1998;545-579.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 545-579
    • Workman, J.L.1
  • 4
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., et al. The language of covalent histone modifications. Nature. 403:2000;41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1
  • 5
    • 0031835267 scopus 로고    scopus 로고
    • Co-activators and co-repressors in the integration of transcriptional responses
    • Torchia J., et al. Co-activators and co-repressors in the integration of transcriptional responses. Curr. Opin. Cell Biol. 10:1998;373-383.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 373-383
    • Torchia, J.1
  • 6
    • 0034912742 scopus 로고    scopus 로고
    • Histone acetyltransferases
    • Roth S.Y., et al. Histone acetyltransferases. Annu. Rev. Biochem. 70:2001;81-120.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 81-120
    • Roth, S.Y.1
  • 7
    • 0030954208 scopus 로고    scopus 로고
    • GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein
    • Neuwald A.F., et al. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 22:1997;154-155.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 154-155
    • Neuwald, A.F.1
  • 8
    • 0037242383 scopus 로고    scopus 로고
    • The MYST family of histone acetyltransferases
    • Utley R.T., Cote J. The MYST family of histone acetyltransferases. Curr. Top. Microbiol. Immunol. 274:2003;203-236.
    • (2003) Curr. Top. Microbiol. Immunol. , vol.274 , pp. 203-236
    • Utley, R.T.1    Cote, J.2
  • 9
    • 0033590107 scopus 로고    scopus 로고
    • Sas3 is a histone acetyltransferase and requires a zinc finger motif
    • Takechi S., et al. Sas3 is a histone acetyltransferase and requires a zinc finger motif. Biochem. Biophys. Res. Commun. 266:1999;405-410.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 405-410
    • Takechi, S.1
  • 10
    • 0030797349 scopus 로고    scopus 로고
    • Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: Characterization of an Ada complex and the SAGA (Spt/Ada) complex
    • Grant P.A., et al. Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex. Genes Dev. 11:1997;1640-1650.
    • (1997) Genes Dev. , vol.11 , pp. 1640-1650
    • Grant, P.A.1
  • 11
    • 0034637554 scopus 로고    scopus 로고
    • The yeast histone acetyltransferase A2 complex, but not free Gcn5p, binds stably to nucleosomal arrays
    • Sendra R., et al. The yeast histone acetyltransferase A2 complex, but not free Gcn5p, binds stably to nucleosomal arrays. J. Biol. Chem. 275:2000;24928-24934.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24928-24934
    • Sendra, R.1
  • 12
    • 0037041022 scopus 로고    scopus 로고
    • Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation
    • Balasubramanian R., et al. Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation. J. Biol. Chem. 277:2002;7989-7995.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7989-7995
    • Balasubramanian, R.1
  • 13
    • 0033605238 scopus 로고    scopus 로고
    • Expanded lysine acetylation specificity of Gcn5 in native complexes
    • Grant P.A., et al. Expanded lysine acetylation specificity of Gcn5 in native complexes. J. Biol. Chem. 274:1999;5895-5900.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5895-5900
    • Grant, P.A.1
  • 14
    • 0030712311 scopus 로고    scopus 로고
    • Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60
    • Yamamoto T., et al. Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60. J. Biol. Chem. 272:1997;30595-30598.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30595-30598
    • Yamamoto, T.1
  • 15
    • 0032965152 scopus 로고    scopus 로고
    • Esa1p is an essential histone acetyltransferase required for cell cycle progression
    • Clarke A.S., et al. Esa1p is an essential histone acetyltransferase required for cell cycle progression. Mol. Cell. Biol. 19:1999;2515-2526.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2515-2526
    • Clarke, A.S.1
  • 16
    • 0033567954 scopus 로고    scopus 로고
    • NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p
    • Allard S., et al. NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p. EMBO J. 18:1999;5108-5119.
    • (1999) EMBO J. , vol.18 , pp. 5108-5119
    • Allard, S.1
  • 17
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • Ikura T., et al. Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell. 102:2000;463-473.
    • (2000) Cell , vol.102 , pp. 463-473
    • Ikura, T.1
  • 18
    • 85031177703 scopus 로고    scopus 로고
    • Yeast Enhancer of polycomb defines global Esa1-dependent acetylation of chromatin
    • in press
    • Boudreault, A.A. et al. Yeast Enhancer of polycomb defines global Esa1-dependent acetylation of chromatin. Genes Dev. (in press).
    • Genes Dev.
    • Boudreault, A.A.1
  • 19
    • 0033988212 scopus 로고    scopus 로고
    • The Drosophila MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation
    • Smith E.R., et al. The Drosophila MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation. Mol. Cell. Biol. 20:2000;312-318.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 312-318
    • Smith, E.R.1
  • 20
    • 0034657420 scopus 로고    scopus 로고
    • The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex
    • John S., et al. The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex. Genes Dev. 14:2000;1196-1208.
    • (2000) Genes Dev. , vol.14 , pp. 1196-1208
    • John, S.1
  • 21
    • 0032254147 scopus 로고    scopus 로고
    • The ATM-related cofactor Tra1 is a component of the purified SAGA complex
    • Grant P.A., et al. The ATM-related cofactor Tra1 is a component of the purified SAGA complex. Mol. Cell. 2:1998;863-867.
    • (1998) Mol. Cell , vol.2 , pp. 863-867
    • Grant, P.A.1
  • 22
    • 18744374136 scopus 로고    scopus 로고
    • The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway
    • Pray-Grant M.G., et al. The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway. Mol. Cell. Biol. 22:2002;8774-8786.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8774-8786
    • Pray-Grant, M.G.1
  • 23
    • 0037015044 scopus 로고    scopus 로고
    • SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription
    • Sterner D.E., et al. SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription. Proc. Natl. Acad. Sci. U. S. A. 99:2002;11622-11627.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11622-11627
    • Sterner, D.E.1
  • 24
    • 0032238342 scopus 로고    scopus 로고
    • The 400 kDa subunit of the PCAF acetylase complex belongs to the ATM superfamily
    • Vassilev A., et al. The 400 kDa subunit of the PCAF acetylase complex belongs to the ATM superfamily. Mol. Cell. 2:1998;869-875.
    • (1998) Mol. Cell , vol.2 , pp. 869-875
    • Vassilev, A.1
  • 25
    • 0033603317 scopus 로고    scopus 로고
    • Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction
    • Brand M., et al. Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. J. Biol. Chem. 274:1999;18285-18289.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18285-18289
    • Brand, M.1
  • 26
    • 0034812915 scopus 로고    scopus 로고
    • Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo
    • Martinez E., et al. Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. Mol. Cell. Biol. 21:2001;6782-6795.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6782-6795
    • Martinez, E.1
  • 27
    • 0033970431 scopus 로고    scopus 로고
    • The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc
    • McMahon S.B., et al. The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc. Mol. Cell. Biol. 20:2000;556-562.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 556-562
    • McMahon, S.B.1
  • 28
    • 0035933521 scopus 로고    scopus 로고
    • Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit
    • Brown C.E., et al. Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit. Science. 292:2001;2333-2337.
    • (2001) Science , vol.292 , pp. 2333-2337
    • Brown, C.E.1
  • 29
    • 0035793642 scopus 로고    scopus 로고
    • The yeast NuA4 and Drosophila MSL complexes contain homologous subunits important for transcription regulation
    • Eisen A., et al. The yeast NuA4 and Drosophila MSL complexes contain homologous subunits important for transcription regulation. J. Biol. Chem. 276:2001;3484-3491.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3484-3491
    • Eisen, A.1
  • 30
    • 0033964661 scopus 로고    scopus 로고
    • Mammalian chromodomain proteins: Their role in genome organisation and expression
    • Jones D.O., et al. Mammalian chromodomain proteins: their role in genome organisation and expression. BioEssays. 22:2000;124-137.
    • (2000) BioEssays , vol.22 , pp. 124-137
    • Jones, D.O.1
  • 31
    • 0031917787 scopus 로고    scopus 로고
    • Targeting of MOF, a putative histone acetyl transferase, to the X chromosome of Drosophila melanogaster
    • Gu W., et al. Targeting of MOF, a putative histone acetyl transferase, to the X chromosome of Drosophila melanogaster. Dev. Genet. 22:1998;56-64.
    • (1998) Dev. Genet. , vol.22 , pp. 56-64
    • Gu, W.1
  • 32
    • 0345654336 scopus 로고    scopus 로고
    • Identification of a gene that reverses the immortal phenotype of a subset of cells and is a member of a novel family of transcription factor-like genes
    • Bertram M.J., et al. Identification of a gene that reverses the immortal phenotype of a subset of cells and is a member of a novel family of transcription factor-like genes. Mol. Cell. Biol. 19:1999;1479-1485.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1479-1485
    • Bertram, M.J.1
  • 33
    • 0034780285 scopus 로고    scopus 로고
    • Role of an ING1 growth regulator in transcriptional activation and targeted histone acetylation by the NuA4 complex
    • Nourani A., et al. Role of an ING1 growth regulator in transcriptional activation and targeted histone acetylation by the NuA4 complex. Mol. Cell. Biol. 21:2001;7629-7640.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7629-7640
    • Nourani, A.1
  • 34
    • 0036293470 scopus 로고    scopus 로고
    • Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 H3 histone acetyltransferase complex
    • Howe L., et al. Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 H3 histone acetyltransferase complex. Mol. Cell. Biol. 22:2002;5047-5053.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5047-5053
    • Howe, L.1
  • 35
    • 0035577669 scopus 로고    scopus 로고
    • The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae
    • Meijsing S.H., et al. The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae. Genes Dev. 15:2001;3169-3182.
    • (2001) Genes Dev. , vol.15 , pp. 3169-3182
    • Meijsing, S.H.1
  • 36
    • 0035576789 scopus 로고    scopus 로고
    • The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1
    • Osada S., et al. The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1. Genes Dev. 15:2001;3155-3168.
    • (2001) Genes Dev. , vol.15 , pp. 3155-3168
    • Osada, S.1
  • 37
    • 0033623238 scopus 로고    scopus 로고
    • Loss of Gcn5l2 leads to increased apoptosis and mesodermal defects during mouse development
    • Xu W., et al. Loss of Gcn5l2 leads to increased apoptosis and mesodermal defects during mouse development. Nat. Genet. 26:2000;229-232.
    • (2000) Nat. Genet. , vol.26 , pp. 229-232
    • Xu, W.1
  • 38
    • 0032101179 scopus 로고    scopus 로고
    • Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase
    • Zhang W., et al. Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase. EMBO J. 17:1998;3155-3167.
    • (1998) EMBO J. , vol.17 , pp. 3155-3167
    • Zhang, W.1
  • 39
    • 0034269239 scopus 로고    scopus 로고
    • Global role for chromatin remodeling enzymes in mitotic gene expression
    • Krebs J.E., et al. Global role for chromatin remodeling enzymes in mitotic gene expression. Cell. 102:2000;587-598.
    • (2000) Cell , vol.102 , pp. 587-598
    • Krebs, J.E.1
  • 40
    • 0035979992 scopus 로고    scopus 로고
    • E2F transcriptional activation requires TRRAP and GCN5 cofactors
    • Lang S.E., et al. E2F transcriptional activation requires TRRAP and GCN5 cofactors. J. Biol. Chem. 276:2001;32627-32634.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32627-32634
    • Lang, S.E.1
  • 41
    • 0032581751 scopus 로고    scopus 로고
    • Transcriptional activators direct histone acetyltransferase complexes to nucleosomes
    • Utley R.T., et al. Transcriptional activators direct histone acetyltransferase complexes to nucleosomes. Nature. 394:1998;498-502.
    • (1998) Nature , vol.394 , pp. 498-502
    • Utley, R.T.1
  • 42
    • 0034212345 scopus 로고    scopus 로고
    • Distribution of acetylated histones resulting from Gal4-VP16 recruitment of SAGA and NuA4 complexes
    • Vignali M., et al. Distribution of acetylated histones resulting from Gal4-VP16 recruitment of SAGA and NuA4 complexes. EMBO J. 19:2000;2629-2640.
    • (2000) EMBO J. , vol.19 , pp. 2629-2640
    • Vignali, M.1
  • 43
    • 0035839135 scopus 로고    scopus 로고
    • Snf1 - a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription
    • Lo W.-S., et al. Snf1 - a histone kinase that works in concert with the histone acetyltransferase Gcn5 to regulate transcription. Science. 293:2001;1142-1146.
    • (2001) Science , vol.293 , pp. 1142-1146
    • Lo, W.-S.1
  • 44
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea S., et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature. 406:2000;593-599.
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1
  • 45
    • 0034704815 scopus 로고    scopus 로고
    • The Gcn5 bromodomain co-ordinates nucleosome remodelling
    • Syntichaki P., et al. The Gcn5 bromodomain co-ordinates nucleosome remodelling. Nature. 404:2000;414-417.
    • (2000) Nature , vol.404 , pp. 414-417
    • Syntichaki, P.1
  • 46
    • 0036847620 scopus 로고    scopus 로고
    • Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes
    • Hassan A.H., et al. Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes. Cell. 111:2002;369-379.
    • (2002) Cell , vol.111 , pp. 369-379
    • Hassan, A.H.1
  • 47
    • 0036258095 scopus 로고    scopus 로고
    • Components of the SAGA histone acetyltransferase complex are required for repressed transcription of ARG1 in rich medium
    • Ricci A.R., et al. Components of the SAGA histone acetyltransferase complex are required for repressed transcription of ARG1 in rich medium. Mol. Cell. Biol. 22:2002;4033-4042.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4033-4042
    • Ricci, A.R.1
  • 48
    • 0035875666 scopus 로고    scopus 로고
    • UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation
    • Brand M., et al. UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation. EMBO J. 20:2001;3187-3196.
    • (2001) EMBO J. , vol.20 , pp. 3187-3196
    • Brand, M.1
  • 49
    • 0027760994 scopus 로고
    • Dual roles of a multiprotein complex from S. cerevisiae in transcription and DNA repair
    • Feaver W.J., et al. Dual roles of a multiprotein complex from S. cerevisiae in transcription and DNA repair. Cell. 75:1993;1379-1387.
    • (1993) Cell , vol.75 , pp. 1379-1387
    • Feaver, W.J.1
  • 50
    • 0036888874 scopus 로고    scopus 로고
    • Histone h3 and the histone acetyltransferase hat1p contribute to DNA double-strand break repair
    • Qin S., et al. Histone h3 and the histone acetyltransferase hat1p contribute to DNA double-strand break repair. Mol. Cell. Biol. 22:2002;8353-8365.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8353-8365
    • Qin, S.1
  • 51
    • 0033634693 scopus 로고    scopus 로고
    • Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription
    • Galarneau L., et al. Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription. Mol. Cell. 5:2000;927-937.
    • (2000) Mol. Cell , vol.5 , pp. 927-937
    • Galarneau, L.1
  • 52
    • 0035577668 scopus 로고    scopus 로고
    • Histone H3 specific acetyltransferases are essential for cell cycle progression
    • Howe L., et al. Histone H3 specific acetyltransferases are essential for cell cycle progression. Genes Dev. 15:2001;3144-3154.
    • (2001) Genes Dev. , vol.15 , pp. 3144-3154
    • Howe, L.1
  • 53
    • 0035857061 scopus 로고    scopus 로고
    • Recruitment of TRRAP required for oncogenic transformation by E1A
    • Deleu L., et al. Recruitment of TRRAP required for oncogenic transformation by E1A. Oncogene. 20:2001;8270-8275.
    • (2001) Oncogene , vol.20 , pp. 8270-8275
    • Deleu, L.1
  • 54
    • 0034790436 scopus 로고    scopus 로고
    • Disruption of Trrap causes early embryonic lethality and defects in cell cycle progression
    • Herceg Z., et al. Disruption of Trrap causes early embryonic lethality and defects in cell cycle progression. Nat. Genet. 29:2001;206-211.
    • (2001) Nat. Genet. , vol.29 , pp. 206-211
    • Herceg, Z.1
  • 55
    • 0034515772 scopus 로고    scopus 로고
    • Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esa1 histone acetylase
    • Reid J.L., et al. Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esa1 histone acetylase. Mol. Cell. 6:2000;1297-1307.
    • (2000) Mol. Cell , vol.6 , pp. 1297-1307
    • Reid, J.L.1
  • 56
    • 0034707037 scopus 로고    scopus 로고
    • Global histone acetylation and deacetylation in yeast
    • Vogelauer M., et al. Global histone acetylation and deacetylation in yeast. Nature. 408:2000;495-498.
    • (2000) Nature , vol.408 , pp. 495-498
    • Vogelauer, M.1
  • 57
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X., et al. A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science. 293:2001;115-120.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1
  • 58
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein
    • Baek S.H., et al. Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein. Cell. 110:2002;55-67.
    • (2002) Cell , vol.110 , pp. 55-67
    • Baek, S.H.1
  • 59
    • 0034597001 scopus 로고    scopus 로고
    • Targeting the chromatin-remodeling MSL complex of Drosophila to its sites of action on the X chromosome requires both acetyl transferase and ATPase activities
    • Gu W., et al. Targeting the chromatin-remodeling MSL complex of Drosophila to its sites of action on the X chromosome requires both acetyl transferase and ATPase activities. EMBO J. 19:2000;5202-5211.
    • (2000) EMBO J. , vol.19 , pp. 5202-5211
    • Gu, W.1
  • 60
    • 0037126635 scopus 로고    scopus 로고
    • Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein
    • Kitabayashi I., et al. Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein. EMBO J. 20:2001;7184-7196.
    • (2001) EMBO J. , vol.20 , pp. 7184-7196
    • Kitabayashi, I.1
  • 61
    • 0029741343 scopus 로고    scopus 로고
    • Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases
    • Reifsnyder C., et al. Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases. Nat. Genet. 14:1996;42-48.
    • (1996) Nat. Genet. , vol.14 , pp. 42-48
    • Reifsnyder, C.1
  • 62
    • 0030939235 scopus 로고    scopus 로고
    • The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function
    • Ehrenhofer-Murray A.E., et al. The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function. Genetics. 145:1997;923-934.
    • (1997) Genetics , vol.145 , pp. 923-934
    • Ehrenhofer-Murray, A.E.1
  • 63
    • 0035254535 scopus 로고    scopus 로고
    • RNA polymerase III and RNA polymerase II promoter complexes are heterochromatin barriers in Saccharomyces cerevisiae
    • Donze D., et al. RNA polymerase III and RNA polymerase II promoter complexes are heterochromatin barriers in Saccharomyces cerevisiae. EMBO J. 20:2001;520-531.
    • (2001) EMBO J. , vol.20 , pp. 520-531
    • Donze, D.1
  • 64
    • 0036842129 scopus 로고    scopus 로고
    • Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin
    • Suka N., et al. Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine16 and spreading of heterochromatin. Nat. Genet. 32:2002;378-383.
    • (2002) Nat. Genet. , vol.32 , pp. 378-383
    • Suka, N.1
  • 65
    • 0036843170 scopus 로고    scopus 로고
    • Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing
    • Kimura A., et al. Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing. Nat. Genet. 32:2002;370-377.
    • (2002) Nat. Genet. , vol.32 , pp. 370-377
    • Kimura, A.1
  • 66
    • 0037197806 scopus 로고    scopus 로고
    • The MYST domain acetyltransferase chameau functions in epigenetic mechanisms of transcriptional repression
    • Grienenberger A., et al. The MYST domain acetyltransferase chameau functions in epigenetic mechanisms of transcriptional repression. Curr. Biol. 12:2002;762-766.
    • (2002) Curr. Biol. , vol.12 , pp. 762-766
    • Grienenberger, A.1
  • 67
    • 0031908714 scopus 로고    scopus 로고
    • Enhancer of Polycomb is a suppressor of position-effect variegation in Drosophila melanogaster
    • Sinclair D.A., et al. Enhancer of Polycomb is a suppressor of position-effect variegation in Drosophila melanogaster. Genetics. 148:1998;211-220.
    • (1998) Genetics , vol.148 , pp. 211-220
    • Sinclair, D.A.1
  • 68
    • 0037007236 scopus 로고    scopus 로고
    • Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation
    • Legube G., et al. Tip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation. EMBO J. 21:2002;1704-1712.
    • (2002) EMBO J. , vol.21 , pp. 1704-1712
    • Legube, G.1
  • 69
    • 0036889332 scopus 로고    scopus 로고
    • NuA4 subunit Yng2 function in intra-S-phase DNA damage response
    • Choy J.S., et al. NuA4 subunit Yng2 function in intra-S-phase DNA damage response. Mol. Cell. Biol. 22:2002;8215-8225.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8215-8225
    • Choy, J.S.1
  • 70
    • 0037179692 scopus 로고    scopus 로고
    • Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair
    • Bird A.W., et al. Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair. Nature. 419:2002;411-415.
    • (2002) Nature , vol.419 , pp. 411-415
    • Bird, A.W.1


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