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Volumn 9, Issue 5, 1999, Pages 499-504

Nuclear receptor cofactors as chromatin remodelers

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELL NUCLEUS RECEPTOR; HISTONE;

EID: 0032871893     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(99)00010-6     Document Type: Review
Times cited : (90)

References (61)
  • 1
  • 2
    • 0024280881 scopus 로고
    • Extremely conserved histone H4 N terminus is dispenable for growth but essential for repressing the silent mating loci in yeast
    • Kayne PS, Kim U, Han M, Mullen JR, Yoshizaki F, Grunstein M Extremely conserved histone H4 N terminus is dispenable for growth but essential for repressing the silent mating loci in yeast. Cell. 55:1988;27-39.
    • (1988) Cell , vol.55 , pp. 27-39
    • Kayne, P.S.1    Kim, U.2    Han, M.3    Mullen, J.R.4    Yoshizaki, F.5    Grunstein, M.6
  • 3
    • 0025093599 scopus 로고
    • Genetic analysis of histone H4: Essential role of lysines subject to reversible acetylation
    • Megee PC, Morgan BA, Miltman BA, Smith MM Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation. Science. 247:1990;841-845.
    • (1990) Science , vol.247 , pp. 841-845
    • Megee, P.C.1    Morgan, B.A.2    Miltman, B.A.3    Smith, M.M.4
  • 4
    • 0031455415 scopus 로고    scopus 로고
    • Histone acetyltransferases regulate HIV-1 enhancer activity in vitro
    • Sheridan PL, Mayall TP, Verdin E, Jones KA Histone acetyltransferases regulate HIV-1 enhancer activity in vitro. Genes Dev. 11:1997;3327-3340.
    • (1997) Genes Dev , vol.11 , pp. 3327-3340
    • Sheridan, P.L.1    Mayall, T.P.2    Verdin, E.3    Jones, K.A.4
  • 5
    • 0032574802 scopus 로고    scopus 로고
    • Perturbation of nucleosome core structure by the SWI/SNF complex persists after its detachment, enhancing subsequent transcription factor binding
    • Côté J, Peterson CL, Workman JL Perturbation of nucleosome core structure by the SWI/SNF complex persists after its detachment, enhancing subsequent transcription factor binding. Proc Natl Acad Sci USA. 95:1998;4947-4952.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4947-4952
    • Côté, J.1    Peterson, C.L.2    Workman, J.L.3
  • 6
    • 0032525139 scopus 로고    scopus 로고
    • Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin
    • Nightingale KP, Wellinger RE, Sogo JM, Becker PB Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin. EMBO J. 17:1998;2865-2876.
    • (1998) EMBO J , vol.17 , pp. 2865-2876
    • Nightingale, K.P.1    Wellinger, R.E.2    Sogo, J.M.3    Becker, P.B.4
  • 8
    • 0028846193 scopus 로고
    • Sequence and characterization of a co-activator for the steroid hormone receptor superfamily
    • Onate SA, Tsai SY, Tsai MJ, O'Malley BW Sequence and characterization of a co-activator for the steroid hormone receptor superfamily. Science. 270:1995;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
  • 9
    • 0032213938 scopus 로고    scopus 로고
    • Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation
    • The authors dissect the contributions of different LXXLL motifs as determinants for SRC-1/NCoA-1 function. Nuclear microinjection of anti-SRC-1/NCoA-1 antibodies blocked nuclear receptor transactivation. The ability of different LXXLL mutations in the context of SRC-1/NCoA-1 to rescue the block was used as a functional readout for LXXLL specificity, and that demonstrates that these determinants are distinct for different subclasses of receptors.
    • McInerney EM, Rose DW, Flynn SE, Westin S, Mullen T-M, Krones A, Inostroza J, Torcia J, Assa-Munt N, Milburn MVet al. Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes Dev. 12:1998;3357-3368. The authors dissect the contributions of different LXXLL motifs as determinants for SRC-1/NCoA-1 function. Nuclear microinjection of anti-SRC-1/NCoA-1 antibodies blocked nuclear receptor transactivation. The ability of different LXXLL mutations in the context of SRC-1/NCoA-1 to rescue the block was used as a functional readout for LXXLL specificity, and that demonstrates that these determinants are distinct for different subclasses of receptors.
    • (1998) Genes Dev , vol.12 , pp. 3357-3368
    • McInerney, E.M.1    Rose, D.W.2    Flynn, S.E.3    Westin, S.4    Mullen, T.-M.5    Krones, A.6    Inostroza, J.7    Torcia, J.8    Assa-Munt, N.9    Milburn, M.V.10
  • 10
    • 0032006563 scopus 로고    scopus 로고
    • P300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation
    • This study demonstrates for the first time ligand-dependent transactivation by estrogen receptor in vitro. The authors use a crude nuclear extract, but for the first time with a nuclear receptor, utilize chromatin assembled templates that confer a complete dependence by the receptor on estradiol. The study described a potent additional stimulation of ER transactivation by the addition of purified p300. Single-round transcription experiments suggested that one role of ligand could be to promote re-initiation of transcription from ER/p300-recruited pre-initiation complexes.
    • Kraus WL, Kadonaga JT p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation. Genes Dev. 12:1998;331-342. This study demonstrates for the first time ligand-dependent transactivation by estrogen receptor in vitro. The authors use a crude nuclear extract, but for the first time with a nuclear receptor, utilize chromatin assembled templates that confer a complete dependence by the receptor on estradiol. The study described a potent additional stimulation of ER transactivation by the addition of purified p300. Single-round transcription experiments suggested that one role of ligand could be to promote re-initiation of transcription from ER/p300-recruited pre-initiation complexes.
    • (1998) Genes Dev , vol.12 , pp. 331-342
    • Kraus, W.L.1    Kadonaga, J.T.2
  • 11
    • 0033119162 scopus 로고    scopus 로고
    • Coactivator and corepressor complexes in nuclear receptor function
    • Xu L, Glass CG, Rosenfeld MG Coactivator and corepressor complexes in nuclear receptor function. Curr Opin Genet Dev. 9:1999;140-147.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 140-147
    • Xu, L.1    Glass, C.G.2    Rosenfeld, M.G.3
  • 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, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell. 90:1997;569-580.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 17
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides T Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet Dev. 9:1999;40-48.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 18
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W, Roeder RG Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell. 90:1997;595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 19
    • 0032910957 scopus 로고    scopus 로고
    • CREB-binding protein acetylates hematopoietic transcription factor GATA-1 at important residues
    • Hung HL, Lau J, Kim AY, Weiss MJ, Blobel GA CREB-binding protein acetylates hematopoietic transcription factor GATA-1 at important residues. Mol Cell Biol. 19:1999;3496-3505.
    • (1999) Mol Cell Biol , vol.19 , pp. 3496-3505
    • Hung, H.L.1    Lau, J.2    Kim, A.Y.3    Weiss, M.J.4    Blobel, G.A.5
  • 20
  • 21
    • 0032581751 scopus 로고    scopus 로고
    • Transcriptional activators direct histone acetyltransferase complexes to nucleosomes
    • This study demonstrates that acetyl-CoA and specific co-activator complexes possessing HAT-activity stimulate transcriptional enhancement by activators from chromatin templates in a cell-free system. Both VP16 and yGCN4 interact with and recruit SAGA and NuA4 (but not Ada and Nua3) to nucleosomes to effect transcriptional stimulation which is largely dependent on the addition of acetyl-CoA.
    • Utley RT, Ikeda K, Grant PA, Côté J, Steger DJ, Eberharter A, John S, Workman JL Transcriptional activators direct histone acetyltransferase complexes to nucleosomes. Nature. 394:1998;498-502. This study demonstrates that acetyl-CoA and specific co-activator complexes possessing HAT-activity stimulate transcriptional enhancement by activators from chromatin templates in a cell-free system. Both VP16 and yGCN4 interact with and recruit SAGA and NuA4 (but not Ada and Nua3) to nucleosomes to effect transcriptional stimulation which is largely dependent on the addition of acetyl-CoA.
    • (1998) Nature , vol.394 , pp. 498-502
    • Utley, R.T.1    Ikeda, K.2    Grant, P.A.3    Côté, J.4    Steger, D.J.5    Eberharter, A.6    John, S.7    Workman, J.L.8
  • 22
    • 0033515428 scopus 로고    scopus 로고
    • Increasing the complexity of coactivation in nuclear receptor signalling
    • Freedman LP Increasing the complexity of coactivation in nuclear receptor signalling. Cell. 97:1999;5-8.
    • (1999) Cell , vol.97 , pp. 5-8
    • Freedman, L.P.1
  • 23
    • 0032554825 scopus 로고    scopus 로고
    • Distinct roles of the co-activators p300 and CBP in retinoic-acid induced F9-cell differentiation
    • The authors use hammer-head ribozymes to selectively inactivate CBP or p300, and demonstrate that these factors are critical to RAR-mediated gene activation. However, CBP and p300 appear to be differentially required by specific genes in retinoic acid-responsive cells.
    • Kawasaki H, Eckner R, Yao T-P, Taira K, Chiu R, Livingston DM, Yokoyama KK Distinct roles of the co-activators p300 and CBP in retinoic-acid induced F9-cell differentiation. Nature. 393:1998;284-289. The authors use hammer-head ribozymes to selectively inactivate CBP or p300, and demonstrate that these factors are critical to RAR-mediated gene activation. However, CBP and p300 appear to be differentially required by specific genes in retinoic acid-responsive cells.
    • (1998) Nature , vol.393 , pp. 284-289
    • Kawasaki, H.1    Eckner, R.2    Yao, T.-P.3    Taira, K.4    Chiu, R.5    Livingston, D.M.6    Yokoyama, K.K.7
  • 24
    • 0032079794 scopus 로고    scopus 로고
    • The yeast Ada complex mediates the ligand-dependent activation function of retinoid-X and estrogen receptors
    • vom Baur E, Harbers M, Um S-J, Benecke A, Chambon P The yeast Ada complex mediates the ligand-dependent activation function of retinoid-X and estrogen receptors. Genes Dev. 12:1998;1278-1289.
    • (1998) Genes Dev , vol.12 , pp. 1278-1289
    • Vom Baur, E.1    Harbers, M.2    Um, S.-J.3    Benecke, A.4    Chambon, P.5
  • 26
    • 0031941912 scopus 로고    scopus 로고
    • Distinct interactions of PML-RARα and PLZF-RARα with co-repressors determine differential responses to RA in APL
    • The authors generate PML-RARα and PLZF-RARα transgenic mice, demonstrating for the first time and directly the critical role these fusion proteins play in leukemogenesis, and demonstrating the lack of responsiveness of PLZF-RAR mice to retinoic acid, whereas PML-RAR mice are responsive. They further show that this difference can be correlated to the ability or inability of retinoic acid to induce a dissociation of the corepressor SMRT from PML-RARα versus PLZF-RARα, respectively.
    • He L-Z, Guidez F, Tribioli C, Peruzzi D, Ruthardt M, Zelent A, Pandolfi PP Distinct interactions of PML-RARα and PLZF-RARα with co-repressors determine differential responses to RA in APL. Nat Genet. 18:1998;126-135. The authors generate PML-RARα and PLZF-RARα transgenic mice, demonstrating for the first time and directly the critical role these fusion proteins play in leukemogenesis, and demonstrating the lack of responsiveness of PLZF-RAR mice to retinoic acid, whereas PML-RAR mice are responsive. They further show that this difference can be correlated to the ability or inability of retinoic acid to induce a dissociation of the corepressor SMRT from PML-RARα versus PLZF-RARα, respectively.
    • (1998) Nat Genet , vol.18 , pp. 126-135
    • He, L.-Z.1    Guidez, F.2    Tribioli, C.3    Peruzzi, D.4    Ruthardt, M.5    Zelent, A.6    Pandolfi, P.P.7
  • 27
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • The authors of this paper demonstrate that PML-RARα and PLZF-RARα associate with the HDAC complex, although only PLZF-RARα interacts directly with both SMRT and mSin3A, and that retinoic-acid-dependent dissociation SMRT from the fusion proteins is impaired.
    • Lin RJ, Nagy L, Inoue S, Shao W, Miller WH Jr., Evans RM Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature. 391:1998;811-814. The authors of this paper demonstrate that PML-RARα and PLZF-RARα associate with the HDAC complex, although only PLZF-RARα interacts directly with both SMRT and mSin3A, and that retinoic-acid-dependent dissociation SMRT from the fusion proteins is impaired.
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.4    Miller W.H., Jr.5    Evans, R.M.6
  • 28
    • 0028292448 scopus 로고
    • The SNF/SWI family of global transcriptional activators
    • Carlson M, Laurent BC The SNF/SWI family of global transcriptional activators. Curr Biol. 6:1994;396-402.
    • (1994) Curr Biol , vol.6 , pp. 396-402
    • Carlson, M.1    Laurent, B.C.2
  • 29
    • 0028467446 scopus 로고
    • Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex
    • Côté J, Quinn J, Workman JL, Peterson CL Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex. Science. 265:1994;53-60.
    • (1994) Science , vol.265 , pp. 53-60
    • Côté, J.1    Quinn, J.2    Workman, J.L.3    Peterson, C.L.4
  • 30
    • 0028068714 scopus 로고
    • Facilitated binding of TATA-binding protein to nucleosomal DNA
    • Imbalzano AN, Kwon H, Green MR, Kingston RE Facilitated binding of TATA-binding protein to nucleosomal DNA. Nature. 370:1994;481-485.
    • (1994) Nature , vol.370 , pp. 481-485
    • Imbalzano, A.N.1    Kwon, H.2    Green, M.R.3    Kingston, R.E.4
  • 32
    • 0032504102 scopus 로고    scopus 로고
    • Human Swi/SNF interconverts a nucleosome between its base state and a stable remodeled state
    • Schnitzler G, Sif S, Kingston RE Human Swi/SNF interconverts a nucleosome between its base state and a stable remodeled state. Cell. 94:1998;17-27.
    • (1998) Cell , vol.94 , pp. 17-27
    • Schnitzler, G.1    Sif, S.2    Kingston, R.E.3
  • 33
    • 0033023899 scopus 로고    scopus 로고
    • Stable remodeling of tailless nucleosomes by the human SWI-SNF complex
    • Guyon JR, Narlikar GJ, Sif S, Kingston RE Stable remodeling of tailless nucleosomes by the human SWI-SNF complex. Mol Cell Biol. 19:1999;2088-2097.
    • (1999) Mol Cell Biol , vol.19 , pp. 2088-2097
    • Guyon, J.R.1    Narlikar, G.J.2    Sif, S.3    Kingston, R.E.4
  • 34
    • 0027048595 scopus 로고
    • Roles of SWI1, SWI2 and SWI3 proteins for transcriptional enhancement by steroid receptors
    • Yoshinaga SK, Peterson CL, Herskowitz I, Yamamoto KR Roles of SWI1, SWI2 and SWI3 proteins for transcriptional enhancement by steroid receptors. Science. 258:1992;1598-1604.
    • (1992) Science , vol.258 , pp. 1598-1604
    • Yoshinaga, S.K.1    Peterson, C.L.2    Herskowitz, I.3    Yamamoto, K.R.4
  • 35
    • 0027434083 scopus 로고
    • A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor
    • Muchardt C, Yaniv M A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor. EMBO J. 12:1993;4279-4290.
    • (1993) EMBO J , vol.12 , pp. 4279-4290
    • Muchardt, C.1    Yaniv, M.2
  • 36
    • 0343632400 scopus 로고    scopus 로고
    • Ligand-dependent interaction between the estrogen receptor and the human homologues of SWI2/SNF2
    • Ichinose H, Garnier JM, Chambon P, Losson R Ligand-dependent interaction between the estrogen receptor and the human homologues of SWI2/SNF2. Gene. 188:1997;95-100.
    • (1997) Gene , vol.188 , pp. 95-100
    • Ichinose, H.1    Garnier, J.M.2    Chambon, P.3    Losson, R.4
  • 37
    • 0030610563 scopus 로고    scopus 로고
    • SNF2β-BRG1 is essential for the viability of F9 murine embryonal carcinoma cells
    • Sumi-Ichinose C, Ichinose H, Metzger D, Chambon P SNF2β-BRG1 is essential for the viability of F9 murine embryonal carcinoma cells. Mol Cell Biol. 17:1997;5976-5986.
    • (1997) Mol Cell Biol , vol.17 , pp. 5976-5986
    • Sumi-Ichinose, C.1    Ichinose, H.2    Metzger, D.3    Chambon, P.4
  • 38
    • 0030451142 scopus 로고    scopus 로고
    • Interaction of steroid hormone recptors with the transcription initiation complex
    • Beato M, Sanchez-Pacheo A Interaction of steroid hormone recptors with the transcription initiation complex. Endocrine Reviews. 17:1996;587-609.
    • (1996) Endocrine Reviews , vol.17 , pp. 587-609
    • Beato, M.1    Sanchez-Pacheo, A.2
  • 39
    • 0032492846 scopus 로고    scopus 로고
    • Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex
    • This study shows that the SNF/Swi subunit BRG-1 is a direct target of both GR and PR and suggests that transcriptional squelching due to cross-talk between these steroid receptors may be mediated at the level of template access in a chromatin context and not by competition for CBP/p300 and NCoA p160 coactivators.
    • Fryer CJ, Archer TK Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature. 393:1998;88-91. This study shows that the SNF/Swi subunit BRG-1 is a direct target of both GR and PR and suggests that transcriptional squelching due to cross-talk between these steroid receptors may be mediated at the level of template access in a chromatin context and not by competition for CBP/p300 and NCoA p160 coactivators.
    • (1998) Nature , vol.393 , pp. 88-91
    • Fryer, C.J.1    Archer, T.K.2
  • 40
    • 0033119021 scopus 로고    scopus 로고
    • Chromatin modifying and remodeling complexes
    • Kornberg RD, Lorch Y Chromatin modifying and remodeling complexes. Curr Opin Genet Dev. 9:1999;148-151.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 148-151
    • Kornberg, R.D.1    Lorch, Y.2
  • 41
    • 0031444148 scopus 로고    scopus 로고
    • ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor
    • Ito T, Bulger M, Pazin MJ, Kobayashi R, Kadonaga JT ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor. Cell. 90:1997;145-155.
    • (1997) Cell , vol.90 , pp. 145-155
    • Ito, T.1    Bulger, M.2    Pazin, M.J.3    Kobayashi, R.4    Kadonaga, J.T.5
  • 42
    • 0030839857 scopus 로고    scopus 로고
    • Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II
    • Varga-Weisz PD, Wilm M, Bonte E, Dumas K, Mann M, Becker PB Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II. Nature. 388:1997;598-602.
    • (1997) Nature , vol.388 , pp. 598-602
    • Varga-Weisz, P.D.1    Wilm, M.2    Bonte, E.3    Dumas, K.4    Mann, M.5    Becker, P.B.6
  • 43
    • 0032484098 scopus 로고    scopus 로고
    • Requirement of RSF and FACT for transcription of chromatin templates in vitro
    • The purification of the first human ISWI-containing ATP-dependent remodeling factor, RSF is described, as well as its functional requirement for initiation of transcription from chromatin templates in a highly purified transcription reaction in vitro. RSF appears to comprise hSNF2h and one additional subunit and also requires the chromatin-selective elongation factor, FACT, for transcription stimulated by the VP16 transactivator.
    • LeRoy G, Orphanides G, Lane WS, Reinberg D Requirement of RSF and FACT for transcription of chromatin templates in vitro. Science. 282:1998;1900-1904. The purification of the first human ISWI-containing ATP-dependent remodeling factor, RSF is described, as well as its functional requirement for initiation of transcription from chromatin templates in a highly purified transcription reaction in vitro. RSF appears to comprise hSNF2h and one additional subunit and also requires the chromatin-selective elongation factor, FACT, for transcription stimulated by the VP16 transactivator.
    • (1998) Science , vol.282 , pp. 1900-1904
    • Leroy, G.1    Orphanides, G.2    Lane, W.S.3    Reinberg, D.4
  • 44
    • 0029562736 scopus 로고
    • Purification and properties of an ATP-dependent nucleosome remodeling factor
    • Tsukiyama T, Wu C Purification and properties of an ATP-dependent nucleosome remodeling factor. Cell. 83:1995;1011-1020.
    • (1995) Cell , vol.83 , pp. 1011-1020
    • Tsukiyama, T.1    Wu, C.2
  • 45
    • 0031306557 scopus 로고    scopus 로고
    • Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin
    • Mizuguchi G, Tsukiyama T, Wisniewski J, Wu C Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin. Mol Cell. 1:1997;141-150.
    • (1997) Mol Cell , vol.1 , pp. 141-150
    • Mizuguchi, G.1    Tsukiyama, T.2    Wisniewski, J.3    Wu, C.4
  • 47
    • 0032538293 scopus 로고    scopus 로고
    • The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities
    • •] describe the purification of deacetylase-containing complexes, NURD, that have intrinsic ATP-dependent remodeling activity which stimulate their ability to deacetylate histones. The deacetylase inhibitor TSA does not, however, inhibit NURD's ability to remodel nucleosomes. Additionally, antibodies directed against the ATPase activity partially relieve thyroid hormone receptor-dependent repression of the TRβa promoter by microinjection experiments in Xenopus oocytes.
    • •] describe the purification of deacetylase-containing complexes, NURD, that have intrinsic ATP-dependent remodeling activity which stimulate their ability to deacetylate histones. The deacetylase inhibitor TSA does not, however, inhibit NURD's ability to remodel nucleosomes. Additionally, antibodies directed against the ATPase activity partially relieve thyroid hormone receptor-dependent repression of the TRβa promoter by microinjection experiments in Xenopus oocytes.
    • (1998) Cell , vol.95 , pp. 279-289
    • Zhang, Y.1    Leroy, G.2    Seelig, H.P.3    Lane, W.S.4    Reinberg, D.5
  • 49
    • 0033614417 scopus 로고    scopus 로고
    • Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex
    • ••] demonstrate that the vitamin D3 receptor interacts with a large, novel multiprotein complex from transcriptionally active nuclear extracts only in the presence of ligand and is important for nuclear-receptor-mediated transcription in vitro. The DRIP complex is characterized and its identity to the TRAP and ARC coactivator complexes, as well as its relationship to the SRB/Mediator complex, are established. The authors also demonstrate that the DRIP complex is essential for ligand-dependent, nuclear-receptor-mediated transactivation in vitro on chromatin-assembled templates, although the purified, transcriptionally active DRIP complex itself lacks any detectable HAT activity.
    • ••] demonstrate that the vitamin D3 receptor interacts with a large, novel multiprotein complex from transcriptionally active nuclear extracts only in the presence of ligand and is important for nuclear-receptor-mediated transcription in vitro. The DRIP complex is characterized and its identity to the TRAP and ARC coactivator complexes, as well as its relationship to the SRB/Mediator complex, are established. The authors also demonstrate that the DRIP complex is essential for ligand-dependent, nuclear-receptor-mediated transactivation in vitro on chromatin-assembled templates, although the purified, transcriptionally active DRIP complex itself lacks any detectable HAT activity.
    • (1999) Nature , vol.398 , pp. 824-828
    • Rachez, C.1    Lemon, B.D.2    Suldan, Z.3    Bromleigh, V.4    Gamble, M.5    Näär, A.M.6    Erdjument-Bromage, H.7    Tempst, P.8    Freedman, L.P.9
  • 50
    • 0029758906 scopus 로고    scopus 로고
    • Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex
    • Fondell JD, Ge H, Roeder RG Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex. Proc Natl Acad Sci USA. 93:1996;8329-8333.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8329-8333
    • Fondell, J.D.1    Ge, H.2    Roeder, R.G.3
  • 51
    • 0033587052 scopus 로고    scopus 로고
    • A shared but complex bridge
    • Kingston RE A shared but complex bridge. Nature. 399:1999;199-200.
    • (1999) Nature , vol.399 , pp. 199-200
    • Kingston, R.E.1
  • 52
    • 0033118984 scopus 로고    scopus 로고
    • RNA polymerase II as a control panel for multiple coactivator complexes
    • Hampsey M, Reinberg D RNA polymerase II as a control panel for multiple coactivator complexes. Curr Opin Genet Dev. 9:1999;132-139.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 132-139
    • Hampsey, M.1    Reinberg, D.2
  • 53
    • 0040368298 scopus 로고    scopus 로고
    • Composite coactivator ARC mediates chromatin-directed transcriptional activation
    • •], demonstrates the generality of this complex in transcriptional activation.
    • •], demonstrates the generality of this complex in transcriptional activation.
    • (1999) Nature , vol.398 , pp. 828-832
    • Näär, A.M.1    Beaurang, P.A.2    Zhou, S.3    Abrahams, A.4    Solomon, W.5    Tjian, R.6
  • 54
    • 0032135274 scopus 로고    scopus 로고
    • NAT, a human complex containing Srb polypeptides that functions as a negative regulator of activated transcription
    • This isolation of a multi-subunit complex, called NAT, by standard biochemical approaches and affinity chromatography using an anti-CDK8 (SRB10) antibody is described and demonstrated to repress activated transcription in vitro. Several NAT subunits transpire to be shared by the DRIP/TRAP/ARC complex, and NAT is essentially identical to SMCC. The results suggest that subunits unique to NAT may confer its repressive effects.
    • Sun X, Zhang Y, Cho H, Rickert P, Lees E, Lane W, Reinberg D NAT, a human complex containing Srb polypeptides that functions as a negative regulator of activated transcription. Mol Cell. 2:1998;213-222. This isolation of a multi-subunit complex, called NAT, by standard biochemical approaches and affinity chromatography using an anti-CDK8 (SRB10) antibody is described and demonstrated to repress activated transcription in vitro. Several NAT subunits transpire to be shared by the DRIP/TRAP/ARC complex, and NAT is essentially identical to SMCC. The results suggest that subunits unique to NAT may confer its repressive effects.
    • (1998) Mol Cell , vol.2 , pp. 213-222
    • Sun, X.1    Zhang, Y.2    Cho, H.3    Rickert, P.4    Lees, E.5    Lane, W.6    Reinberg, D.7
  • 55
    • 0033105821 scopus 로고    scopus 로고
    • Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators
    • A previously characterized SRB/Med-containing cofactor complex, SMCC, is shown to be essentially identical to the TRAP (DRIP/ARC) complex. Moreover, distinct subunits of TRAP are shown to interact directly with different activators, such as thyroid receptor versus p53
    • Ito M, Yuan C-X, Malik S, Gu W, Fondell JD, Yamamura S, Fu Z-Y, Zhang X, Qin J, Roeder RG Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators. Mol Cell. 3:1999;361-370. A previously characterized SRB/Med-containing cofactor complex, SMCC, is shown to be essentially identical to the TRAP (DRIP/ARC) complex. Moreover, distinct subunits of TRAP are shown to interact directly with different activators, such as thyroid receptor versus p53.
    • (1999) Mol Cell , vol.3 , pp. 361-370
    • Ito, M.1    Yuan, C.-X.2    Malik, S.3    Gu, W.4    Fondell, J.D.5    Yamamura, S.6    Fu, Z.-Y.7    Zhang, X.8    Qin, J.9    Roeder, R.G.10
  • 56
    • 0033587187 scopus 로고    scopus 로고
    • Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein
    • An E1A-interacting protein is identified as the human homologue of C. elegans Sur-2, which is a subunit of the DRIP/TRAP/ARC and NAT complexes. An antibody to hSur-2 is used to co-immunoprecipitate a complex containing human Mediator subunits, and this complex stimulates transcription in response to E1A and VP16. This paper is another link to the generality of the DRIP/TRAP/ARC complex in transcription activation.
    • Boyer TG, Martin MED, Lees E, Ricciardi RP, Berk AJ Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein. Nature. 399:1999;276-279. An E1A-interacting protein is identified as the human homologue of C. elegans Sur-2, which is a subunit of the DRIP/TRAP/ARC and NAT complexes. An antibody to hSur-2 is used to co-immunoprecipitate a complex containing human Mediator subunits, and this complex stimulates transcription in response to E1A and VP16. This paper is another link to the generality of the DRIP/TRAP/ARC complex in transcription activation.
    • (1999) Nature , vol.399 , pp. 276-279
    • Boyer, T.G.1    Martin, M.E.D.2    Lees, E.3    Ricciardi, R.P.4    Berk, A.J.5
  • 57
    • 0028282551 scopus 로고
    • A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA Polymerase II
    • Kim Y-J, Bjorkland S, Li Y, Sayre MH, Kornberg RD A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA Polymerase II. Cell. 77:1994;599-608.
    • (1994) Cell , vol.77 , pp. 599-608
    • Kim, Y.-J.1    Bjorkland, S.2    Li, Y.3    Sayre, M.H.4    Kornberg, R.D.5
  • 58
    • 0004788326 scopus 로고    scopus 로고
    • Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways
    • This paper describes the identification of a mouse Mediator complex, containing several subunits now known to be part of the coactivator DRIP/TRAP/ARC complex.
    • Jiang YW, Veschambre P, Erdjument-Bromage H, Tempst P, Conaway JW, Conaway RC, Kornberg RD Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways. Proc Natl Acad Sci USA. 95:1998;8538-8543. This paper describes the identification of a mouse Mediator complex, containing several subunits now known to be part of the coactivator DRIP/TRAP/ARC complex.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8538-8543
    • Jiang, Y.W.1    Veschambre, P.2    Erdjument-Bromage, H.3    Tempst, P.4    Conaway, J.W.5    Conaway, R.C.6    Kornberg, R.D.7
  • 59
    • 0033521956 scopus 로고    scopus 로고
    • The transcriptional co-factor complex CRSP is required for activity of the enhancer-binding protein Sp1
    • CRSP, a complex isolated functionally as an activity that stimulates Sp1 transcription in vitro is identified and found to contain subunits homologous to the yeast SRB/mediator. The subsequent identification of DRIP/TRAP/ARC revealed that it is highly related to CRSP, which itself could represent a subcomplex of DRIP/ARC/TRAP or may be a smaller specialized co-factor which has adopted 1 or 2 unique subunits.
    • Ryu S, Zhou S, Ladurner AG, Tjian R The transcriptional co-factor complex CRSP is required for activity of the enhancer-binding protein Sp1. Nature. 397:1999;446-450. CRSP, a complex isolated functionally as an activity that stimulates Sp1 transcription in vitro is identified and found to contain subunits homologous to the yeast SRB/mediator. The subsequent identification of DRIP/TRAP/ARC revealed that it is highly related to CRSP, which itself could represent a subcomplex of DRIP/ARC/TRAP or may be a smaller specialized co-factor which has adopted 1 or 2 unique subunits.
    • (1999) Nature , vol.397 , pp. 446-450
    • Ryu, S.1    Zhou, S.2    Ladurner, A.G.3    Tjian, R.4
  • 60
    • 0032518799 scopus 로고    scopus 로고
    • Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase
    • Wong J, Patterton D, Imhof A, Guschin D, Shi Y-B, Wolf AP Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase. EMBO J. 17:1998;520-534.
    • (1998) EMBO J , vol.17 , pp. 520-534
    • Wong, J.1    Patterton, D.2    Imhof, A.3    Guschin, D.4    Shi, Y.-B.5    Wolf, A.P.6
  • 61
    • 0032475845 scopus 로고    scopus 로고
    • A SWI/SNF-related chromatin remodeling complex, E-RC1, is required for tissue-specific transcriptional regulation by EKLF in vitro
    • This study describes the identification of an erythrocyte-specific SNF/Swi complex, E-RC1, which is required for ELKF-stimulated transcription of the β-globin promoter reconstituted into chromatin in a cell free system. Interestingly, E-RC1 purified from mouse erythroleukemia cells was unable to mediate TFE-3-stimulated transcription of the HIV-1 promoter. Thus ERC-1 is not a general cofactor for chromatin remodeling and may represent an activator- and/or gene-selective SNF/swi complex.
    • Armstrong JA, Bieker JJ, Emerson BM A SWI/SNF-related chromatin remodeling complex, E-RC1, is required for tissue-specific transcriptional regulation by EKLF in vitro. Cell. 95:1998;93-104. This study describes the identification of an erythrocyte-specific SNF/Swi complex, E-RC1, which is required for ELKF-stimulated transcription of the β-globin promoter reconstituted into chromatin in a cell free system. Interestingly, E-RC1 purified from mouse erythroleukemia cells was unable to mediate TFE-3-stimulated transcription of the HIV-1 promoter. Thus ERC-1 is not a general cofactor for chromatin remodeling and may represent an activator- and/or gene-selective SNF/swi complex.
    • (1998) Cell , vol.95 , pp. 93-104
    • Armstrong, J.A.1    Bieker, J.J.2    Emerson, B.M.3


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