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Volumn 19, Issue 9, 1999, Pages 5847-5860

Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4 connection in the Xenopus oocyte

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; HISTONE DEACETYLASE;

EID: 0032812342     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.19.9.5847     Document Type: Article
Times cited : (65)

References (87)
  • 1
    • 0030959244 scopus 로고    scopus 로고
    • Role of NCoR and histone deacetylase in Sin3-mediated transcriptional and oncogenic repression
    • Alland, L., R. Muhle, H. Hou, Jr., J. Potes, L. Chin, N. Schreiber-Agus, and R. A. De Pinho. 1997. Role of NCoR and histone deacetylase in Sin3-mediated transcriptional and oncogenic repression. Nature 387:49-55.
    • (1997) Nature , vol.387 , pp. 49-55
    • Alland, L.1    Muhle, R.2    Hou H., Jr.3    Potes, J.4    Chin, L.5    Schreiber-Agus, N.6    De Pinho, R.A.7
  • 2
    • 0027385167 scopus 로고
    • Replication-coupled chromatin assembly is required for the repression of basal transcription in vivo
    • Almouzni, G., and A. P. Wolffe. 1993. Replication-coupled chromatin assembly is required for the repression of basal transcription in vivo. Genes Dev. 7:2033-2047.
    • (1993) Genes Dev. , vol.7 , pp. 2033-2047
    • Almouzni, G.1    Wolffe, A.P.2
  • 3
    • 0027258499 scopus 로고
    • Nuclear assembly, structure, and function: The use of Xenopus in vitro systems
    • Almouzni, G., and A. P. Wolffe. 1993. Nuclear assembly, structure, and function: the use of Xenopus in vitro systems. Exp. Cell Res. 205:1-15.
    • (1993) Exp. Cell Res. , vol.205 , pp. 1-15
    • Almouzni, G.1    Wolffe, A.P.2
  • 4
    • 0343768774 scopus 로고
    • Assembly of spaced chromatin by DNA synthesis in extracts from Xenopus eggs
    • Almouzni, G., and M. Mechali. 1988. Assembly of spaced chromatin by DNA synthesis in extracts from Xenopus eggs. EMBO J. 7:664-672.
    • (1988) EMBO J. , vol.7 , pp. 664-672
    • Almouzni, G.1    Mechali, M.2
  • 5
    • 0002216824 scopus 로고
    • Histone acetylation during chromatin replication and nucleosome assembly
    • 4a. Annunziato, A. T. 1995. Histone acetylation during chromatin replication and nucleosome assembly. Nucleus 1:31-58.
    • (1995) Nucleus , vol.1 , pp. 31-58
    • Annunziato, A.T.1
  • 6
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1Å resolution: A tripartite protein assembly and a left-handed superhelix
    • Arents, G., R. W. Burlingame, B. W. Wang, W. E. Love, and E. N. Moudrianakis. 1991. The nucleosomal core histone octamer at 3.1Å resolution: a tripartite protein assembly and a left-handed superhelix. Proc. Natl. Acad. Sci. USA 88:10148-10152.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.W.3    Love, W.E.4    Moudrianakis, E.N.5
  • 7
    • 0028905563 scopus 로고
    • Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3
    • Ayer, D. E., Q. A. Lawrence, and R. N. Eisenman. 1995. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell 80:767-776.
    • (1995) Cell , vol.80 , pp. 767-776
    • Ayer, D.E.1    Lawrence, Q.A.2    Eisenman, R.N.3
  • 9
    • 0027431276 scopus 로고
    • A switch from Myc-Max to Mad-Max accompanies monocyte/macrophage differentiation
    • Ayer, D. E., and R. N. Eisenman. 1993. A switch from Myc-Max to Mad-Max 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
  • 10
    • 0032484989 scopus 로고    scopus 로고
    • Retinoblastoma protein recruits histone deacetylase to repress transcription
    • Brehm, A., E. A. Miska, D. J. McCance, J. L. Reid, A. J. Bannister, and T. Kouzarides. 1998. Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature 391:601-605.
    • (1998) Nature , vol.391 , pp. 601-605
    • Brehm, A.1    Miska, E.A.2    McCance, D.J.3    Reid, J.L.4    Bannister, A.J.5    Kouzarides, T.6
  • 11
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell, J. E., J. Zhou, T. Ranalli, R. Kobayashi, D. G. Edmondson, S. Y. Roth, and C. D. Allis. 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    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 12
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen, H., R. J. Lin, R. L. Schlitz, D. Chakravarti, A. Nash, L. Nagy, M. L. Privalsky, Y. Nakatani, and R. M. Evans. 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90:569-580.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schlitz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 13
    • 0029077733 scopus 로고
    • Effects of the MYC oncogene antagonist, MAD on proliferation, cell cycling and the malignant phenotype of human brain tumor cells
    • Chen, J., T. Willingham, L. R. Margraf, N. Schreiber-Agus, R. A. De Pinho, and P. D. Nisen. 1995. Effects of the MYC oncogene antagonist, MAD on proliferation, cell cycling and the malignant phenotype of human brain tumor cells. Nat. Med. 1:638-643.
    • (1995) Nat. Med. , vol.1 , pp. 638-643
    • Chen, J.1    Willingham, T.2    Margraf, L.R.3    Schreiber-Agus, N.4    De Pinho, R.A.5    Nisen, P.D.6
  • 15
    • 0029856861 scopus 로고    scopus 로고
    • Remodeling somatic nuclei in Xenopus laevis egg extracts: Molecular mechanisms for the selective release of histone H1 and H1° from chromatin and the acquisition of transcriptional competence
    • Dimitrov, S., and A. P. Wolffe. 1996. Remodeling somatic nuclei in Xenopus laevis egg extracts: molecular mechanisms for the selective release of histone H1 and H1° from chromatin and the acquisition of transcriptional competence. EMBO J. 15:5897-5906.
    • (1996) EMBO J. , vol.15 , pp. 5897-5906
    • Dimitrov, S.1    Wolffe, A.P.2
  • 16
    • 0028296414 scopus 로고
    • Molecular cloning and functional analysis of the adenovirus E1A-associated 300-KD protein (p300) reveals a protein with properties of a transcriptional adaptor
    • Eckner, R., M. E. Ewen, D. Newsome, M. Gerdes, J. A. DeCaprio, J. B. Lawrence, and D. M. Livington. 1994. Molecular cloning and functional analysis of the adenovirus E1A-associated 300-KD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 7:869-884.
    • (1994) Genes Dev. , vol.7 , pp. 869-884
    • Eckner, R.1    Ewen, M.E.2    Newsome, D.3    Gerdes, M.4    Decaprio, J.A.5    Lawrence, J.B.6    Livington, D.M.7
  • 17
    • 0029850314 scopus 로고    scopus 로고
    • Functional assays for assembly of histones H3 and H4 into the chromatin of Xenopus embryos
    • Freeman, L., H. Kurumizaka, and A. P. Wolffe. 1996. Functional assays for assembly of histones H3 and H4 into the chromatin of Xenopus embryos. Proc. Natl. Acad. Sci. USA 93:12780-12785.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12780-12785
    • Freeman, L.1    Kurumizaka, H.2    Wolffe, A.P.3
  • 19
    • 0026783834 scopus 로고
    • Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription
    • Georgakopoulos, T., and G. Thireos. 1992. Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription. EMBO J. 11:4145-4152.
    • (1992) EMBO J. , vol.11 , pp. 4145-4152
    • Georgakopoulos, T.1    Thireos, G.2
  • 20
    • 0030741529 scopus 로고    scopus 로고
    • Role of histone tails in nucleosome remodeling by Drosophila NURF
    • Georgel, P. T., T. Tsukiyama, and C. Wu. 1997. Role of histone tails in nucleosome remodeling by Drosophila NURF. EMBO J. 16:4717-4726.
    • (1997) EMBO J. , vol.16 , pp. 4717-4726
    • Georgel, P.T.1    Tsukiyama, T.2    Wu, C.3
  • 21
    • 0344193100 scopus 로고    scopus 로고
    • Life with nucleosomes: Chromatin remodelling in gene regulation
    • Gregory, P. D., and W. Horz. 1998. Life with nucleosomes: chromatin remodelling in gene regulation. Curr. Opin. Cell Biol. 10:339-345.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 339-345
    • Gregory, P.D.1    Horz, W.2
  • 22
    • 0031007189 scopus 로고    scopus 로고
    • Histone deacetylase activity is required for full transcriptional repression by mSin 3A
    • Hassig, C. A., T. C. Fleischer, A. N. Billin, S. L. Schreiber, and D. E. Ayer. 1997. Histone deacetylase activity is required for full transcriptional repression by mSin 3A. Cell 89:341-347.
    • (1997) Cell , vol.89 , pp. 341-347
    • Hassig, C.A.1    Fleischer, T.C.2    Billin, A.N.3    Schreiber, S.L.4    Ayer, D.E.5
  • 25
    • 0030584819 scopus 로고    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., C. Queva, P. J. Koskinen, E. Steingrimsson, D. E. Ayer, N. G. Copeland, N. A. Jenkins, and R. N. Eisenman. 1996. Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation. EMBO J. 15:2030-2040.
    • (1996) EMBO J. , vol.15 , pp. 2030-2040
    • 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
  • 26
    • 0344769145 scopus 로고    scopus 로고
    • Unpublished data
    • 24a. Imhof, A. Unpublished data.
    • Imhof, A.1
  • 28
    • 0032520953 scopus 로고    scopus 로고
    • Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo
    • Kadosh, D., and K. Struhl. 1998. Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo. Genes Dev. 12:797-805.
    • (1998) Genes Dev. , vol.12 , pp. 797-805
    • Kadosh, D.1    Struhl, K.2
  • 29
    • 0030042971 scopus 로고    scopus 로고
    • Postreplicative chromatin assembly by Drosophila and human chromatin assembly factor I
    • Kamakaka, R. T., M. Bulger, P. D. Kaufman, B. Stillman, and J. T. Kadonaga. 1996. Postreplicative chromatin assembly by Drosophila and human chromatin assembly factor I. Mol. Cell. Biol. 16:810-817.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 810-817
    • Kamakaka, R.T.1    Bulger, M.2    Kaufman, P.D.3    Stillman, B.4    Kadonaga, J.T.5
  • 31
    • 0030716393 scopus 로고    scopus 로고
    • Identification of the Saccharomyces cerevisiae STB1-STB5 encoding Sin3p binding proteins
    • Kasten, M. M., and D. J. Stillman. 1997. Identification of the Saccharomyces cerevisiae STB1-STB5 encoding Sin3p binding proteins. Mol. Gen. Genet. 256:376-386.
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 376-386
    • Kasten, M.M.1    Stillman, D.J.2
  • 32
    • 0030877160 scopus 로고    scopus 로고
    • A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators
    • Kasten, M. M., S. Dorland, and D. J. Stillman. 1997. A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators. Mol. Cell. Biol. 17:4852-4858.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4852-4858
    • Kasten, M.M.1    Dorland, S.2    Stillman, D.J.3
  • 33
    • 0029982704 scopus 로고    scopus 로고
    • SIN3 dependent transcriptional repression by interaction with the Mad1 DNA binding protein
    • Kasten, M. M., D. E. Ayer, and D. J. Stillman. 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
  • 34
    • 0031043134 scopus 로고    scopus 로고
    • Ultraviolet radiation sensitivity and reduction of telomeric silencing in Saccharomyces cerevisiae cells lacking chromatin assembly factor-1
    • Kaufman, P. D., R. Kobayashi, and B. Stillman. 1997. Ultraviolet radiation sensitivity and reduction of telomeric silencing in Saccharomyces cerevisiae cells lacking chromatin assembly factor-1. Genes Dev. 11:345-357.
    • (1997) Genes Dev. , vol.11 , pp. 345-357
    • Kaufman, P.D.1    Kobayashi, R.2    Stillman, B.3
  • 35
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylase associated with the mSin3 corepressor mediate Mad transcriptional repression
    • Laherty, C. D., W. M. Yang, J. M. Sun, J. R. Davie, E. Seto, and R. M. Eisenman. 1997. Histone deacetylase associated with the mSin3 corepressor mediate Mad transcriptional repression. Cell 89:349-356.
    • (1997) Cell , vol.89 , pp. 349-356
    • Laherty, C.D.1    Yang, W.M.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5    Eisenman, R.M.6
  • 37
    • 0028157947 scopus 로고
    • Nucleosome-mediated disruption of transcription factor-chromatin initiation complexes at the mouse mammary tumor virus long terminal repeat in vitro
    • Lee, H. H., and T. K. Archer. 1994. Nucleosome-mediated disruption of transcription factor-chromatin initiation complexes at the mouse mammary tumor virus long terminal repeat in vitro. Mol. Cell. Biol. 14:32-41.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 32-41
    • Lee, H.H.1    Archer, T.K.2
  • 38
    • 0030812917 scopus 로고    scopus 로고
    • Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily
    • Leipe, D. D., and D. Landsman. 1997. Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily. Nucleic Acids Res. 25:3693-3697.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3693-3697
    • Leipe, D.D.1    Landsman, D.2
  • 39
    • 0032476596 scopus 로고    scopus 로고
    • Xenopus NF-Y presents chromatin to potentiate p300 and acetylation responsive transcription from the Xenopus hsp70 promoter in vivo
    • Li, Q., M. Herrler, N. Landsberger, N. Kaludov, V. V. Ogryzyko, Y. Nakatani, and A. P. Wolffe. 1998. Xenopus NF-Y presents chromatin to potentiate p300 and acetylation responsive transcription from the Xenopus hsp70 promoter in vivo. EMBO J. 17:6300-6315.
    • (1998) EMBO J. , vol.17 , pp. 6300-6315
    • Li, Q.1    Herrler, M.2    Landsberger, N.3    Kaludov, N.4    Ogryzyko, V.V.5    Nakatani, Y.6    Wolffe, A.P.7
  • 40
    • 0031587289 scopus 로고    scopus 로고
    • Characterization of nucleosome core particles containing histone proteins made in bacteria
    • Luger, K., T. J. Rechsteiner, A. J. Flaus, M. M. Y. Wayne, and T. J. Richmond. 1997. Characterization of nucleosome core particles containing histone proteins made in bacteria. J. Mol. Biol. 272:301-311.
    • (1997) J. Mol. Biol. , vol.272 , pp. 301-311
    • Luger, K.1    Rechsteiner, T.J.2    Flaus, A.J.3    Wayne, M.M.Y.4    Richmond, T.J.5
  • 41
    • 1842411320 scopus 로고    scopus 로고
    • X-ray structure of the nucleosome core particle at 2.8Å resolution
    • Luger, K., A. W. Mader, R. K. Richmond, D. F. Sargent, and T. J. Richmond. 1997. X-ray structure of the nucleosome core particle at 2.8Å resolution. Nature 389:251-259.
    • (1997) Nature , vol.389 , pp. 251-259
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 42
    • 0030771898 scopus 로고    scopus 로고
    • Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein
    • Lusser, A., G. Brosch, A. Loidl, H. Haas, and P. Loidl. 1997. Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein. Science 277:88-91.
    • (1997) Science , vol.277 , pp. 88-91
    • Lusser, A.1    Brosch, G.2    Loidl, A.3    Haas, H.4    Loidl, P.5
  • 45
    • 0031964479 scopus 로고    scopus 로고
    • Linking histone acetylation to transcriptional regulation
    • Mizzen, C. A., and C. D. Allis. 1998. Linking histone acetylation to transcriptional regulation. Cell. Mol. Life Sci. 54:6-20.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 6-20
    • Mizzen, C.A.1    Allis, C.D.2
  • 46
    • 0030953186 scopus 로고    scopus 로고
    • Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
    • Nagy, L., H. Y. Kao, D. Chakravarti, R. J. Lin, C. A. Hassig, D. E. Ayer, S. L. Schreiber, and R. M. Evans. 1997. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 89: 373-380.
    • (1997) Cell , vol.89 , pp. 373-380
    • Nagy, L.1    Kao, H.Y.2    Chakravarti, D.3    Lin, R.J.4    Hassig, C.A.5    Ayer, D.E.6    Schreiber, S.L.7    Evans, R.M.8
  • 47
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan, X., H. H. Ng, C. A. Johnson, C. D. Laherty, B. M. Turner, R. N. Eisenman, and A. Bird. 1998. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature 393: 386-389.
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1    Ng, H.H.2    Johnson, C.A.3    Laherty, C.D.4    Turner, B.M.5    Eisenman, R.N.6    Bird, A.7
  • 48
    • 0030954208 scopus 로고    scopus 로고
    • GCN5-related histone N-acetyl-transferases belong to a superfamily that includes the yeast SPT10 protein
    • Neuwald, A. F., and D. Landsman. 1997. GCN5-related histone N-acetyl-transferases belong to a superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 22:154-155.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 49
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V. V., R. L. Schiltz, V. Russanova, B. H. Howard, and Y. Nakatani. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. 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
  • 50
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate, S. A., S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley. 1995. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354-1357.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.-J.3    O'Malley, B.W.4
  • 51
    • 0030271392 scopus 로고    scopus 로고
    • The major cytoplasmic histone acetyltransferase in yeast: Links to chromatin assembly and histone metabolism
    • Parthun, M. R., J. Widom, and D. E. Gottschling. 1996. The major cytoplasmic histone acetyltransferase in yeast: links to chromatin assembly and histone metabolism. Cell 87:85-94.
    • (1996) Cell , vol.87 , pp. 85-94
    • Parthun, M.R.1    Widom, J.2    Gottschling, D.E.3
  • 52
    • 0031730382 scopus 로고    scopus 로고
    • The Drosophila SIN3 gene encodes a widely distributed transcription factor essential for embryonic viability
    • Pennetta, G., and D. Pauli. 1998. The Drosophila SIN3 gene encodes a widely distributed transcription factor essential for embryonic viability. Dev. Genes Evol. 208:531-536.
    • (1998) Dev. Genes Evol. , vol.208 , pp. 531-536
    • Pennetta, G.1    Pauli, D.2
  • 53
    • 0027320814 scopus 로고
    • A retinoblastoma-binding protein related to a negative regulator of Ras in yeast
    • Qian, Y. W., Y.-C. J. Wang, R. E. J. Hollingsworth, D. Jones, N. Ling, and E. Y.-H. P. Lee. 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.J.2    Hollingsworth, R.E.J.3    Jones, D.4    Ling, N.5    Lee, E.Y.-H.P.6
  • 54
    • 0028856782 scopus 로고
    • Dual retinoblastoma-binding proteins with properties related to a negative regulator of Ras in yeast
    • Qian, Y. W., and E. Y.-H. P. Lee. 1995. Dual retinoblastoma-binding proteins with properties related to a negative regulator of Ras in yeast. J. Biol. Chem. 270:25507-25513.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25507-25513
    • Qian, Y.W.1    Lee, E.Y.-H.P.2
  • 56
  • 57
    • 0029856225 scopus 로고    scopus 로고
    • HDA1 and RPD3 are members of distinct histone deacetylase complexes that regulate silencing and transcription
    • Rundlett, S. E., A. A. Carmen, R. Kobayashi, S. Bavykin, B. M. Turner, and M. Grunstein. 1996. HDA1 and RPD3 are members of distinct 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
  • 59
    • 0024384868 scopus 로고
    • The assembly of regularly spaced nucleosomes in the Xenopus oocyte S150 extract is accompanied by deacetylation of histone H4
    • 56a. Shimamura, A., and A. Worcel. 1989. The assembly of regularly spaced nucleosomes in the Xenopus oocyte S150 extract is accompanied by deacetylation of histone H4. J. Biol. Chem. 264:14524-14530.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14524-14530
    • Shimamura, A.1    Worcel, A.2
  • 60
    • 0024372060 scopus 로고
    • Purification and characterization of CAF1, a human cell factor required for chromatin assembly during DNA replication in vitro
    • Smith, S., and B. W. Stillman. 1989. Purification and characterization of CAF1, a human cell factor required for chromatin assembly during DNA replication in vitro. Cell 58:15-25.
    • (1989) Cell , vol.58 , pp. 15-25
    • Smith, S.1    Stillman, B.W.2
  • 61
    • 0031172243 scopus 로고    scopus 로고
    • Cell growth inhibition by the Mad/Max complex through recruitment of histone deacetylase activity
    • Sommer, A., S. Hilfenhaus, A. Menkel, E. Kremmer, C. Siser, P. Loidl, and B. Luscher. 1997. Cell growth inhibition by the Mad/Max complex through recruitment of histone deacetylase activity. Curr. Biol. 7:357-365.
    • (1997) Curr. Biol. , vol.7 , pp. 357-365
    • Sommer, A.1    Hilfenhaus, S.2    Menkel, A.3    Kremmer, E.4    Siser, C.5    Loidl, P.6    Luscher, B.7
  • 62
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G-protein β γ dimer at 2.1A resolution
    • Erratum, 379:847
    • Sondek, J., A. Bohm, D. G. Lambright, H. E. Hamm, and P. B. Sigler. 1996. Crystal structure of a G-protein β γ dimer at 2.1A resolution. Nature 379: 369-374. (Erratum, 379:847.)
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 64
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to a yeast transcriptional regulator Rpd3
    • Taunton, J., C. A. Hassig, and S. L. Schreiber. 1996. A mammalian histone deacetylase related to a yeast transcriptional regulator Rpd3. Science 272: 408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 65
    • 0032578762 scopus 로고    scopus 로고
    • Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex
    • Tong, J. K., C. A. Hassig, G. R. Schnitzer, R. E. Kingston, and S. L. Schreiber. 1998. Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. Nature 395:917-921.
    • (1998) Nature , vol.395 , pp. 917-921
    • Tong, J.K.1    Hassig, C.A.2    Schnitzer, G.R.3    Kingston, R.E.4    Schreiber, S.L.5
  • 66
    • 0031835267 scopus 로고    scopus 로고
    • Coactivators and core-pressors in the integration of transcriptional responses
    • Torchia, J., C. Glass, and M. G. Rosenfeld. 1998. Coactivators and core-pressors in the integration of transcriptional responses. Curr. Opin. Cell Biol. 10:373-383.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 373-383
    • Torchia, J.1    Glass, C.2    Rosenfeld, M.G.3
  • 67
    • 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., M. Bulger, R. T. Kamakaka, R. Kobayashi, and J. T. Kadonaga. 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    Kobayashi, R.4    Kadonaga, J.T.5
  • 68
    • 0030998534 scopus 로고    scopus 로고
    • Histone acetylation: Influence on transcription nucleosome mobility and positioning and linker histone-dependent transcriptional repression
    • 64a. Ura, K., H. Kurumizaka, S. Dimitrov, G. Almouzni, and A. P. Wolffe. 1997. Histone acetylation: influence on transcription nucleosome mobility and positioning and linker histone-dependent transcriptional repression. EMBO J. 16:2096-2107.
    • (1997) EMBO J. , vol.16 , pp. 2096-2107
    • Ura, K.1    Kurumizaka, H.2    Dimitrov, S.3    Almouzni, G.4    Wolffe, A.P.5
  • 69
    • 0033593347 scopus 로고    scopus 로고
    • Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers
    • Verdel, A., and S. Khochbin. 1999. Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers. J. Biol. Chem. 274:2440-2445.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2440-2445
    • Verdel, A.1    Khochbin, S.2
  • 71
    • 0030272047 scopus 로고    scopus 로고
    • Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
    • Verreault, A., P. D. Kaufman, R. Kobayashi, and B. Stillman. 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
  • 72
    • 0032518442 scopus 로고    scopus 로고
    • Nucleosomal DNA regulates the core-histone binding subunit of the human hat1 acetyltransferase
    • Verreault, A., P. D. Kaufman, R. Kobayashi, and B. Stillman. 1998. Nucleosomal DNA regulates the core-histone binding subunit of the human hat1 acetyltransferase. Curr. Biol. 8:96-108.
    • (1998) Curr. Biol. , vol.8 , pp. 96-108
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3    Stillman, B.4
  • 73
    • 0026060619 scopus 로고
    • RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae
    • Vidal, M., and R. F. Gaber. 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
  • 74
    • 0026046959 scopus 로고
    • RPD1 (S1N3/ UME4) is required for maximal activation and repression of diverse yeast genes
    • Vidal, M., R. Strich, R. E. Esposito, and R. F. Gaber. 1991. RPD1 (S1N3/ UME4) is required for maximal activation and repression of diverse yeast genes. Mol. Cell. Biol. 11:6306-6316.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6306-6316
    • Vidal, M.1    Strich, R.2    Esposito, R.E.3    Gaber, R.F.4
  • 75
    • 0032474826 scopus 로고    scopus 로고
    • The multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase
    • Wade, P. A., P. L. Jones, D. Vermaak, and A. P. Wolffe. 1998. The multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase. Curr. Biol. 8:843-846.
    • (1998) Curr. Biol. , vol.8 , pp. 843-846
    • Wade, P.A.1    Jones, P.L.2    Vermaak, D.3    Wolffe, A.P.4
  • 76
    • 0030940298 scopus 로고    scopus 로고
    • Histone acetylation: Chromatin in action
    • 70a. Wade, P. A., D. Pruss, and A. P. Wolffe. 1997. Histone acetylation: chromatin in action. Trends Biochem. Sci. 22:128-132.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 128-132
    • Wade, P.A.1    Pruss, D.2    Wolffe, A.P.3
  • 78
    • 0025661965 scopus 로고
    • In vitro regulation of a SIN3-dependent DNA-binding activity by stimulatory and inhibitory factors
    • Wang, H., and D. J. Stillman. 1990. In vitro regulation of a SIN3-dependent DNA-binding activity by stimulatory and inhibitory factors. Proc. Natl. Acad. Sci. USA 87:9761-9765.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9761-9765
    • Wang, H.1    Stillman, D.J.2
  • 79
    • 0027479075 scopus 로고
    • Transcriptional repression in Saccharomyces cerevisiae by a SIN3-Lexa fusion protein
    • Wang, H., and D. J. Stillman. 1993. Transcriptional repression in Saccharomyces cerevisiae by a SIN3-LexA fusion protein. Mol. Cell. Biol. 13:1805-1814.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1805-1814
    • Wang, H.1    Stillman, D.J.2
  • 80
    • 0025096058 scopus 로고
    • The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs
    • Wang, H., I. Clark, P. R. Nicholson, I. Herskowitz, and D. J. Stillman. 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
  • 81
    • 0032518799 scopus 로고    scopus 로고
    • Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase
    • Wong, J., D. Patterton, A. Imhof, Y.-B. Shi, and A. P. Wolffe. 1998. Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase. EMBO J. 17:520-534.
    • (1998) EMBO J. , vol.17 , pp. 520-534
    • Wong, J.1    Patterton, D.2    Imhof, A.3    Shi, Y.-B.4    Wolffe, A.P.5
  • 82
    • 0029128377 scopus 로고
    • Coordinated regulation of and transcriptional activation by Xenopus thyroid hormone and retinoid X receptors
    • Wong, J., and Y. B. Shi. 1995. Coordinated regulation of and transcriptional activation by Xenopus thyroid hormone and retinoid X receptors. J. Biol. Chem. 270:18479-18483.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18479-18483
    • Wong, J.1    Shi, Y.B.2
  • 83
    • 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., C. Inouye, Y. Zeng, D. Bearss, and E. Soto. 1996. 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    Soto, E.5
  • 84
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral E1A oncoprotein
    • Yang, X.-J., V. V. Ogryzko, J.-I. Nishikawa, B. Howard, and Y. Nakatani. 1996. A p300/CBP-associated factor that competes with the adenoviral E1A oncoprotein. Nature 382:319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.-J.1    Ogryzko, V.V.2    Nishikawa, J.-I.3    Howard, B.4    Nakatani, Y.5
  • 85
    • 0030916729 scopus 로고    scopus 로고
    • Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
    • Zhang, Y., R. Iratni, H. Erdjument-Bromage, P. Tempst, and O. Reinberg. 1997. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell 89:357-364.
    • (1997) Cell , vol.89 , pp. 357-364
    • Zhang, Y.1    Iratni, R.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, O.5
  • 86
    • 0032538293 scopus 로고    scopus 로고
    • The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities
    • Zhang, Y., G. LeRoy, H. P. Seelig, W. S. Lane, and D. Reinberg. 1998. The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell 95: 279-289.
    • (1998) Cell , vol.95 , pp. 279-289
    • Zhang, Y.1    Leroy, G.2    Seelig, H.P.3    Lane, W.S.4    Reinberg, D.5
  • 87
    • 0032088533 scopus 로고    scopus 로고
    • SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex
    • Zhang, Y., Z.-W. Sun, R. Iratni, H. Erdjument-Bromage, P. Tempst, M. Hampsey, and D. Reinberg. 1998. SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex. Mol. Cell 1:1021-1031.
    • (1998) Mol. Cell , vol.1 , pp. 1021-1031
    • Zhang, Y.1    Sun, Z.-W.2    Iratni, R.3    Erdjument-Bromage, H.4    Tempst, P.5    Hampsey, M.6    Reinberg, D.7


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