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Volumn 89, Issue 3, 1997, Pages 341-347

Histone deacetylase activity is required for full transcriptional repression by mSin3A

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; ENZYME INHIBITOR; HELIX LOOP HELIX PROTEIN; HISTONE DEACETYLASE; LEUCINE ZIPPER PROTEIN; TRANSCRIPTION FACTOR; TRAPOXIN A; UNCLASSIFIED DRUG;

EID: 0031007189     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80214-7     Document Type: Article
Times cited : (675)

References (43)
  • 1
    • 0028084338 scopus 로고
    • Myc-max-mad: A transcription factor network controlling cell cycle progression, differentiation and death
    • Amati, B., and Land, H. (1994). Myc-Max-Mad: a transcription factor network controlling cell cycle progression, differentiation and death. Curr. Opin. Genet. Dev. 4, 102-108.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 102-108
    • Amati, B.1    Land, H.2
  • 2
    • 0027431276 scopus 로고
    • A switch from myc:Max to mad:Max heterocomplexes accompanies monocyte/macrophage differentiation
    • Ayer, D.E., and Eisenman, R.N. (1993). A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation. Genes Dev. 7, 2110-2119.
    • (1993) Genes Dev. , vol.7 , pp. 2110-2119
    • Ayer, D.E.1    Eisenman, R.N.2
  • 3
    • 0027408096 scopus 로고
    • Mad: A heterodimeric partner for max that antagonizes myc transcriptional activity
    • Ayer, D.E., Kretzner, L., and Eisenman, R.N. (1993). Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 72, 211-222.
    • (1993) Cell , vol.72 , pp. 211-222
    • Ayer, D.E.1    Kretzner, L.2    Eisenman, R.N.3
  • 4
    • 0028905563 scopus 로고
    • Mad-max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3
    • Ayer, D.E., Lawrence, Q.A., and Eisenman, R.N. (1995). Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell 50, 767-776.
    • (1995) Cell , vol.50 , pp. 767-776
    • Ayer, D.E.1    Lawrence, Q.A.2    Eisenman, R.N.3
  • 6
    • 0029353422 scopus 로고
    • Transcriptional regulation. Flipping the Myc switch
    • Bernards, R. (1995). Transcriptional regulation. Flipping the Myc switch. Curr. Biol. 5, 859-861.
    • (1995) Curr. Biol. , vol.5 , pp. 859-861
    • Bernards, R.1
  • 7
    • 0027192267 scopus 로고
    • Transcriptional 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). Transcriptional 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
  • 8
    • 0025297904 scopus 로고
    • Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate
    • Bresnick, E.H., John, S., Berard, D.S., LeFebvre, P., and Hager, G.L. (1990). Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate. Proc. Natl. Acad. Sci. USA 87, 3977-3981.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3977-3981
    • Bresnick, E.H.1    John, S.2    Berard, D.S.3    LeFebvre, P.4    Hager, G.L.5
  • 9
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase a: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell, J.E., Zhou, J., Ranalli.T., Kobayashi, R., Edmondson, D.G., Roth, S.Y., and Allis, C.D. (1996). Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84, 843-851.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Kobayashi, R.3    Edmondson, D.G.4    Roth, S.Y.5    Allis, C.D.6
  • 10
    • 0029805633 scopus 로고    scopus 로고
    • The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast
    • De Rubertis, F., Kadosh, D., Henchoz, S., Pauli, D., Reuter, G., Struhl, K., and Spierer, P. (1996). The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast. Nature 384, 589-591.
    • (1996) Nature , vol.384 , pp. 589-591
    • De Rubertis, F.1    Kadosh, D.2    Henchoz, S.3    Pauli, D.4    Reuter, G.5    Struhl, K.6    Spierer, P.7
  • 11
    • 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
  • 12
    • 0028889811 scopus 로고
    • Mad3 and Mad4: Novel Max-interacting transcriptional repressors that suppress c-Myc-dependent transformation and are expressed during neural and epidermal differentiation
    • Hurlin, P.J., Queva, C., Koskinen, P.J., Steingrimsson, E., Ayer, D.E., Copeland, N.G., Jenkins, N.A., and Eisenman, R.N. (1995). Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-Myc-dependent transformation and are expressed during neural and epidermal differentiation. EMBO J. 14, 5646-5659.
    • (1995) EMBO J. , vol.14 , pp. 5646-5659
    • Hurlin, P.J.1    Queva, C.2    Koskinen, P.J.3    Steingrimsson, E.4    Ayer, D.E.5    Copeland, N.G.6    Jenkins, N.A.7    Eisenman, R.N.8
  • 13
    • 0026657006 scopus 로고
    • Sodium butyrate inhibits myogenesis by interfering with the transcriptional activation function of MyoD and myogenin
    • Johnston, L.A., Tapscott, S.J., and Eisen, H. (1992). Sodium butyrate inhibits myogenesis by interfering with the transcriptional activation function of MyoD and myogenin. Mol. Cell. Biol. 12, 5123-5130.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5123-5130
    • Johnston, L.A.1    Tapscott, S.J.2    Eisen, H.3
  • 14
    • 0029982704 scopus 로고    scopus 로고
    • SIN3-dependent transcriptional repression by interaction with the Mad1 DNA binding protein
    • Kasten, M.M., Ayer, D.E., and Stillman, D.J. (1996). SIN3-dependent transcriptional repression by interaction with the Mad1 DNA binding protein. Mol. Cell. Biol. 16, 4215-4221.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4215-4221
    • Kasten, M.M.1    Ayer, D.E.2    Stillman, D.J.3
  • 15
    • 0029065748 scopus 로고
    • Repression of Myc-Ras cotransformation by Mad is mediated by multiple protein-protein interactions
    • Koskinen, P.J., Ayer, D.E., and Eisenman, R.N. (1995). Repression of Myc-Ras cotransformation by Mad is mediated by multiple protein-protein interactions. Cell. Growth Differ. 6, 623-629.
    • (1995) Cell. Growth Differ. , vol.6 , pp. 623-629
    • Koskinen, P.J.1    Ayer, D.E.2    Eisenman, R.N.3
  • 16
    • 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
  • 17
    • 0028608018 scopus 로고
    • Histone acetylation: Facts and questions
    • Loidl, P. (1994). Histone acetylation: facts and questions. Chromosoma 703, 441-449.
    • (1994) Chromosoma , vol.703 , pp. 441-449
    • Loidl, P.1
  • 18
    • 0027948984 scopus 로고
    • Functional similarity and physical association between GCN5 and ADA2: Putative transcriptional adaptors
    • Marcus, G.A., Silverman, N., Berger, S.L., Horiuchi, J., and Guarente, L. (1994). Functional similarity and physical association between GCN5 and ADA2: putative transcriptional adaptors. EMBO. 13, 4807-4815.
    • (1994) EMBO , vol.13 , pp. 4807-4815
    • Marcus, G.A.1    Silverman, N.2    Berger, S.L.3    Horiuchi, J.4    Guarente, L.5
  • 19
    • 0019132555 scopus 로고
    • Butyrate and related inhibitors of histone deacetylation block the induction of egg white genes by steroid hormones
    • McKnight, G.S., Hager, L., and Palmiter, R.D. (1980). Butyrate and related inhibitors of histone deacetylation block the induction of egg white genes by steroid hormones. Cell 22, 469-477.
    • (1980) Cell , vol.22 , pp. 469-477
    • McKnight, G.S.1    Hager, L.2    Palmiter, R.D.3
  • 20
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional activators p300 and CBP are histone acetylases
    • Ogryzko, V.V., Schiltz, R.L., Russanova, V., Howard, B.H., and Nakatani, Y. (1996). The transcriptional activators p300 and CBP are histone acetylases. 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
  • 21
    • 0030271392 scopus 로고    scopus 로고
    • The major cytoplasmic histone acetyltransferase in yeast: Links to chromatin replication and histone metabolism
    • Parthun, M.R., Windom, J., and Gottschling, D.E. (1996). The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism. Cell 87, 85-94.
    • (1996) Cell , vol.87 , pp. 85-94
    • Parthun, M.R.1    Windom, J.2    Gottschling, D.E.3
  • 22
    • 0027320814 scopus 로고
    • A retinoblastoma-binding protein related to a negative regulator of Ras in yeast
    • Qian, Y.W., Wang, Y.C., Hollingsworth, R.E., Jr., Jones, D., Ling, N., and Lee, E.Y. (1993). A retinoblastoma-binding protein related to a negative regulator of Ras in yeast. Nature 364, 648-652.
    • (1993) Nature , vol.364 , pp. 648-652
    • Qian, Y.W.1    Wang, Y.C.2    Hollingsworth R.E., Jr.3    Jones, D.4    Ling, N.5    Lee, E.Y.6
  • 23
  • 24
    • 0029856225 scopus 로고    scopus 로고
    • HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription
    • Rundlett, S.E., Carmen, A.A., Kobayashi, R., Bavykin, S., Turner, B.M., and Grunstein, M. (1996). HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc. Natl. Acad. Sci. USA 93, 14503-14508.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14503-14508
    • Rundlett, S.E.1    Carmen, A.A.2    Kobayashi, R.3    Bavykin, S.4    Turner, B.M.5    Grunstein, M.6
  • 25
    • 0028940364 scopus 로고
    • An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3
    • Schreiber-Agus, N., Chin, L., Chen, K., Torres, R., Rao, G., Guida, P., Skoultchi, A.I., and DePinho, R.A. (1995). An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell 80, 777-786.
    • (1995) Cell , vol.80 , pp. 777-786
    • Schreiber-Agus, N.1    Chin, L.2    Chen, K.3    Torres, R.4    Rao, G.5    Guida, P.6    Skoultchi, A.I.7    DePinho, R.A.8
  • 26
    • 0026582388 scopus 로고
    • Structure of the chicken myelomonocytic growth factor gene and specific activation of its promoter in avian myelomonocytic cells by protein kinases
    • Sterneck, E., Blattner, C., Graf, T., and Leutz, A. (1992). Structure of the chicken myelomonocytic growth factor gene and specific activation of its promoter in avian myelomonocytic cells by protein kinases. Mol. Cell. Biol. 12, 1728-1735.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1728-1735
    • Sterneck, E.1    Blattner, C.2    Graf, T.3    Leutz, A.4
  • 27
    • 0028297156 scopus 로고
    • Epistasis analysis of suppressor mutations that allow HO expression in the absence of the yeast SW15 transcriptional activator
    • Stillman, D.J., Dorland, S., and Yu, Y. (1994). Epistasis analysis of suppressor mutations that allow HO expression in the absence of the yeast SW15 transcriptional activator. Genetics 136, 781-788.
    • (1994) Genetics , vol.136 , pp. 781-788
    • Stillman, D.J.1    Dorland, S.2    Yu, Y.3
  • 28
    • 0028822470 scopus 로고
    • Suppressors of defective silencing in yeast: Effects on transcriptional repression at the HMR locus, cell growth and telomere structure
    • Sussel, L., Vannier, D., and Shore, D. (1995). Suppressors of defective silencing in yeast: effects on transcriptional repression at the HMR locus, cell growth and telomere structure. Genetics 141, 873-888.
    • (1995) Genetics , vol.141 , pp. 873-888
    • Sussel, L.1    Vannier, D.2    Shore, D.3
  • 29
    • 0029795991 scopus 로고    scopus 로고
    • Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function
    • Taunton, J., Collins, J.L., and Schreiber, S.L. (1996a). Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function. J. Am. Chem. Soc. 118, 10412-10422.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10412-10422
    • Taunton, J.1    Collins, J.L.2    Schreiber, S.L.3
  • 30
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C.A., and Schreiber, S.L. (1996b). A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272, 408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 31
    • 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
  • 32
    • 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
  • 33
    • 0029802540 scopus 로고    scopus 로고
    • The p55 subunit of Drosophila chromatin assembly factor 1 is homologous to a histone deacetylase-associated protein
    • Tyler, J.K., Bulger, M., Kamakaka, R.T., Koybayshi, R., and Kadonaga, J.K. (1996). The p55 subunit of Drosophila chromatin assembly factor 1 is homologous to a histone deacetylase-associated protein. Mol. Cell. Biol. 16, 6149-6159.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6149-6159
    • Tyler, J.K.1    Bulger, M.2    Kamakaka, R.T.3    Koybayshi, R.4    Kadonaga, J.K.5
  • 34
    • 0030272047 scopus 로고    scopus 로고
    • Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
    • Verreault, A., Kaufman, P.D., Kobayashi, R., and Stillman, B. (1996). Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 87, 95-104.
    • (1996) Cell , vol.87 , pp. 95-104
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 35
    • 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 Workman, J.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    Grant, P.A.2    Hebbes, T.R.3    Crane-Robinson, C.4    Allis, C.D.5    Workman, J.L.6
  • 36
    • 0026060619 scopus 로고
    • RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in saccharomyces cerevisiae
    • Vidal, M., and Gaber, R.F. (1991). RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol. Cell. Biol. 11, 6317-6327.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6317-6327
    • Vidal, M.1    Gaber, R.F.2
  • 37
    • 0025096058 scopus 로고
    • The saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs
    • Wang, H., Clark, I., Nicholson, P.R., Herskowitz, I., and Stillman, D.J. (1990). The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs. Mol. Cell. Biol. 10, 5927-5936.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5927-5936
    • Wang, H.1    Clark, I.2    Nicholson, P.R.3    Herskowitz, I.4    Stillman, D.J.5
  • 38
    • 0028589384 scopus 로고
    • Genetic interactions between SIN3 mutations and the saccharomyces cerevisiae transcriptional activators encoded by MCM1, STE12, and SWI1
    • Wang, H., Reynolds-Hager, L., and Stillman, D.J. (1994). Genetic interactions between SIN3 mutations and the Saccharomyces cerevisiae transcriptional activators encoded by MCM1, STE12, and SWI1. Mol. Gen. Genet. 245, 675-685.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 675-685
    • Wang, H.1    Reynolds-Hager, L.2    Stillman, D.J.3
  • 39
    • 0029869172 scopus 로고    scopus 로고
    • Histone deacetylase: A regulator of transcription
    • Wolffe, A.P. (1996). Histone deacetylase: a regulator of transcription. Science 272, 371-372.
    • (1996) Science , vol.272 , pp. 371-372
    • Wolffe, A.P.1
  • 40
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3
    • Yang, W.-M., Inouye, C., Zeng, Y., Bearss, D., and Seto, E. (1996a). Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3. Proc. Natl. Acad. Sci. USA 93, 12845-12850.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12845-12850
    • Yang, W.-M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 41
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang, X.J., Ogryzko, V.V., Nishikawa, J., Howard, B.H., and Nakatani, Y. (1996b). A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382, 319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 42
    • 0026685177 scopus 로고
    • The saccharomyces cerevisiae GAM2/SIN3 protein plays a role in both activation and repression of transcription
    • Yoshimoto, H., Ohmae, M., and Yamashita, I. (1992). The Saccharomyces cerevisiae GAM2/SIN3 protein plays a role in both activation and repression of transcription. Mol. Gen. Genet. 233, 327-330.
    • (1992) Mol. Gen. Genet. , vol.233 , pp. 327-330
    • Yoshimoto, H.1    Ohmae, M.2    Yamashita, I.3
  • 43
    • 0027511606 scopus 로고
    • Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
    • Zervos, A.S., Gyuris, J., and Brent, R. (1993). Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell 72, 223-232.
    • (1993) Cell , vol.72 , pp. 223-232
    • Zervos, A.S.1    Gyuris, J.2    Brent, R.3


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