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Paranjape, S.M.1
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Grunstein M. Histone acetylation in chromatin structure and transcription. Nature. 389:1997;349-352.
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Grunstein, M.1
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Pazin, M.J.1
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0029671333
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NF-κB-mediated chromatin reconfiguration and transcriptional activation of the HIV-1 enhancer in vitro
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of special interest. Synergistic transcriptional activation of chromatin-assembled HIV-1 templates by specific enhancer-binding proteins, NF-κB, Lef-1, Ets-1, Sp1, and TFE-3 was demonstrated in vitro. Distinct roles of NF-κB subunits, p50 and p65, in nucleosome remodeling and transcriptional activation of HIV-1 were also apparent in this system, which mimicked the configuration and potential of the latent and activated viral promoter.
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Pazin MJ, Sheridan PL, Cannon K, Cao Z, Keck JG, Kadonaga JT, Jones KA. NF-κB-mediated chromatin reconfiguration and transcriptional activation of the HIV-1 enhancer in vitro. of special interest Genes Dev. 10:1996;37-49 Synergistic transcriptional activation of chromatin-assembled HIV-1 templates by specific enhancer-binding proteins, NF-κB, Lef-1, Ets-1, Sp1, and TFE-3 was demonstrated in vitro. Distinct roles of NF-κB subunits, p50 and p65, in nucleosome remodeling and transcriptional activation of HIV-1 were also apparent in this system, which mimicked the configuration and potential of the latent and activated viral promoter.
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Genes Dev
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Pazin, M.J.1
Sheridan, P.L.2
Cannon, K.3
Cao, Z.4
Keck, J.G.5
Kadonaga, J.T.6
Jones, K.A.7
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7
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Stable co-occupancy of transcription factors and histones at the HIV-1 enhancer
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Steger DJ, Workman JL. Stable co-occupancy of transcription factors and histones at the HIV-1 enhancer. EMBO. 16:1997;2463-2472.
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Steger, D.J.1
Workman, J.L.2
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8
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0030946171
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Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: Hormone-regulated chromatin disruption is not sufficient for transcriptional activation
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of special interest. Insights into the mechanism of thyroid hormone dependent chromatin disruption and transcriptional activation were here obtained in oocyte microinjection experiments. Disruption and gene activation occur in two distinct stages: in the absence of hormone, thyroid hormone receptor (TR-RXR) remodels nucleosomes locally and silences transcription; in the presence of hormone, extensive chromatin disruption and transcriptional activation occurs. A specific domain within the TR protein was identified which is required for hormone binding, extensive chromatin disruption, and transcriptional activation.
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Wong J, Shi Y-B, Wolffe AP. Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: hormone-regulated chromatin disruption is not sufficient for transcriptional activation. of special interest EMBO. 16:1997;3158-3171 Insights into the mechanism of thyroid hormone dependent chromatin disruption and transcriptional activation were here obtained in oocyte microinjection experiments. Disruption and gene activation occur in two distinct stages: in the absence of hormone, thyroid hormone receptor (TR-RXR) remodels nucleosomes locally and silences transcription; in the presence of hormone, extensive chromatin disruption and transcriptional activation occurs. A specific domain within the TR protein was identified which is required for hormone binding, extensive chromatin disruption, and transcriptional activation.
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(1997)
EMBO
, vol.16
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Wong, J.1
Shi Y-B2
Wolffe, A.P.3
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9
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0030935280
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RNA polymerase II holoenzyme recruitment is sufficient to remodel chromatin at the yeast PH05 promoter
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Gaudreau L, Schmid A, Blaschke D, Ptashne M, Hörz W. RNA polymerase II holoenzyme recruitment is sufficient to remodel chromatin at the yeast PH05 promoter. Cell. 89:1997;55-62.
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Gaudreau, L.1
Schmid, A.2
Blaschke, D.3
Ptashne, M.4
Hörz, W.5
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10
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0030943424
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Distinct roles for P-CREB and LEF-1 in TCRα enhancer assembly and activation on chromatin templates in vitro
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Mayall TP, Sheridan PL, Montminy MR, Jones KA. Distinct roles for P-CREB and LEF-1 in TCRα enhancer assembly and activation on chromatin templates in vitro. Genes Dev. 11:1997;887-899.
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Mayall, T.P.1
Sheridan, P.L.2
Montminy, M.R.3
Jones, K.A.4
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11
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An HMG I/Y-containing repressor complex and supercoiled DNA topology are critical for long-range enhancer-dependent transcription in vitro
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Bagga R, Emerson BM. An HMG I/Y-containing repressor complex and supercoiled DNA topology are critical for long-range enhancer-dependent transcription in vitro. Genes Dev. 11:1997;629-639.
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Bagga, R.1
Emerson, B.M.2
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12
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Barton, M.C.1
Madani, N.2
Emerson, B.M.3
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13
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NF-E2 disrupts chromatin structure at human β-globin locus control region hypersensitive site 2 in vitro
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Armstrong JA, Emerson BM. NF-E2 disrupts chromatin structure at human β-globin locus control region hypersensitive site 2 in vitro. Mol Cell Biol. 16:1996;5634-5644.
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Armstrong, J.A.1
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RNA polymerase I transcription on nucleosomal templates: The transcription termination factor TTF-I induces chromatin remodeling and relieves transcriptional repression
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Längst G, Blank TA, Becker PB, Grummt I. RNA polymerase I transcription on nucleosomal templates: the transcription termination factor TTF-I induces chromatin remodeling and relieves transcriptional repression. EMBO J. 16:1997;760-768.
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Längst, G.1
Blank, T.A.2
Becker, P.B.3
Grummt, I.4
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Pazin MJ, Bhargava P, Geiduschek EP, Kadonaga JT. Nucleosome mobility and the maintenance of nucleosome positioning. Science. 276:1997;809-812.
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Pazin, M.J.1
Bhargava, P.2
Geiduschek, E.P.3
Kadonaga, J.T.4
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16
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0029826906
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Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex
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of special interest. In vitro analysis demonstrating that the ATP-dependent chromatin disruption caused by the interaction of purified yeast SWI/SNF with a nucleosomal array persisted at specific nucleosomes which were bound by the activator protein Gal 4, even after the removal of SWI/SNF, SWI/SNF is required only transiently to generate a stable chromatin structural change in the presence of transcription factors.
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Owen-Hughes T, Utley RT, Côté J, Peterson CL, Workman JL. Persistent site-specific remodeling of a nucleosome array by transient action of the SWI/SNF complex. of special interest Science. 273:1996;513-516 In vitro analysis demonstrating that the ATP-dependent chromatin disruption caused by the interaction of purified yeast SWI/SNF with a nucleosomal array persisted at specific nucleosomes which were bound by the activator protein Gal 4, even after the removal of SWI/SNF, SWI/SNF is required only transiently to generate a stable chromatin structural change in the presence of transcription factors.
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Science
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Owen-Hughes, T.1
Utley, R.T.2
Côté, J.3
Peterson, C.L.4
Workman, J.L.5
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17
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1842375739
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SWI/SNF stimulates the formation of disparate activator-nucleosome complexes but is partially redundant with cooperative binding
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Utley RT, Côté J, Owen-Hughes T, Workman JL. SWI/SNF stimulates the formation of disparate activator-nucleosome complexes but is partially redundant with cooperative binding. J Biol Chem. 272:1997;12642-12649.
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Utley, R.T.1
Côté, J.2
Owen-Hughes, T.3
Workman, J.L.4
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18
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0031444148
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ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor
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of outstanding interest. The purification of a novel protein complex, ACF, from Drosophila that assembles nucleosomes, in combination with histone chaperones, and remodels preformed chromatin to facilitate protein binding and transcriptional activation; both processes are ATP-dependent. This is the first biochemical demonstration of a remodeling complex that directly activates transcription of chromatin templates. ACF contains the ATPase, ISWI, but is distinct from other ISWI-containing Drosophila remodeling complexes, NURF and CHRAC.
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Ito T, Bulger M, Pazin MJ, Kobayashi R, Kadonaga JT. ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor. of outstanding interest Cell. 90:1997;145-155 The purification of a novel protein complex, ACF, from Drosophila that assembles nucleosomes, in combination with histone chaperones, and remodels preformed chromatin to facilitate protein binding and transcriptional activation; both processes are ATP-dependent. This is the first biochemical demonstration of a remodeling complex that directly activates transcription of chromatin templates. ACF contains the ATPase, ISWI, but is distinct from other ISWI-containing Drosophila remodeling complexes, NURF and CHRAC.
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(1997)
Cell
, vol.90
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Ito, T.1
Bulger, M.2
Pazin, M.J.3
Kobayashi, R.4
Kadonaga, J.T.5
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19
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0030447612
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RSC, an essential, abundant chromatin-remodeling complex
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of special interest. This paper describes the purification of a novel chromatin remodeling complex from the yeast Saccharomyces cerevisiae. RSC shares similarities to SWI/SNF in terms of overlapping subunit composition within a large complex and ATP-dependent nucleosome disruption ability but is distinct by being ten-fold more abundant and essential for mitotic growth. This suggests that it has a much different and less specialized function than SWI/SNF in chromatin remodeling.
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Cairns BR, Lorch Y, Li Y, Zhang M, Lacomis L, Erdjument-Bromage H, Tempst P, Du J, Laurent B, Kornberg RD. RSC, an essential, abundant chromatin-remodeling complex. of special interest Cell. 87:1996;1249-1260 This paper describes the purification of a novel chromatin remodeling complex from the yeast Saccharomyces cerevisiae. RSC shares similarities to SWI/SNF in terms of overlapping subunit composition within a large complex and ATP-dependent nucleosome disruption ability but is distinct by being ten-fold more abundant and essential for mitotic growth. This suggests that it has a much different and less specialized function than SWI/SNF in chromatin remodeling.
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(1996)
Cell
, vol.87
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Cairns, B.R.1
Lorch, Y.2
Li, Y.3
Zhang, M.4
Lacomis, L.5
Erdjument-Bromage, H.6
Tempst, P.7
Du, J.8
Laurent, B.9
Kornberg, R.D.10
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20
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0031306557
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Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin
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of special interest. In this paper, NURF is shown to facilitate transcription from preformed chromatin templates in combination with GAL4-HSF. After chromatin remodeling occurs, NURF is no longer required to maintain an active promoter configuration. NURF can function with a variety of proteins containing distinct DNA binding domains to remodel nucleosomes.
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Mizuguchi G, Tsukiyama T, Wisniewski J, Wu C. Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin. of special interest Mol Cell. 1:1998;141-150 In this paper, NURF is shown to facilitate transcription from preformed chromatin templates in combination with GAL4-HSF. After chromatin remodeling occurs, NURF is no longer required to maintain an active promoter configuration. NURF can function with a variety of proteins containing distinct DNA binding domains to remodel nucleosomes.
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(1998)
Mol Cell
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, pp. 141-150
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Mizuguchi, G.1
Tsukiyama, T.2
Wisniewski, J.3
Wu, C.4
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21
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0032498273
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FACT, a factor that facilitates transcript elongation through nucleosomes
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of special interest. Purification of a novel heterodimeric complex, FACT, that is required for transcriptional elongation of chromatin-assembled templates. FACT is distinct from chromatin remodeling complexes because it does not facilitate transcriptional initiation or require ATP hydrolysis.
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Orphanides G, LeRoy G, Chang C-H, Luse DS, Reinberg D. FACT, a factor that facilitates transcript elongation through nucleosomes. of special interest Cell. 92:1998;105-116 Purification of a novel heterodimeric complex, FACT, that is required for transcriptional elongation of chromatin-assembled templates. FACT is distinct from chromatin remodeling complexes because it does not facilitate transcriptional initiation or require ATP hydrolysis.
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(1998)
Cell
, vol.92
, pp. 105-116
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Orphanides, G.1
Leroy, G.2
Chang C-H3
Luse, D.S.4
Reinberg, D.5
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22
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0030741529
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Role of histone tails in nucleosome remodeling by Drosophila NURF
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Georgel PT, Tsukiyama T, Wu C. Role of histone tails in nucleosome remodeling by Drosophila NURF. EMBO J. 16:1997;4717-4726.
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EMBO J
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Georgel, P.T.1
Tsukiyama, T.2
Wu, C.3
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23
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0030842478
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The yeast SWI-SNF complex facilitates binding of a transcriptional activator to nucleosomal sites in vivo
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of special interest. Genetic studies on the role of SWI/SNF in transcriptional regulation by the yeast Gal4 activator revealed that SWI/SNF-dependence occurred in promoters having low-affinity Gal4 binding sites. SWI/SNF-independence was conferred by high-affinity Gal4 sites or by placing the low-affinity sites in a nucleosome-free region.
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Burns LG, Peterson CL. The yeast SWI-SNF complex facilitates binding of a transcriptional activator to nucleosomal sites in vivo. of special interest Mol Cell Biol. 17:1997;4811-4819 Genetic studies on the role of SWI/SNF in transcriptional regulation by the yeast Gal4 activator revealed that SWI/SNF-dependence occurred in promoters having low-affinity Gal4 binding sites. SWI/SNF-independence was conferred by high-affinity Gal4 sites or by placing the low-affinity sites in a nucleosome-free region.
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(1997)
Mol Cell Biol
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Burns, L.G.1
Peterson, C.L.2
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24
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0031939873
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Drosophila NURF-55, a WD repeat protein involved in histone metabolism
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Martinez-Balbas MA, Tsukiyama T, Gdula D, Wu C. Drosophila NURF-55, a WD repeat protein involved in histone metabolism. Proc Natl Acad Sci USA. 95:1998;132-137.
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Martinez-Balbas, M.A.1
Tsukiyama, T.2
Gdula, D.3
Wu, C.4
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25
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0030986934
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SWI2/SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions?
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Pazin MJ, Kadonaga JT. SWI2/SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions? Cell. 88:1997;737-740.
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Pazin, M.J.1
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Steger, D.J.1
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0030839857
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Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II
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of special interest. A description of the purification of a novel Drosophila protein complex, CHRAC. This complex is multi-subunit and contains two ATPases - ISWI and topoisomerase II - in contrast to other ISWI-containing Drosophila remodeling complexes, NURF and ACF, CHRAC reconfigures chromatin by increasing its general accessibility and converts irregular nucleosomal arrays to physiologically spaced structures. It is the first remodeling complex shown to contain activities that can modulate both nucleosomal structure and DNA topology.
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Varga-Weisz PD, Wilm M, Bonte E, Dumas K, Mann M, Becker PB. Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II. of special interest Nature. 388:1997;598-602 A description of the purification of a novel Drosophila protein complex, CHRAC. This complex is multi-subunit and contains two ATPases - ISWI and topoisomerase II - in contrast to other ISWI-containing Drosophila remodeling complexes, NURF and ACF, CHRAC reconfigures chromatin by increasing its general accessibility and converts irregular nucleosomal arrays to physiologically spaced structures. It is the first remodeling complex shown to contain activities that can modulate both nucleosomal structure and DNA topology.
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Nature
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Bonte, E.3
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of outstanding interest. This study redirected the field of histone acetylation by identifying the Tetrahymena p55 HAT A protein as being homologous to the yeast transcription factor Gcn5. Recombinant Gcn5 was shown to possess HAT activity in vitro.
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Brownell JE, Zhou J, Ranalli T, Kobayashi R, Edmondson DG, Roth SY, Allis CD. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. of outstanding interest Cell. 84:1996;843-851 This study redirected the field of histone acetylation by identifying the Tetrahymena p55 HAT A protein as being homologous to the yeast transcription factor Gcn5. Recombinant Gcn5 was shown to possess HAT activity in vitro.
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Roth, S.Y.6
Allis, C.D.7
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Kouzarides, T.2
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0030740253
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Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
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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.
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Nagy, L.6
Privalsky, M.L.7
Nakatani, Y.8
Evans, R.M.9
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35
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Steroid receptor coactivator-1 is a histone acetyltransferase
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Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou J, Mizzen CA, McKenna NJ, Onate SA, Tsai SY, Tsai MJ, O'Malley BW. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature. 389:1997;194-198.
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Tsai, S.Y.9
Tsai, M.J.10
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36
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The TAFII250 subunit of TFIID has histone acetyltransferase activity
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Mizzen CA, Yang X-J, Kukubo T, Brownell JE, Bannister AJ, Owen-Hughes T, Workman J, Wang L, Berger SL, Kouzarides T, et al. The TAFII250 subunit of TFIID has histone acetyltransferase activity. Cell. 87:1996;1261-1270.
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Workman, J.7
Wang, L.8
Berger, S.L.9
Kouzarides, T.10
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37
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0030797349
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Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: Characterization of an Ada complex and the SAGA (Spt/Ada) complex
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of special interest. Four yeast nucleosome acetyltransferase complexes were isolated on the basis of their fortuitous affinity for a Ni-agarose column. Two of these complexes, Ada and SAGA, contain Gcn5 as their catalytic subunit. Ada and SAGA complexes were lost in gcn5Δ, ada2Δ, and ada3Δ strains. SAGA also contains Spt gene products.
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of special interest. The tumor suppressor p53 is acetylated in vitro and in vivo by its coactivator, p300, at a site located in the carboxy-terminal DNA-binding regulatory domain. Acetylation of p53 promotes sequence-specific binding. Other transcription factors such as Max, USF, and CREB were not acetylated by p300.
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Crystal structure of the nucleosome core particle at 2.8 Å resolution
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Luger, K.1
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