-
1
-
-
0024261583
-
Nucleosome loss activates yeast downstream promoters in vivo
-
Han M, Grunstein M. Nucleosome loss activates yeast downstream promoters in vivo. Cell. 55:1988;1137-1145.
-
(1988)
Cell
, vol.55
, pp. 1137-1145
-
-
Han, M.1
Grunstein, M.2
-
2
-
-
0026598102
-
Nucleosome loss activates CUP1 and HIS3 promoters to fully induced levels in the yeast Saccharomyces cerevisiae
-
Durrin LK, Mann RK, Grunstein M. Nucleosome loss activates CUP1 and HIS3 promoters to fully induced levels in the yeast Saccharomyces cerevisiae. Mol Cell Biol. 12:1992;1621-1629.
-
(1992)
Mol Cell Biol
, vol.12
, pp. 1621-1629
-
-
Durrin, L.K.1
Mann, R.K.2
Grunstein, M.3
-
3
-
-
0030613542
-
Amino termini of histones H3 and H4 are required for a1-alpha 2 repression in yeast
-
Huang L, Zhang WZ, Roth SY. Amino termini of histones H3 and H4 are required for a1-alpha 2 repression in yeast. Mol Cell Biol. 17:1997;6555-6562.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 6555-6562
-
-
Huang, L.1
Zhang, W.Z.2
Roth, S.Y.3
-
4
-
-
0030999604
-
Histone octamer function in vivo: Mutations in the dimer-tetramer interfaces disrupt both gene activation and repression
-
Santisteban MS, Arents G, Moudrianakis EN, Smith MM. Histone octamer function in vivo: mutations in the dimer-tetramer interfaces disrupt both gene activation and repression. EMBO J. 16:1997;2493-2506.
-
(1997)
EMBO J
, vol.16
, pp. 2493-2506
-
-
Santisteban, M.S.1
Arents, G.2
Moudrianakis, E.N.3
Smith, M.M.4
-
5
-
-
0030926592
-
Three steps in the regulation of transcription by the thyroid hormone receptor: Establishment of a repressive chromatin structure, disruption of chromatin and transcriptional activation
-
Wolffe AP, Wong J, Li Q, Levi BZ, Shi YB. Three steps in the regulation of transcription by the thyroid hormone receptor: establishment of a repressive chromatin structure, disruption of chromatin and transcriptional activation. Biochem Soc Trans. 25:1997;612-615.
-
(1997)
Biochem Soc Trans
, vol.25
, pp. 612-615
-
-
Wolffe, A.P.1
Wong, J.2
Li, Q.3
Levi, B.Z.4
Shi, Y.B.5
-
6
-
-
0031585394
-
Nucleosome transactions on the promoter of the yeast GAL and PHO genes
-
Lohr D. Nucleosome transactions on the promoter of the yeast GAL and PHO genes. J Biol Chem. 272:1997;26795-26798.
-
(1997)
J Biol Chem
, vol.272
, pp. 26795-26798
-
-
Lohr, D.1
-
7
-
-
0029848624
-
Chromatin structure and the regulation of gene expression: Remodeling at the MMTV promoter
-
Beato M. Chromatin structure and the regulation of gene expression: remodeling at the MMTV promoter. J Mol Med. 74:1997;711-724.
-
(1997)
J Mol Med
, vol.74
, pp. 711-724
-
-
Beato, M.1
-
8
-
-
0030868391
-
Retinoid-induced chromatin structure alterations in the retinoic acid receptor beta 2 promoter
-
Bhattacharyya N, Dey A, Minucci S, Zimmer A, John S, Hager G, Ozato K. Retinoid-induced chromatin structure alterations in the retinoic acid receptor beta 2 promoter. Mol Cell Biol. 17:1997;6481-6490.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 6481-6490
-
-
Bhattacharyya, N.1
Dey, A.2
Minucci, S.3
Zimmer, A.4
John, S.5
Hager, G.6
Ozato, K.7
-
9
-
-
0031106575
-
Transcription factors vs nucleosomes: Regulation of the PHO5 promoter in yeast
-
Svaren J, Hörz W. Transcription factors vs nucleosomes: regulation of the PHO5 promoter in yeast. Trends Biochem Sci. 22:1997;93-97.
-
(1997)
Trends Biochem Sci
, vol.22
, pp. 93-97
-
-
Svaren, J.1
Hörz, W.2
-
10
-
-
0030935280
-
RNA polymerase II holoenzyme recruitment is sufficient to remodel chromatin at the yeast PHO5 promoter
-
of special interest. The requirement for a classical activation domain in both transcriptional activation and chromatin remodelling is by-passed by the use of Pho4 - Gal11 fusion proteins which are believed to directly recruit the RNA polymerase II transcription machinery to the PHO5 promoter DNA. Remodelling with neither wild-type Pho4, nor Pho4 - Gal11 requires the Swi/Snf remodelling machine.
-
Gaudreau L, Schmid A, Blaschke D, Ptashne M, Hörz W. RNA polymerase II holoenzyme recruitment is sufficient to remodel chromatin at the yeast PHO5 promoter. of special interest Cell. 89:1997;55-62 The requirement for a classical activation domain in both transcriptional activation and chromatin remodelling is by-passed by the use of Pho4 - Gal11 fusion proteins which are believed to directly recruit the RNA polymerase II transcription machinery to the PHO5 promoter DNA. Remodelling with neither wild-type Pho4, nor Pho4 - Gal11 requires the Swi/Snf remodelling machine.
-
(1997)
Cell
, vol.89
, pp. 55-62
-
-
Gaudreau, L.1
Schmid, A.2
Blaschke, D.3
Ptashne, M.4
Hörz, W.5
-
11
-
-
0030979099
-
Chromatin remodeling by transcriptional activation domains in a yeast episome
-
Stafford GA, Morse RH. Chromatin remodeling by transcriptional activation domains in a yeast episome. J Biol Chem. 272:1997;11526-11534.
-
(1997)
J Biol Chem
, vol.272
, pp. 11526-11534
-
-
Stafford, G.A.1
Morse, R.H.2
-
12
-
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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
-
of outstanding interest. A domain of the thyroid hormone receptor (TR) is defined which is necessary for the chromatin disruption activity of the protein in vivo. Mutations in this specific domain allow the receptor to bind both DNA and hormone but abolish its ability to perturb chromatin. Mutations of basal promoter elements demonstrate that this hormone-dependent chromatin disruption can occur in the absence of transcription. Thus binding of the receptor to the promoter DNA, chromatin remodelling, and transcription are shown to be separable stages in gene activation in vivo.
-
Wong J, Shi YB, 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 outstanding interest EMBO J. 16:1997;3158-3171 A domain of the thyroid hormone receptor (TR) is defined which is necessary for the chromatin disruption activity of the protein in vivo. Mutations in this specific domain allow the receptor to bind both DNA and hormone but abolish its ability to perturb chromatin. Mutations of basal promoter elements demonstrate that this hormone-dependent chromatin disruption can occur in the absence of transcription. Thus binding of the receptor to the promoter DNA, chromatin remodelling, and transcription are shown to be separable stages in gene activation in vivo.
-
(1997)
EMBO J
, vol.16
, pp. 3158-3171
-
-
Wong, J.1
Shi, Y.B.2
Wolffe, A.P.3
-
13
-
-
0030995542
-
Nucleosome-mediated synergism between transcription factors on the mouse mammary tumor virus promoter
-
Chavez S, Beato M. Nucleosome-mediated synergism between transcription factors on the mouse mammary tumor virus promoter. Proc Natl Acad Sci USA. 94:1997;2885-2890.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 2885-2890
-
-
Chavez, S.1
Beato, M.2
-
14
-
-
0030713405
-
Disruption of downstream chromatin directed by a transcriptional activator
-
Brown SA, Kingston RE. Disruption of downstream chromatin directed by a transcriptional activator. Genes Dev. 11:1997;3116-3121.
-
(1997)
Genes Dev
, vol.11
, pp. 3116-3121
-
-
Brown, S.A.1
Kingston, R.E.2
-
15
-
-
0032498273
-
FACT, a factor that facilitates transcript elongation through nucleosomes
-
of special interest. An accessory factor purified from HeLa cell nuclear extracts is shown to relieve a nucleosome-induced block to transcriptional elongation. FACT (facilitates chromatin transcription) is unable to initiate transcription; however, it facilitates transcription through nucleosomes. In the in vitro transcription system employed, activator-dependent chromatin remodelling of the promoter was therefore necessary but not sufficient for productive transcription.
-
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 An accessory factor purified from HeLa cell nuclear extracts is shown to relieve a nucleosome-induced block to transcriptional elongation. FACT (facilitates chromatin transcription) is unable to initiate transcription; however, it facilitates transcription through nucleosomes. In the in vitro transcription system employed, activator-dependent chromatin remodelling of the promoter was therefore necessary but not sufficient for productive transcription.
-
(1998)
Cell
, vol.92
, pp. 105-116
-
-
Orphanides, G.1
Leroy, G.2
Chang C-H3
Luse, D.S.4
Reinberg, D.5
-
16
-
-
0030739851
-
Remodeling of regulatory nucleoprotein complexes of the Xenopus hsp70 promoter during meiotic maturation of the Xenopus oocyte
-
Landsberger N, Wolffe AP. Remodeling of regulatory nucleoprotein complexes of the Xenopus hsp70 promoter during meiotic maturation of the Xenopus oocyte. EMBO J. 16:1997;4361-4373.
-
(1997)
EMBO J
, vol.16
, pp. 4361-4373
-
-
Landsberger, N.1
Wolffe, A.P.2
-
17
-
-
1842369150
-
Glucocorticoid receptor-glucocorticoid response element binding stimulates nucleosome disruption by the SWI/SNF complex
-
Ostlund-Farrants AK, Blomquist P, Kwon H, Wrange O. Glucocorticoid receptor-glucocorticoid response element binding stimulates nucleosome disruption by the SWI/SNF complex. Mol Cell Biol. 17:1997;895-905.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 895-905
-
-
Ostlund-Farrants, A.K.1
Blomquist, P.2
Kwon, H.3
Wrange, O.4
-
18
-
-
0031034468
-
Two domains of MyoD mediate transcriptional activation of genes in repressive chromatin: A mechanism for lineage determination in myogenesis
-
of special interest. Two domains of the muscle-specific transcriptional activator MyoD, separable from the classical activation domain, are shown to be involved in this protein's ability to remodel promoters and activate transcription. The ability of MyoD to open chromatin could be inhibited by sodium butyrate, suggesting a requirement for a specific level of histone acetylation in activation and further linking this protein with the modulation of chromatin.
-
Gerber AN, Klesert TR, Bergstrom DA, Tapscott SJ. Two domains of MyoD mediate transcriptional activation of genes in repressive chromatin: a mechanism for lineage determination in myogenesis. of special interest Genes Dev. 11:1997;436-450 Two domains of the muscle-specific transcriptional activator MyoD, separable from the classical activation domain, are shown to be involved in this protein's ability to remodel promoters and activate transcription. The ability of MyoD to open chromatin could be inhibited by sodium butyrate, suggesting a requirement for a specific level of histone acetylation in activation and further linking this protein with the modulation of chromatin.
-
(1997)
Genes Dev
, vol.11
, pp. 436-450
-
-
Gerber, A.N.1
Klesert, T.R.2
Bergstrom, D.A.3
Tapscott, S.J.4
-
19
-
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0030986934
-
SWI2-SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions?
-
Pazin MJ, Kadonaga JT. SWI2-SNF2 and related proteins: ATP-driven motors that disrupt protein-DNA interactions? Cell. 88:1997;737-740.
-
(1997)
Cell
, vol.88
, pp. 737-740
-
-
Pazin, M.J.1
Kadonaga, J.T.2
-
20
-
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0028801404
-
Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription
-
Kruger W, Peterson CL, Sil A, Coburn C, Arents G, Moudrianakis EN, Herskowitz I. Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription. Genes Dev. 9:1995;2770-2779.
-
(1995)
Genes Dev
, vol.9
, pp. 2770-2779
-
-
Kruger, W.1
Peterson, C.L.2
Sil, A.3
Coburn, C.4
Arents, G.5
Moudrianakis, E.N.6
Herskowitz, I.7
-
21
-
-
0030893061
-
Effects of Sin-versions of histone H4 on yeast chromatin structure and function
-
Wechser MA, Kladde MP, Alfieri JA, Peterson CL. Effects of Sin-versions of histone H4 on yeast chromatin structure and function. EMBO J. 16:1997;2086-2095.
-
(1997)
EMBO J
, vol.16
, pp. 2086-2095
-
-
Wechser, M.A.1
Kladde, M.P.2
Alfieri, J.A.3
Peterson, C.L.4
-
22
-
-
1842375739
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SWI/SNF stimulates the formation of disparate activator nucleosome complexes but is partially redundant with cooperative binding
-
Utley RT, Cote 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.
-
(1997)
J Biol Chem
, vol.272
, pp. 12642-12649
-
-
Utley, R.T.1
Cote, J.2
Owen-Hughes, T.3
Workman, J.L.4
-
23
-
-
0030842478
-
The yeast SWI-SNF complex facilitates binding of a transcriptional activator to nucleosomal sites in vivo
-
of special interest. This paper determines the in vivo requirements for the Swi/Snf remodelling machine. It is shown for the transactivator Gal4 that only weak binding sites located within a nucleosome show significant Swi/Snf dependence.
-
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 This paper determines the in vivo requirements for the Swi/Snf remodelling machine. It is shown for the transactivator Gal4 that only weak binding sites located within a nucleosome show significant Swi/Snf dependence.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 4811-4819
-
-
Burns, L.G.1
Peterson, C.L.2
-
24
-
-
0030881740
-
Role for ADA/GCN5 products in antagonizing chromatin-mediated transcriptional repression
-
Pollard KJ, Peterson CL. Role for ADA/GCN5 products in antagonizing chromatin-mediated transcriptional repression. Mol Cell Biol. 17:1997;6212-6222.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 6212-6222
-
-
Pollard, K.J.1
Peterson, C.L.2
-
25
-
-
0030876429
-
Essential functional interactions of SAGA, a Saccharomyces cerevisiae complex of Spt, Ada, and Gcn5 proteins, with the Snf-Swi and Srb-mediator complexes
-
of outstanding interest. A screen for mutants causing synthetic lethality in conjunction with a deletion of the SAGA subunit Spt20 identified genes from two transcription associated complexes: the Swi/Snf chromatin remodelling machine and the Srb/Mediator complex, which is involved in the proper regulation of RNA polymerase II genes. The connections established here demonstrate both the interdependence and the redundancy between these different molecular activities.
-
Roberts SM, Winston F. Essential functional interactions of SAGA, a Saccharomyces cerevisiae complex of Spt, Ada, and Gcn5 proteins, with the Snf-Swi and Srb-mediator complexes. of outstanding interest Genetics. 147:1997;451-465 A screen for mutants causing synthetic lethality in conjunction with a deletion of the SAGA subunit Spt20 identified genes from two transcription associated complexes: the Swi/Snf chromatin remodelling machine and the Srb/Mediator complex, which is involved in the proper regulation of RNA polymerase II genes. The connections established here demonstrate both the interdependence and the redundancy between these different molecular activities.
-
(1997)
Genetics
, vol.147
, pp. 451-465
-
-
Roberts, S.M.1
Winston, F.2
-
26
-
-
0030447612
-
RSC, an essential, abundant chromatin-remodeling complex
-
Cairns BR, Lorch Y, Li Y, Zhang MC, Lacomis L, Erdjument-Bromage H, Tempst P, Du J, Laurent B, Kornberg RD. RSC, an essential, abundant chromatin-remodeling complex. Cell. 87:1996;1249-1260.
-
(1996)
Cell
, vol.87
, pp. 1249-1260
-
-
Cairns, B.R.1
Lorch, Y.2
Li, Y.3
Zhang, M.C.4
Lacomis, L.5
Erdjument-Bromage, H.6
Tempst, P.7
Du, J.8
Laurent, B.9
Kornberg, R.D.10
-
27
-
-
0030952319
-
Interaction of a Swi3 homolog with Sth1 provides evidence for a Swi/Snf-related complex with an essential function in Saccharomyces cerevisiae
-
Treich I, Carlson M. Interaction of a Swi3 homolog with Sth1 provides evidence for a Swi/Snf-related complex with an essential function in Saccharomyces cerevisiae. Mol Cell Biol. 17:1997;1768-1775.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 1768-1775
-
-
Treich, I.1
Carlson, M.2
-
28
-
-
0030946972
-
Sfh1p, a component of a novel chromatin-remodeling complex, is required for cell cycle progression
-
Cao Y, Cairns BR, Kornberg RD, Laurent BC. Sfh1p, a component of a novel chromatin-remodeling complex, is required for cell cycle progression. Mol Cell Biol. 17:1997;3323-3334.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 3323-3334
-
-
Cao, Y.1
Cairns, B.R.2
Kornberg, R.D.3
Laurent, B.C.4
-
29
-
-
0026580006
-
Brahma: A regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2/SWI2
-
Tamkun JW, Deuring R, Scott MP, Kissinger M, Pattatucci AM, Kaufman TC, Kennison JA. brahma: a regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2/SWI2. Cell. 68:1992;561-572.
-
(1992)
Cell
, vol.68
, pp. 561-572
-
-
Tamkun, J.W.1
Deuring, R.2
Scott, M.P.3
Kissinger, M.4
Pattatucci, A.M.5
Kaufman, T.C.6
Kennison, J.A.7
-
30
-
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0027493251
-
BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription
-
Khavari PA, Peterson CL, Tamkun JW, Mendel DB, Crabtree GR. BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription. Nature. 366:1993;170-174.
-
(1993)
Nature
, vol.366
, pp. 170-174
-
-
Khavari, P.A.1
Peterson, C.L.2
Tamkun, J.W.3
Mendel, D.B.4
Crabtree, G.R.5
-
31
-
-
0028055116
-
ATP-dependent nucleosome disruption at a heat-shock promoter mediated by binding of GAGA transcription factor
-
Tsukiyama T, Becker PB, Wu C. ATP-dependent nucleosome disruption at a heat-shock promoter mediated by binding of GAGA transcription factor. Nature. 367:1994;525-532.
-
(1994)
Nature
, vol.367
, pp. 525-532
-
-
Tsukiyama, T.1
Becker, P.B.2
Wu, C.3
-
32
-
-
0030839857
-
Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II
-
of special interest. This paper reports the isolation and partial characterisation of CHRAC (chromatin accessibility complex) from Drosophila. In addition to acting in the energy-dependent remodelling of chromatin this complex may also play a role in chromatin assembly, since it is able to utilise ATP to convert an irregular chromatin template into an ordered nucleosomal array. In addition to the Snf2-like protein ISWI (imitation switch), which is also found in nucleosome remodelling factor (NURF) and ACF (see Ito 1997 [33]), CHRAC also contains topisomerase 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. of special interest Nature. 388:1997;598-602 This paper reports the isolation and partial characterisation of CHRAC (chromatin accessibility complex) from Drosophila. In addition to acting in the energy-dependent remodelling of chromatin this complex may also play a role in chromatin assembly, since it is able to utilise ATP to convert an irregular chromatin template into an ordered nucleosomal array. In addition to the Snf2-like protein ISWI (imitation switch), which is also found in nucleosome remodelling factor (NURF) and ACF (see Ito 1997 [33]), CHRAC also contains topisomerase II.
-
(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
-
33
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-
0031444148
-
ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor
-
of special interest. The identification of the ATP-utilising chromatin assembly and remodelling factor (ACF) is described. ACF, like the nucleosome remodelling factor (NURF) and chromatin accessibility complex (CHRAC), contains the ISWI (imitation switch) protein and is able to perturb chromatin structure in an energy-dependent manner, and can assist promoter-specific chromatin reconfiguration by the complex Gal4 - VP16. Furthermore, this complex, in conjunction with ATP and a histone chaperone, is able to catalyse the formation of a periodic nucleosomal array, suggesting a role in assembly.
-
Ito T, Bulger M, Pazin MJ, Kobayashi R, Kadonaga JT. ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor. of special interest Cell. 90:1997;145-155 The identification of the ATP-utilising chromatin assembly and remodelling factor (ACF) is described. ACF, like the nucleosome remodelling factor (NURF) and chromatin accessibility complex (CHRAC), contains the ISWI (imitation switch) protein and is able to perturb chromatin structure in an energy-dependent manner, and can assist promoter-specific chromatin reconfiguration by the complex Gal4 - VP16. Furthermore, this complex, in conjunction with ATP and a histone chaperone, is able to catalyse the formation of a periodic nucleosomal array, suggesting a role in assembly.
-
(1997)
Cell
, vol.90
, pp. 145-155
-
-
Ito, T.1
Bulger, M.2
Pazin, M.J.3
Kobayashi, R.4
Kadonaga, J.T.5
-
34
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0031306557
-
Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin
-
of special interest. Nucleosome remodelling factor (NURF) is shown to be able to assist gene activation by a Gal4 - activation domain fusion protein in a chromatin environment. Once remodelling of chromatin by the transactivator is achieved NURF activity is not required, either for the continued recruitment of the general transcription factors or for the transcriptional process itself.
-
Mizuguchi G, Tsukiyama T, Wisniewski J, Wu C. Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin. of special interest Mol Cell. 1:1997;141-150 Nucleosome remodelling factor (NURF) is shown to be able to assist gene activation by a Gal4 - activation domain fusion protein in a chromatin environment. Once remodelling of chromatin by the transactivator is achieved NURF activity is not required, either for the continued recruitment of the general transcription factors or for the transcriptional process itself.
-
(1997)
Mol Cell
, vol.1
, pp. 141-150
-
-
Mizuguchi, G.1
Tsukiyama, T.2
Wisniewski, J.3
Wu, C.4
-
35
-
-
0030033699
-
RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodeling
-
Wilson CJ, Chao DM, Imbalzano AN, Schnitzler GR, Kingston RE, Young RA. RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodeling. Cell. 84:1996;235-244.
-
(1996)
Cell
, vol.84
, pp. 235-244
-
-
Wilson, C.J.1
Chao, D.M.2
Imbalzano, A.N.3
Schnitzler, G.R.4
Kingston, R.E.5
Young, R.A.6
-
36
-
-
10144228410
-
Purification and biochemical heterogeneity of the mammalian SWI-SNF complex
-
Wang WD, Cote J, Xue Y, Zhou S, Khavari PA, Biggar SR, Muchardt C, Kalpana GV, Goff SP, Yaniv M, et al. Purification and biochemical heterogeneity of the mammalian SWI-SNF complex. EMBO J. 15:1996;5370-5382.
-
(1996)
EMBO J
, vol.15
, pp. 5370-5382
-
-
Wang, W.D.1
Cote, J.2
Xue, Y.3
Zhou, S.4
Khavari, P.A.5
Biggar, S.R.6
Muchardt, C.7
Kalpana, G.V.8
Goff, S.P.9
Yaniv, M.10
-
38
-
-
1842411320
-
Crystal structure of the nucleosome core particle at 2.8 Å resolution
-
of outstanding interest. The X-ray crystal structure of the nucleosomal core particle is determined, visualising in atomic detail the relationship between the histone octamer and its 146 base pairs of DNA. Importantly, this structure suggests that the potentially acetylated histone amino-terminal tails do not contact the DNA backbone itself but pass over and between the DNA gyres to contact neighbouring particles.
-
Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 Å resolution. of outstanding interest Nature. 389:1997;251-260 The X-ray crystal structure of the nucleosomal core particle is determined, visualising in atomic detail the relationship between the histone octamer and its 146 base pairs of DNA. Importantly, this structure suggests that the potentially acetylated histone amino-terminal tails do not contact the DNA backbone itself but pass over and between the DNA gyres to contact neighbouring particles.
-
(1997)
Nature
, vol.389
, pp. 251-260
-
-
Luger, K.1
Mader, A.W.2
Richmond, R.K.3
Sargent, D.F.4
Richmond, T.J.5
-
39
-
-
0030967242
-
The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
-
Ng KW, Ridgway P, Cohen DR, Tremethick DJ. The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome. EMBO J. 16:1997;2072-2085.
-
(1997)
EMBO J
, vol.16
, pp. 2072-2085
-
-
Ng, K.W.1
Ridgway, P.2
Cohen, D.R.3
Tremethick, D.J.4
-
40
-
-
0030998534
-
Histone acetylation: Influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression
-
Ura K, Kurumizaka H, Dimitrov S, Almouzni G, Wolffe AP. Histone acetylation: influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression. EMBO J. 16:1997;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
-
41
-
-
0029984469
-
Tetrahymena histone acetyltransferase a: A homolog to yeast Gcn5p linking histone acetylation to gene activation
-
Brownell JE, Zhou JX, 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. Cell. 84:1996;843-851.
-
(1996)
Cell
, vol.84
, pp. 843-851
-
-
Brownell, J.E.1
Zhou, J.X.2
Ranalli, T.3
Kobayashi, R.4
Edmondson, D.G.5
Roth, S.Y.6
Allis, C.D.7
-
42
-
-
0031031755
-
Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo
-
of special interest. Two domains of Gcn5 required for histone acetylation activity and interaction with Ada2 are identified and shown to be essential for normal growth and transcriptional activation of specific promoters in the cell. This work provided evidence for the in vivo importance of the Adaptor complex and its acetylation activity.
-
Candau R, Zhou JX, Allis CD, Berger SL. Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo. of special interest EMBO J. 16:1997;555-565 Two domains of Gcn5 required for histone acetylation activity and interaction with Ada2 are identified and shown to be essential for normal growth and transcriptional activation of specific promoters in the cell. This work provided evidence for the in vivo importance of the Adaptor complex and its acetylation activity.
-
(1997)
EMBO J
, vol.16
, pp. 555-565
-
-
Candau, R.1
Zhou, J.X.2
Allis, C.D.3
Berger, S.L.4
-
43
-
-
0029932309
-
Structural and functional analysis of yeast putative adaptors. Evidence for an adaptor complex in vivo
-
Candau R, Berger SL. Structural and functional analysis of yeast putative adaptors. Evidence for an adaptor complex in vivo. J Biol Chem. 271:1996;5237-5245.
-
(1996)
J Biol Chem
, vol.271
, pp. 5237-5245
-
-
Candau, R.1
Berger, S.L.2
-
44
-
-
0030797349
-
Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: Characterization of an Ada complex and the SAGA (Spt-Ada) complex
-
of outstanding interest. Gcn5 was shown to be the catalytic histone acetyltransferase subunit for two multisubunit complexes able to acetylate histones within native nucleosomes. Both complexes contained the Ada2 and Ada3 proteins of the previously characterised Adaptor (Ada) complex. Furthermore, the second and larger complex (SAGA) also contained Spt genes associated with TATA-box-binding protein function. Furthermore, this work identified two additional complexes able to acetylate nucleosomal histones that do not contain Gcn5.
-
Grant PA, Duggan L, Cote J, Roberts SM, Brownell JE, Candau R, Ohba R, Owen-Hughes T, Allis CD, Winston F, et al. Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt-Ada) complex. of outstanding interest Genes Dev. 11:1997;1640-1650 Gcn5 was shown to be the catalytic histone acetyltransferase subunit for two multisubunit complexes able to acetylate histones within native nucleosomes. Both complexes contained the Ada2 and Ada3 proteins of the previously characterised Adaptor (Ada) complex. Furthermore, the second and larger complex (SAGA) also contained Spt genes associated with TATA-box-binding protein function. Furthermore, this work identified two additional complexes able to acetylate nucleosomal histones that do not contain Gcn5.
-
(1997)
Genes Dev
, vol.11
, pp. 1640-1650
-
-
Grant, P.A.1
Duggan, L.2
Cote, J.3
Roberts, S.M.4
Brownell, J.E.5
Candau, R.6
Ohba, R.7
Owen-Hughes, T.8
Allis, C.D.9
Winston, F.10
-
45
-
-
0032031606
-
Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo
-
Wang L, Lui L, Berger SL. Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo. Genes Dev. 12:1998;640-653.
-
(1998)
Genes Dev
, vol.12
, pp. 640-653
-
-
Wang, L.1
Lui, L.2
Berger, S.L.3
-
46
-
-
0031451166
-
Genetics of transcriptional regulation in yeast: Connections to the RNA polymerase II CTD
-
Carlson M. Genetics of transcriptional regulation in yeast: Connections to the RNA polymerase II CTD. Annu Rev Cell Dev Biol. 13:1997;1-23.
-
(1997)
Annu Rev Cell Dev Biol
, vol.13
, pp. 1-23
-
-
Carlson, M.1
-
47
-
-
0028104786
-
Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription
-
Silverman N, Agapite J, Guarente L. Yeast ADA2 protein binds to the VP16 protein activation domain and activates transcription. Proc Natl Acad Sci USA. 91:1994;11665-11668.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 11665-11668
-
-
Silverman, N.1
Agapite, J.2
Guarente, L.3
-
48
-
-
0029096813
-
Characterization of physical interactions of the putative transcriptional adaptor, ADA2, with acidic activation domains and TATA-binding protein
-
Barlev NA, Candau R, Wang L, Darpino P, Silverman N, Berger SL. Characterization of physical interactions of the putative transcriptional adaptor, ADA2, with acidic activation domains and TATA-binding protein. J Biol Chem. 270:1995;19337-19344.
-
(1995)
J Biol Chem
, vol.270
, pp. 19337-19344
-
-
Barlev, N.A.1
Candau, R.2
Wang, L.3
Darpino, P.4
Silverman, N.5
Berger, S.L.6
-
49
-
-
0029775651
-
ADR1 activation domains contact the histone acetyltransferase GCN5 and the core transcriptional factor TFIIB
-
Chiang YC, Komarnitsky P, Chase D, Denis CL. ADR1 activation domains contact the histone acetyltransferase GCN5 and the core transcriptional factor TFIIB. J Biol Chem. 271:1996;32359-32365.
-
(1996)
J Biol Chem
, vol.271
, pp. 32359-32365
-
-
Chiang, Y.C.1
Komarnitsky, P.2
Chase, D.3
Denis, C.L.4
-
50
-
-
0026764896
-
SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae
-
Eisenmann DM, Arndt KM, Ricupero SL, Rooney JW, Winston F. SPT3 interacts with TFIID to allow normal transcription in Saccharomyces cerevisiae. Genes Dev. 6:1992;1319-1331.
-
(1992)
Genes Dev
, vol.6
, pp. 1319-1331
-
-
Eisenmann, D.M.1
Arndt, K.M.2
Ricupero, S.L.3
Rooney, J.W.4
Winston, F.5
-
51
-
-
0029665857
-
A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
-
of special interest. The p300/CBP associated factor (PCAF) is shown to have intrinsic histone transferase (HAT) activity. Furthermore, p300/CBP itself also possesses HAT activity and the two together are suggested to function in concert in the acetylation of histones. This work is one example of several similar studies [52-57] in which components of the general transcription machinery are shown in vitro to possess HAT activity. For brevity, only this reference of the series has been annotated.
-
Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. of special interest Nature. 382:1996;319-324 The p300/CBP associated factor (PCAF) is shown to have intrinsic histone transferase (HAT) activity. Furthermore, p300/CBP itself also possesses HAT activity and the two together are suggested to function in concert in the acetylation of histones. This work is one example of several similar studies [52-57] in which components of the general transcription machinery are shown in vitro to possess HAT activity. For brevity, only this reference of the series has been annotated.
-
(1996)
Nature
, vol.382
, pp. 319-324
-
-
Yang, X.J.1
Ogryzko, V.V.2
Nishikawa, J.3
Howard, B.H.4
Nakatani, Y.5
-
52
-
-
0031036154
-
Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation
-
of special interest. See annotation to Yang 1996 [51].
-
Wang LA, Mizzen C, Ying C, Candau R, Barlev N, Brownell JE, Allis CD, Berger SL. Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation. of special interest Mol Cell Biol. 17:1997;519-527 See annotation to Yang 1996 [51].
-
(1997)
Mol Cell Biol
, vol.17
, pp. 519-527
-
-
Wang, L.A.1
Mizzen, C.2
Ying, C.3
Candau, R.4
Barlev, N.5
Brownell, J.E.6
Allis, C.D.7
Berger, S.L.8
-
53
-
-
0030480969
-
The CBP co-activator is a histone acetyltransferase
-
of special interest. See annotation to Yang 1996 [51].
-
Bannister AJ, Kouzanides T. The CBP co-activator is a histone acetyltransferase. of special interest Nature. 384:1996;641-643 See annotation to Yang 1996 [51].
-
(1996)
Nature
, vol.384
, pp. 641-643
-
-
Bannister, A.J.1
Kouzanides, T.2
-
54
-
-
0030447943
-
The TAF(II)250 subunit of TFIID has histone acetyltransferase activity
-
of special interest. See annotation to Yang 1996 [51].
-
Mizzen CA, Yang XJ, Kokubo T, Brownell JE, Bannister AJ, Owen-Hughes T, Workman J, Wang L, Berger SL, Kouzarides T, et al. The TAF(II)250 subunit of TFIID has histone acetyltransferase activity. of special interest Cell. 87:1996;1261-1270 See annotation to Yang 1996 [51].
-
(1996)
Cell
, vol.87
, pp. 1261-1270
-
-
Mizzen, C.A.1
Yang, X.J.2
Kokubo, T.3
Brownell, J.E.4
Bannister, A.J.5
Owen-Hughes, T.6
Workman, J.7
Wang, L.8
Berger, S.L.9
Kouzarides, T.10
-
55
-
-
0030768745
-
Steroid receptor coactivator-1 is a histone acetyltransferase
-
of special interest. See annotation to Yang 1996 [51].
-
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. of special interest Nature. 389:1997;194-198 See annotation to Yang 1996 [51].
-
(1997)
Nature
, vol.389
, pp. 194-198
-
-
Spencer, T.E.1
Jenster, G.2
Burcin, M.M.3
Allis, C.D.4
Zhou, J.5
Mizzen, C.A.6
McKenna, N.J.7
Onate, S.A.8
Tsai, S.Y.9
Tsai, M.J.10
O'Malley, B.W.11
-
56
-
-
0030740253
-
Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P-CAF and CBP-p300
-
of special interest. See annotation to Yang 1996 [51].
-
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. of special interest Cell. 90:1997;569-580 See annotation to Yang 1996 [51].
-
(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
-
57
-
-
0030891858
-
Mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila
-
of special interest. See annotation to Yang 1996 [51].
-
Hilfiker A, Hilfiker KD, Pannuti A, Lucchesi JC. Mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila. of special interest EMBO J. 16:1997;2054-2060 See annotation to Yang 1996 [51].
-
(1997)
EMBO J
, vol.16
, pp. 2054-2060
-
-
Hilfiker, A.1
Hilfiker, K.D.2
Pannuti, A.3
Lucchesi, J.C.4
-
58
-
-
0031239891
-
Acetylation of general transcription factors by histone acetyltransferases
-
Imhof A, Yang XJ, Ogryzko VV, Nakatani Y, Wolffe AP, Ge H. Acetylation of general transcription factors by histone acetyltransferases. Curr Biol. 7:1997;689-692.
-
(1997)
Curr Biol
, vol.7
, pp. 689-692
-
-
Imhof, A.1
Yang, X.J.2
Ogryzko, V.V.3
Nakatani, Y.4
Wolffe, A.P.5
Ge, H.6
-
59
-
-
0030797585
-
Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
-
of outstanding interest. The p53 transcriptional activator was shown to be modified both in vivo and in vitro by acetylation by its co-activator p300. Acetylation occurs in the carboxy-terminal DNA-binding domain and stimulates the protein's DNA binding ability. These data provided the first in vivo evidence for a nonhistone protein target of a histone acetyltransferase (HAT) activity involved in transcription. Thus histones may not be the targets of the many HAT activities identified.
-
Gu W, Roeder RG. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. of outstanding interest Cell. 90:1992;595-606 The p53 transcriptional activator was shown to be modified both in vivo and in vitro by acetylation by its co-activator p300. Acetylation occurs in the carboxy-terminal DNA-binding domain and stimulates the protein's DNA binding ability. These data provided the first in vivo evidence for a nonhistone protein target of a histone acetyltransferase (HAT) activity involved in transcription. Thus histones may not be the targets of the many HAT activities identified.
-
(1992)
Cell
, vol.90
, pp. 595-606
-
-
Gu, W.1
Roeder, R.G.2
-
60
-
-
0029932598
-
A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
-
Taunton J, Hassig CA, Schreiber SL. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science. 272:1996;408-411.
-
(1996)
Science
, vol.272
, pp. 408-411
-
-
Taunton, J.1
Hassig, C.A.2
Schreiber, S.L.3
-
61
-
-
0029856225
-
HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription
-
Rundlett SE, Carmen AA, Kobayashi R, Bavykin S, Turner BM, Grunstein M. HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription. Proc Natl Acad Sci USA. 93:1996;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
-
62
-
-
0030877160
-
A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators
-
Kasten MM, Dorland S, Stillman DJ. A large protein complex containing the yeast Sin3p and Rpd3p transcriptional regulators. Mol Cell Biol. 17:1997;4852-4858.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 4852-4858
-
-
Kasten, M.M.1
Dorland, S.2
Stillman, D.J.3
-
63
-
-
0030916729
-
Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
-
Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell. 89:1997;357-364.
-
(1997)
Cell
, vol.89
, pp. 357-364
-
-
Zhang, Y.1
Iratni, R.2
Erdjument-Bromage, H.3
Tempst, P.4
Reinberg, D.5
-
64
-
-
0030953186
-
Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
-
of special interest. The SMRT and N-CoR transcriptional co-repressors, which function to repress genes controlled by the retinoid and thyroid receptors, are shown to directly interact with mSin3A, a homolog of the yeast global transcriptional repressor, and with the histone deacetylase complex HDAC1 to form a multisubunit repressor complex. This work is one of several studies [64-71] which linked transcriptional repression with the recruitment of a histone deacetylase via a co-repressor, thus formally connecting repression with a proposed alteration in the level of histone acetylation. For brevity only this reference of the series has been annotated.
-
Nagy L, Kao HY, Chakravarti D, Lin RJ, Hassig CA, Ayer DE, Schreiber SL, Evans RM. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. of special interest Cell. 89:1997;373-380 The SMRT and N-CoR transcriptional co-repressors, which function to repress genes controlled by the retinoid and thyroid receptors, are shown to directly interact with mSin3A, a homolog of the yeast global transcriptional repressor, and with the histone deacetylase complex HDAC1 to form a multisubunit repressor complex. This work is one of several studies [64-71] which linked transcriptional repression with the recruitment of a histone deacetylase via a co-repressor, thus formally connecting repression with a proposed alteration in the level of histone acetylation. For brevity only this reference of the series has been annotated.
-
(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
-
65
-
-
0343924289
-
Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters
-
of special interest. See annotation to Nagy 1997 [64].
-
Kadosh D, Struhl K. Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters. of special interest Cell. 89:1997;365-371 See annotation to Nagy 1997 [64].
-
(1997)
Cell
, vol.89
, pp. 365-371
-
-
Kadosh, D.1
Struhl, K.2
-
66
-
-
0030969516
-
Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression
-
of special interest. See annotation to Nagy 1997 [64].
-
Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN. Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. of special interest Cell. 89:1997;349-356 See annotation to Nagy 1997 [64].
-
(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.N.6
-
67
-
-
0031007189
-
Histone deacetylase activity is required for full transcriptional repression by mSin3a
-
of special interest. See annotation to Nagy 1997 [64].
-
Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE. Histone deacetylase activity is required for full transcriptional repression by mSin3a. of special interest Cell. 89:1997;341-347 See annotation to Nagy 1997 [64].
-
(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
-
68
-
-
0030959244
-
Role for N-CoR and histone deacetylase in Sin3 mediated transcriptional repression
-
of special interest. See annotation to Nagy 1997 [64].
-
Alland L, Muhle R, Hou H, Potes J, Chin L, Schreiberagus N, Depinho RA. Role for N-CoR and histone deacetylase in Sin3 mediated transcriptional repression. of special interest Nature. 387:1997;49-55 See annotation to Nagy 1997 [64].
-
(1997)
Nature
, vol.387
, pp. 49-55
-
-
Alland, L.1
Muhle, R.2
Hou, H.3
Potes, J.4
Chin, L.5
Schreiberagus, N.6
Depinho, R.A.7
-
69
-
-
17744413444
-
A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression
-
of special interest. See annotation to Nagy 1997 [64].
-
Heinzel T, Lavinsky RM, Mullen TM, Soderstrom M, Laherty CD, Torchia J, Yang WM, Brard G, Ngo SD, Davie JR, et al. A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. of special interest Nature. 387:1997;43-48 See annotation to Nagy 1997 [64].
-
(1997)
Nature
, vol.387
, pp. 43-48
-
-
Heinzel, T.1
Lavinsky, R.M.2
Mullen, T.M.3
Soderstrom, M.4
Laherty, C.D.5
Torchia, J.6
Yang, W.M.7
Brard, G.8
Ngo, S.D.9
Davie, J.R.10
-
70
-
-
0032484989
-
Retinoblastoma protein recruits histone deacetylase to repress transcription
-
of special interest. See annotation to Nagy 1997 [64].
-
Brehm A, Miska EA, McCance DJ, Reid JL, Bannister AJ, Kouzarides T. Retinoblastoma protein recruits histone deacetylase to repress transcription. of special interest Nature. 391:1998;597-601 See annotation to Nagy 1997 [64].
-
(1998)
Nature
, vol.391
, pp. 597-601
-
-
Brehm, A.1
Miska, E.A.2
McCance, D.J.3
Reid, J.L.4
Bannister, A.J.5
Kouzarides, T.6
-
71
-
-
0032484904
-
Retinoblastoma protein represses transcription by recruiting a histone deacetylase
-
of special interest. See annotation to Nagy 1997 [64].
-
Magnaghi-Jaulin L, Groisman R, Naguibneva I, Robin P, Lorain S, Le Villain JP, Troalen F, Trouche D, Harel-Bellan A. Retinoblastoma protein represses transcription by recruiting a histone deacetylase. of special interest Nature. 391:1998;601-605 See annotation to Nagy 1997 [64].
-
(1998)
Nature
, vol.391
, pp. 601-605
-
-
Magnaghi-Jaulin, L.1
Groisman, R.2
Naguibneva, I.3
Robin, P.4
Lorain, S.5
Le Villain, J.P.6
Troalen, F.7
Trouche, D.8
Harel-Bellan, A.9
-
72
-
-
0032030906
-
The histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo
-
of special interest. This paper addresses the question of whether local promoter-specific changes in the level of chromatin acetylation occur upon activation in vivo. Activation of Gcn5-dependent promoters is found to result in an increase in the local level of acetylation. Furthermore, mutations in residues critical for the HAT activity of Gcn5 abolish this alteration and the resultant transcriptional activation. Thus, in vivo evidence is provided for the importance of Gcn5-dependent promoter-specific histone acetylation in gene activation.
-
Kuo MH, Zhou J, Jambeck P, Churchill MEA, Allis CD. The histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo. of special interest Genes Dev. 12:1998;627-639 This paper addresses the question of whether local promoter-specific changes in the level of chromatin acetylation occur upon activation in vivo. Activation of Gcn5-dependent promoters is found to result in an increase in the local level of acetylation. Furthermore, mutations in residues critical for the HAT activity of Gcn5 abolish this alteration and the resultant transcriptional activation. Thus, in vivo evidence is provided for the importance of Gcn5-dependent promoter-specific histone acetylation in gene activation.
-
(1998)
Genes Dev
, vol.12
, pp. 627-639
-
-
Kuo, M.H.1
Zhou, J.2
Jambeck, P.3
Churchill, M.E.A.4
Allis, C.D.5
-
73
-
-
0032015582
-
Absence of Gcn5 HAT activity defines a novel state in the opening of chromatin at the PHO5 promoter in yeast
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of special interest. Deletion of Gcn5, or mutation of specific residues critical for catalytic histone acetyltransferase (HAT) activity, prevents proper chromatin opening of the PHO5 promoter under conditions of submaximal activation. The resulting chromatin structure resembles neither the bona fide open nor closed structures and thus connects Gcn5 HAT activity with the modulation of chromatin in vivo.
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Gregory PD, Schmid A, Zavari M, Lin L, Berger SL, Hörz W. Absence of Gcn5 HAT activity defines a novel state in the opening of chromatin at the PHO5 promoter in yeast. of special interest Mol Cell. 1:1998;405-505 Deletion of Gcn5, or mutation of specific residues critical for catalytic histone acetyltransferase (HAT) activity, prevents proper chromatin opening of the PHO5 promoter under conditions of submaximal activation. The resulting chromatin structure resembles neither the bona fide open nor closed structures and thus connects Gcn5 HAT activity with the modulation of chromatin in vivo.
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(1998)
Mol Cell
, vol.1
, pp. 405-505
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Gregory, P.D.1
Schmid, A.2
Zavari, M.3
Lin, L.4
Berger, S.L.5
Hörz, W.6
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