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Volumn 387, Issue 6628, 1997, Pages 49-55

Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; TRANSCRIPTION FACTOR;

EID: 0030959244     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/387049a0     Document Type: Article
Times cited : (744)

References (50)
  • 1
    • 0029686266 scopus 로고    scopus 로고
    • Proteins of the Myc network: Essential regulators of cell growth and differentiation
    • Henriksson, M. & Luscher, B. Proteins of the Myc network: essential regulators of cell growth and differentiation. Adv. Cancer Res. 68, 109-182 (1996).
    • (1996) Adv. Cancer Res. , vol.68 , pp. 109-182
    • Henriksson, M.1    Luscher, B.2
  • 2
    • 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. & Eisenman, R. N. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell 80, 767-776 (1995).
    • (1995) Cell , vol.80 , pp. 767-776
    • Ayer, D.E.1    Lawrence, Q.A.2    Eisenman, R.N.3
  • 3
    • 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. et al. 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).
    • (1995) Cell , vol.80 , pp. 777-786
    • Schreiber-Agus, N.1
  • 4
    • 0029065748 scopus 로고
    • Repression of Myc-Ras cotransformation by Mad is mediated by multiple protein-protein interactions
    • Koskinen, P. J., Ayer, D. E. & Eisenman, R. N. Repression of Myc-Ras cotransformation by Mad is mediated by multiple protein-protein interactions. Cell Growth Differ. 6, 623-629 (1995).
    • (1995) Cell Growth Differ. , vol.6 , pp. 623-629
    • Koskinen, P.J.1    Ayer, D.E.2    Eisenman, R.N.3
  • 5
    • 9244234957 scopus 로고    scopus 로고
    • Mouse Sin3A interacts with and can functionally substitute for the amino-terminal repression domain of the Myc antagonist Mxi
    • Rao, G. et al. Mouse Sin3A interacts with and can functionally substitute for the amino-terminal repression domain of the Myc antagonist Mxi. Oncogene 12, 1165-1172 (1996).
    • (1996) Oncogene , vol.12 , pp. 1165-1172
    • Rao, G.1
  • 6
    • 0029737603 scopus 로고    scopus 로고
    • Sin3 corepressor function in Myc-induced transcription and transformation
    • Harper, S. E., Qiu, Y. & Sharp, P. A. Sin3 corepressor function in Myc-induced transcription and transformation. Proc. Natl Acad. Sci. USA 93, 8536-8540 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8536-8540
    • Harper, S.E.1    Qiu, Y.2    Sharp, P.A.3
  • 8
    • 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. & Stillman, D. J. The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs. Mol. Cell. Biol. 10, 5927-5936 (1990).
    • (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
  • 9
    • 0027479075 scopus 로고
    • Transcriptional repression in Saccharomyces cerevisiae by a SIN3-Lexa fusion protein
    • Wang, H. & Stillman, D. J. Transcriptional repression in Saccharomyces cerevisiae by a SIN3-LexA fusion protein. Mol. Cell. Biol. 13, 1805-1814 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1805-1814
    • Wang, H.1    Stillman, D.J.2
  • 10
    • 0026046959 scopus 로고
    • RPD1 (SIN3/UME4) is required for maximal activation and repression of diverse yeast genes
    • Vidal, M., Strich, R., Esposito, R. E. & Gaber, R. F. RPD1 (SIN3/UME4) is required for maximal activation and repression of diverse yeast genes. Mol. Cell. Biol. 11, 6306-6316 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6306-6316
    • Vidal, M.1    Strich, R.2    Esposito, R.E.3    Gaber, R.F.4
  • 11
    • 0026641776 scopus 로고
    • Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection
    • Winston, F. & Carlson, M. Yeast SNF/SWI transcriptional activators and the SPT/SIN chromatin connection. Trends Genet. 8, 387-391 (1992).
    • (1992) Trends Genet. , vol.8 , pp. 387-391
    • Winston, F.1    Carlson, M.2
  • 12
    • 0023666079 scopus 로고
    • Both positive and negative regulators of HO transcription are required for mother-cell-specific mating-type switching in yeast
    • Nasmyth, K., Stillman, D. J. & Kipling, D. Both positive and negative regulators of HO transcription are required for mother-cell-specific mating-type switching in yeast. Cell 48, 579-587 (1987).
    • (1987) Cell , vol.48 , pp. 579-587
    • Nasmyth, K.1    Stillman, D.J.2    Kipling, D.3
  • 13
    • 0026060619 scopus 로고
    • RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae
    • Vidal, M. & Gaber, R. F. RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol. Cell. Biol. 11, 6317-6327 (1991).
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6317-6327
    • Vidal, M.1    Gaber, R.F.2
  • 14
    • 0028297156 scopus 로고
    • Epistasis analysis of suppressor mutations that allow HO expression in the absence of the yeast SWI5 transcriptional activator
    • Stillman, D. J., Dorland, S. & Yu, Y. Epistasis analysis of suppressor mutations that allow HO expression in the absence of the yeast SWI5 transcriptional activator. Genetics 136, 781-788 (1994).
    • (1994) Genetics , vol.136 , pp. 781-788
    • Stillman, D.J.1    Dorland, S.2    Yu, Y.3
  • 15
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C. A. & Schreiber, S. L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272, 408-411 (1996).
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 16
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3
    • Yang, A.-M., Inouye, C., Zeng, Y., Bearss, D. & Seto, E. 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).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12845-12850
    • Yang, A.-M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 17
    • 0029869172 scopus 로고    scopus 로고
    • Histone deacetylase: A regulator of transcription
    • Wolffe, A. P. Histone deacetylase: a regulator of transcription. Science 272, 408-411 (1996).
    • (1996) Science , vol.272 , pp. 408-411
    • Wolffe, A.P.1
  • 19
    • 0029132202 scopus 로고
    • Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
    • Hörlein, A. J. et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 377, 397-404 (1995).
    • (1995) Nature , vol.377 , pp. 397-404
    • Hörlein, A.J.1
  • 20
    • 0029837730 scopus 로고    scopus 로고
    • A nuclear hormone receptor compressor mediates transcriptional silencing by receptors with distinct repression domains
    • Zamir, I. et al. A nuclear hormone receptor compressor mediates transcriptional silencing by receptors with distinct repression domains. Mol. Cell. Biol. 16, 5458-5465 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5458-5465
    • Zamir, I.1
  • 21
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/ threonine kinase Raf
    • Vojtek, A. B., Hollenberg, S. M. & Cooper, J. A. Mammalian Ras interacts directly with the serine/ threonine kinase Raf. Cell 74, 205-214 (1993).
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 22
    • 0026505554 scopus 로고
    • Chromatin structure of the yeast SUC2 promoter in regulatory mutants
    • Matallana, E., Franco, L. & Perez-Ortin, J. E. Chromatin structure of the yeast SUC2 promoter in regulatory mutants. Mol. Gen. Genet. 231, 395-400 (1992).
    • (1992) Mol. Gen. Genet. , vol.231 , pp. 395-400
    • Matallana, E.1    Franco, L.2    Perez-Ortin, J.E.3
  • 23
    • 0028264386 scopus 로고
    • The global transcriptional regulators, SSN6 and TUP1, play distinct roles in the establishment of a repressive chromatin structure
    • Cooper, J. P., Roth, S. Y. & Simpson, R. T. The global transcriptional regulators, SSN6 and TUP1, play distinct roles in the establishment of a repressive chromatin structure. Genes Dev. 8, 1400-1410 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 1400-1410
    • Cooper, J.P.1    Roth, S.Y.2    Simpson, R.T.3
  • 24
    • 0028340797 scopus 로고
    • Functional dissection of the yeast Cyc8-Tup1 transcriptional co-repressor complex
    • Tzamarias, D. & Struhl, K. Functional dissection of the yeast Cyc8-Tup1 transcriptional co-repressor complex. Nature 369, 758-761 (1994).
    • (1994) Nature , vol.369 , pp. 758-761
    • Tzamarias, D.1    Struhl, K.2
  • 25
    • 0028131434 scopus 로고
    • Transcriptional repression directed by the yeast alpha-2 protein in vitro
    • Herschbach, B. M., Arnaud, M. B. & Johnson, A. D. Transcriptional repression directed by the yeast alpha-2 protein in vitro. Nature 370, 309-311 (1994).
    • (1994) Nature , vol.370 , pp. 309-311
    • Herschbach, B.M.1    Arnaud, M.B.2    Johnson, A.D.3
  • 26
    • 0028860925 scopus 로고
    • A role for nucleosome assembly in both silencing and activation of the Xenopus TR beta a gene by the thyroid hormone receptor
    • Wong, J., Shi, Y. B. & Wolffe, A. P. A role for nucleosome assembly in both silencing and activation of the Xenopus TR beta A gene by the thyroid hormone receptor. Genes Dev. 9, 2696-2711 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 2696-2711
    • Wong, J.1    Shi, Y.B.2    Wolffe, A.P.3
  • 27
    • 0027493251 scopus 로고
    • BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription
    • Khavari, P. A., Peterson, C. L., Tamkun, J. W. & Crabtree, G. R. BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription. Nature 366, 170-174 (1993).
    • (1993) Nature , vol.366 , pp. 170-174
    • Khavari, P.A.1    Peterson, C.L.2    Tamkun, J.W.3    Crabtree, G.R.4
  • 28
    • 0027434083 scopus 로고
    • A human homologue of Saccharomyces cerevisiae SNF2/SW12 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor
    • Muchardt, C. & Yaniv, M. A human homologue of Saccharomyces cerevisiae SNF2/SW12 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor. EMBO J. 12, 4279-4290 (1993).
    • (1993) EMBO J. , vol.12 , pp. 4279-4290
    • Muchardt, C.1    Yaniv, M.2
  • 29
    • 0028239595 scopus 로고
    • Two human homologues of Saccharomyces cerevisiae SW12/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor
    • Chiba, H., Muramatsu, M., Nomoto, A. & Kato, H. Two human homologues of Saccharomyces cerevisiae SW12/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor. Nucleic Acids Res. 22, 1815-1820 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1815-1820
    • Chiba, H.1    Muramatsu, M.2    Nomoto, A.3    Kato, H.4
  • 30
    • 0028060515 scopus 로고
    • The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest
    • Dunaief, J. L. et al. The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest. Cell 79, 119-130 (1994).
    • (1994) Cell , vol.79 , pp. 119-130
    • Dunaief, J.L.1
  • 31
    • 0029995309 scopus 로고    scopus 로고
    • Functional interactions between the hBRM/hBRG1 transcriptional activators and the pRB family of proteins
    • Strober, B. E., Dunaief, J. L., Guha, S. & Goff, S. P. Functional interactions between the hBRM/hBRG1 transcriptional activators and the pRB family of proteins. Mol. Cell. Biol. 16, 1576-1583 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1576-1583
    • Strober, B.E.1    Dunaief, J.L.2    Guha, S.3    Goff, S.P.4
  • 32
    • 9544220768 scopus 로고    scopus 로고
    • The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein
    • Borrow, J. et al. The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein. Nature Genet. 14, 33-41 (1996).
    • (1996) Nature Genet. , vol.14 , pp. 33-41
    • Borrow, J.1
  • 33
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister, A. J. & Kouzarides, T. The CBP co-activator is a histone acetyltransferase. Nature 384, 641-643 (1996).
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 34
    • 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. & Nakatani, Y. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382, 319-324 (1996).
    • (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
  • 35
    • 0025727771 scopus 로고
    • Novel zinc finger gene implicated as myc collaborator by retrovirally accelerated lymphomagenesis in Eμ-myc transgenic mice
    • Haupt, Y., Alexander, W. S., Barri, G., Klinken, S. P. & Adams, J. M. Novel zinc finger gene implicated as myc collaborator by retrovirally accelerated lymphomagenesis in Eμ-myc transgenic mice. Cell 65, 753-763 (1991).
    • (1991) Cell , vol.65 , pp. 753-763
    • Haupt, Y.1    Alexander, W.S.2    Barri, G.3    Klinken, S.P.4    Adams, J.M.5
  • 36
    • 0025863346 scopus 로고
    • Identification of cooperating oncogenes in Eμ-myc transgenic mice by provirus tagging
    • van Lohuizen, M. et al. Identification of cooperating oncogenes in Eμ-myc transgenic mice by provirus tagging. Cell 65, 737-752 (1991).
    • (1991) Cell , vol.65 , pp. 737-752
    • Van Lohuizen, M.1
  • 37
    • 0025773264 scopus 로고
    • Sequence similarity between the mammalian bmi-1 proto-oncogene and the Drosophila regulatory genes Psc and Su(z)2
    • van Lohuizen, M., Frasch, M., Wientjens, E. & Berns, A. Sequence similarity between the mammalian bmi-1 proto-oncogene and the Drosophila regulatory genes Psc and Su(z)2. Nature 353, 353-355 (1991).
    • (1991) Nature , vol.353 , pp. 353-355
    • Van Lohuizen, M.1    Frasch, M.2    Wientjens, E.3    Berns, A.4
  • 38
    • 0026642195 scopus 로고
    • Induction of apoptosis in fibroblasts by c-myc protein
    • Evan, G. I. et al. Induction of apoptosis in fibroblasts by c-myc protein. Cell 69, 119-128 (1992).
    • (1992) Cell , vol.69 , pp. 119-128
    • Evan, G.I.1
  • 39
    • 0027425699 scopus 로고
    • Direct role for Myc in transcription initiation mediated by interactions with TFII-I
    • Roy, A. L., Carruthers, C., Gutjahr, T. & Roder, R. G. Direct role for Myc in transcription initiation mediated by interactions with TFII-I. Nature 365, 359-361 (1993).
    • (1993) Nature , vol.365 , pp. 359-361
    • Roy, A.L.1    Carruthers, C.2    Gutjahr, T.3    Roder, R.G.4
  • 40
    • 0028169192 scopus 로고
    • C-Myc represses transcription in vivo by a novel mechanism dependent on the initiator element and Myc box II
    • Li, L. H., Nerlov, C., Prendergast, G., MacGregor, D. & Ziff, E. B. c-Myc represses transcription in vivo by a novel mechanism dependent on the initiator element and Myc box II. EMBO J. 13, 4070-4079 (1994).
    • (1994) EMBO J. , vol.13 , pp. 4070-4079
    • Li, L.H.1    Nerlov, C.2    Prendergast, G.3    MacGregor, D.4    Ziff, E.B.5
  • 41
    • 0029912395 scopus 로고    scopus 로고
    • A link between c-Myc-mediated transcriptional repression and neoplastic transformation
    • Lee, L. A., Dolde, C., Barret, J., Wu, C. S. & Dang, C. V. A link between c-Myc-mediated transcriptional repression and neoplastic transformation. J. Clin. Invest. 97, 1687-1695 (1996).
    • (1996) J. Clin. Invest. , vol.97 , pp. 1687-1695
    • Lee, L.A.1    Dolde, C.2    Barret, J.3    Wu, C.S.4    Dang, C.V.5
  • 42
    • 0029779280 scopus 로고    scopus 로고
    • Cdc25 cell-cycle phosphatase as a target of c-myc
    • Galaktionov, K., Chen, X. & Beach, D. Cdc25 cell-cycle phosphatase as a target of c-myc. Nature 382, 511-517 (1996).
    • (1996) Nature , vol.382 , pp. 511-517
    • Galaktionov, K.1    Chen, X.2    Beach, D.3
  • 43
    • 0029997378 scopus 로고    scopus 로고
    • Targeting chromatin disruption: Transcription regulators that acetylate histones
    • Wolffe, A. P. & Prusse, D. Targeting chromatin disruption: transcription regulators that acetylate histones. Cell 84, 817-819 (1996).
    • (1996) Cell , vol.84 , pp. 817-819
    • Wolffe, A.P.1    Prusse, D.2
  • 44
    • 0029925512 scopus 로고    scopus 로고
    • Special HATs for special occasions: Linking histone acetylation to chromatin assembly and gene activation
    • Brownell, J. E. & Allis, C. D. Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation. Curr. Opin. Genet Dev. 6, 176-184 (1996).
    • (1996) Curr. Opin. Genet Dev. , vol.6 , pp. 176-184
    • Brownell, J.E.1    Allis, C.D.2
  • 45
    • 0027192267 scopus 로고
    • Transcriptional silencing in yeast is associated with reduced nucleosome acetylation
    • Braunstein, M., Rose, A. B., Holmes, S. G., Allis, C. D. & Broach, J. R. Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev. 7, 592-604 (1993).
    • (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
  • 46
    • 0029856225 scopus 로고    scopus 로고
    • HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription
    • Rundlett, S. E. et al. 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).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14503-14508
    • Rundlett, S.E.1
  • 47
    • 0029805633 scopus 로고    scopus 로고
    • The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast
    • De Rubertis, F. et al. The histone deacetylase RPD3 counteracts genomic silencing in Drosophila and yeast. Nature 384, 589-591 (1996).
    • (1996) Nature , vol.384 , pp. 589-591
    • De Rubertis, F.1
  • 48
    • 0025953899 scopus 로고
    • Myc family oncogenes in the development of normal and neoplastic cells
    • DePinho, R. A., Schreiber-Agus, N. & Alt, F. W. Myc family oncogenes in the development of normal and neoplastic cells. Adv. Cancer Res. 57, 1-46 (1991).
    • (1991) Adv. Cancer Res. , vol.57 , pp. 1-46
    • DePinho, R.A.1    Schreiber-Agus, N.2    Alt, F.W.3
  • 49
    • 0027408096 scopus 로고
    • Mad: A heterodimeric partner of Max that antagonizes Myc transcriptional activity
    • Ayer, D. E., Kretzner, L. & Eisenman, R. N. Mad: a heterodimeric partner of Max that antagonizes Myc transcriptional activity. Cell 72, 211-222 (1993).
    • (1993) Cell , vol.72 , pp. 211-222
    • Ayer, D.E.1    Kretzner, L.2    Eisenman, R.N.3
  • 50
    • 0028089283 scopus 로고
    • Adenovirus E1B oncoprotein tethers a transcriptional repression domain to p53
    • Yew, P. R., Liu, X. & Berk, A. J. Adenovirus E1B oncoprotein tethers a transcriptional repression domain to p53. Genes Dev. 8, 190-202 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 190-202
    • Yew, P.R.1    Liu, X.2    Berk, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.