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1
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0028347674
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An RNA polymerase II holoenzyme responsive to activators
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Koleske AJ, Young RA. An RNA polymerase II holoenzyme responsive to activators. Nature. 368:1994;466-469.
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(1994)
Nature
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Koleske, A.J.1
Young, R.A.2
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2
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0028282551
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A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II
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Kim YJ, Bjorklund 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.
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Kim, Y.J.1
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3
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0029076822
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General requirement for RNA polymerase II holoenzymes in vivo
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Thompson CM, Young RA. General requirement for RNA polymerase II holoenzymes in vivo. Proc Natl Acad Sci USA. 92:1995;4587-4590.
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Proc Natl Acad Sci USA
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Thompson, C.M.1
Young, R.A.2
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4
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0032561189
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Yeast RNA polymerase II holoenzymes and subcomplexes
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in press
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Myer VE, Young RA. Yeast RNA polymerase II holoenzymes and subcomplexes. J Biol Chem. 1998;. in press.
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(1998)
J Biol Chem
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Myer, V.E.1
Young, R.A.2
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5
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0028897907
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Association of an activator with an RNA polymerase II holoenzyme
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Hengartner CJ, Thompson CM, Zhang J, Chao DM, Liao SM, Koleske AJ, Okamura S, Young RA. Association of an activator with an RNA polymerase II holoenzyme. Genes Dev. 9:1995;897-910.
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Genes Dev
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Hengartner, C.J.1
Thompson, C.M.2
Zhang, J.3
Chao, D.M.4
Liao, S.M.5
Koleske, A.J.6
Okamura, S.7
Young, R.A.8
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6
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0031881688
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The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain
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of special interest. The 'core mediator' complex was purified from yeast cells and found to have 16 polypeptides, the identification of which reveal a subset of Srb proteins factors involved in repression, and several new factors identified as mediators of activation.
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Myers LC, Gustafsson CM, Bushnell DA, Lui M, Erdjument-Bromage H, Tempst P, Kornberg RD. The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain. of special interest Genes Dev. 12:1998;45-54 The 'core mediator' complex was purified from yeast cells and found to have 16 polypeptides, the identification of which reveal a subset of Srb proteins factors involved in repression, and several new factors identified as mediators of activation.
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(1998)
Genes Dev
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Myers, L.C.1
Gustafsson, C.M.2
Bushnell, D.A.3
Lui, M.4
Erdjument-Bromage, H.5
Tempst, P.6
Kornberg, R.D.7
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7
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0032059891
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An activator target in the RNA polymerase II holoenzyme
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of special interest. Prior to this study, considerable evidence had implicated the Srb/mediator complex of the holoenzyme in the activation process, but it was not clear how activators interact with the complex. This study made a case for a physiological interaction between the Gal4 activator and the Srb4 subunit of the holoenzyme using a combination of genetic and biochemical evidence.
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Koh SS, Ansari AZ, Ptashne M, Young RA. An activator target in the RNA polymerase II holoenzyme. of special interest Mol Cell. 1:1998;895-904 Prior to this study, considerable evidence had implicated the Srb/mediator complex of the holoenzyme in the activation process, but it was not clear how activators interact with the complex. This study made a case for a physiological interaction between the Gal4 activator and the Srb4 subunit of the holoenzyme using a combination of genetic and biochemical evidence.
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(1998)
Mol Cell
, vol.1
, pp. 895-904
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Koh, S.S.1
Ansari, A.Z.2
Ptashne, M.3
Young, R.A.4
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8
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0001448546
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A transcriptional mediator protein that is required for activation of many RNA polymerase II promoters and is conserved from yeast to humans
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Lee YC, Min S, Gim BS, Kim YJ. A transcriptional mediator protein that is required for activation of many RNA polymerase II promoters and is conserved from yeast to humans. Mol Cell Biol. 17:1997;4622-4632.
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(1997)
Mol Cell Biol
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, pp. 4622-4632
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Lee, Y.C.1
Min, S.2
Gim, B.S.3
Kim, Y.J.4
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9
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0031451166
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Genetics of transcriptional regulation in yeast: Connections to the RNA polymerase CTD
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Carlson M. Genetics of transcriptional regulation in yeast: connections to the RNA polymerase CTD. Annu Rev Cell Dev Biol. 13:1997;1-23.
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Annu Rev Cell Dev Biol
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Carlson, M.1
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10
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0032110627
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Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin dependent kinases
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of special interest. Previous reports had established that there are two kinases in the RNA polymerase II holoenzyme, but the role of the Srb10 kinase was not understood. This study demonstrated that both kinases phosphorylate the CTD, but the Srb10 kinase functions to repress transcription while the Kin28 kinase plays a positive role.
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Hengartner C J, Myer VE, Liao S-M, Wilson CJ, Koh SS, Young RA. Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin dependent kinases. of special interest Mol Cell. 2:1998;43-53 Previous reports had established that there are two kinases in the RNA polymerase II holoenzyme, but the role of the Srb10 kinase was not understood. This study demonstrated that both kinases phosphorylate the CTD, but the Srb10 kinase functions to repress transcription while the Kin28 kinase plays a positive role.
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(1998)
Mol Cell
, vol.2
, pp. 43-53
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Hengartner, C.J.1
Myer, V.E.2
Liao, S.-M.3
Wilson, C.J.4
Koh, S.S.5
Young, R.A.6
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11
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0030447612
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RSC, an essential, abundant chromatin-remodeling complex
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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. Cell. 87:1996;1249-1260.
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Cell
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Cairns, B.R.1
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Li, Y.3
Zhang, M.4
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Erdjument-Bromage, H.6
Tempst, P.7
Du, J.8
Laurent, B.9
Kornberg, R.D.10
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0028467446
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Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/SNF complex
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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.
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Côté, J.1
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13
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0030033699
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RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodeling
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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.
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(1996)
Cell
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Wilson, C.J.1
Chao, D.M.2
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Schnitzler, G.R.4
Kingston, R.E.5
Young, R.A.6
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0028832869
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A mammalian RNA polymerase II holoenzyme containing all components required for promoter-specific transcription initiation
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Ossipow V, Tassan JP, Nigg EA, Schibler U. A mammalian RNA polymerase II holoenzyme containing all components required for promoter-specific transcription initiation. Cell. 83:1995;137-146.
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Cell
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Ossipow, V.1
Tassan, J.P.2
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Schibler, U.4
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15
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0029867265
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A mammalian SRB protein associated with an RNA polymerase II holoenzyme
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Chao DM, Gadbois EL, Murray PJ, Anderson SF, Sonu MS, Parvin JD, Young RA. A mammalian SRB protein associated with an RNA polymerase II holoenzyme. Nature. 380:1996;82-85.
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(1996)
Nature
, vol.380
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Chao, D.M.1
Gadbois, E.L.2
Murray, P.J.3
Anderson, S.F.4
Sonu, M.S.5
Parvin, J.D.6
Young, R.A.7
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16
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15844390393
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A human RNA polymerase II complex associated with SRB and DNA-repair proteins
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Maldonado E, Shiekhattar R, Sheldon M, Cho H, Drapkin R, Rickert P, Lees E, Anderson CW, Linn S, Reinberg D. A human RNA polymerase II complex associated with SRB and DNA-repair proteins. Nature. 381:1996;86-89.
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Nature
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Maldonado, E.1
Shiekhattar, R.2
Sheldon, M.3
Cho, H.4
Drapkin, R.5
Rickert, P.6
Lees, E.7
Anderson, C.W.8
Linn, S.9
Reinberg, D.10
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17
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0030901305
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The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme
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Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM. The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. Mol Cell Biol. 17:1997;1817-1823.
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(1997)
Mol Cell Biol
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Cujec, T.P.1
Cho, H.2
Maldonado, E.3
Meyer, J.4
Reinberg, D.5
Peterlin, B.M.6
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18
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0030776835
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Interaction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter-specific initiation and responsive to transcriptional activators
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of special interest. A single-step affinity purification of the holoenzyme is effected by attaching to a matrix either of the elongation factors, TFIIS or Elongin A. The basal transcription factors were all purified by this technique and the relative stoichiometry of each factor was found to be approximately equimolar in the complex. Complex purified in this way was competent for activation by the model activators GAL4-VP16 and GAl4-Sp1.
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Pan G, Aso T, Greenblatt J. Interaction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter-specific initiation and responsive to transcriptional activators. of special interest J Biol Chem. 272:1997;24563-24571 A single-step affinity purification of the holoenzyme is effected by attaching to a matrix either of the elongation factors, TFIIS or Elongin A. The basal transcription factors were all purified by this technique and the relative stoichiometry of each factor was found to be approximately equimolar in the complex. Complex purified in this way was competent for activation by the model activators GAL4-VP16 and GAl4-Sp1.
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(1997)
J Biol Chem
, vol.272
, pp. 24563-24571
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Pan, G.1
Aso, T.2
Greenblatt, J.3
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19
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0030965157
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BRCA1 is a component of the RNA polymerase II holoenzyme
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of outstanding interest. In this study, a new purification of the holoenzyme complex was developed, and various factors were screened by western blotting for their presence in the complex. The breast-ovarian specific tumor suppressor, BRCA1, was found to copurify and was found to be a component of the complex by immunoprecipitation experiments. Anti-hSRB7 antibody purified BRCA1, and anti-BRCA1 antibody could specifically purify Pol II, TFIIF, TFIIE, and TFIIH. This finding is the first to identify a highly specific disease gene in a generally functioning holoenzyme complex.
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Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD. BRCA1 is a component of the RNA polymerase II holoenzyme. of outstanding interest Proc Natl Acad Sci USA. 94:1997;5605-5610 In this study, a new purification of the holoenzyme complex was developed, and various factors were screened by western blotting for their presence in the complex. The breast-ovarian specific tumor suppressor, BRCA1, was found to copurify and was found to be a component of the complex by immunoprecipitation experiments. Anti-hSRB7 antibody purified BRCA1, and anti-BRCA1 antibody could specifically purify Pol II, TFIIF, TFIIE, and TFIIH. This finding is the first to identify a highly specific disease gene in a generally functioning holoenzyme complex.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 5605-5610
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-
Scully, R.1
Anderson, S.F.2
Chao, D.M.3
Wei, W.4
Ye, L.5
Young, R.A.6
Livingston, D.M.7
Parvin, J.D.8
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20
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0032004591
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Factors associated with the mammalian RNA polymerase II holoenzyme
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of special interest. This study outlines a purification strategy for the holoenzyme using two conventional steps followed by an affinity step. The p300 factor and the SWI/SNF subunit BRG1 are found associated with the complex and recombination repair factors are not detected in this purification.
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Neish AS, Anderson SF, Schlegel BP, Wei W, Parvin JD. Factors associated with the mammalian RNA polymerase II holoenzyme. of special interest Nucleic Acids Res. 26:1998;847-853 This study outlines a purification strategy for the holoenzyme using two conventional steps followed by an affinity step. The p300 factor and the SWI/SNF subunit BRG1 are found associated with the complex and recombination repair factors are not detected in this purification.
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(1998)
Nucleic Acids Res
, vol.26
, pp. 847-853
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Neish, A.S.1
Anderson, S.F.2
Schlegel, B.P.3
Wei, W.4
Parvin, J.D.5
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21
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0018338917
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Purification of ribosomal proteins from Escherichia coli under nondenaturing conditions
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Dijk J, Littlechild J. Purification of ribosomal proteins from Escherichia coli under nondenaturing conditions. Methods Enzymol. 59:1979;481-502.
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Methods Enzymol
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Dijk, J.1
Littlechild, J.2
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22
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0031037856
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The C-terminal domain of RNA polymerase II couples mRNA processing to transcription
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of special interest. This study utilizes a TFIIS-affinity matrix to purify components of the holoenzyme and uses extremely truncated CTD molecules to map the biological effects in cells. A key conclusion of this study is that the polyadenylation factors are found as components of the holoenzyme.
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McCracken S, Fong N, Yankulov K, Ballantyne S, Pan G, Greenblatt J, Patterson SD, Wickens M, Bentley DL. The C-terminal domain of RNA polymerase II couples mRNA processing to transcription. of special interest Nature. 385:1997;357-361 This study utilizes a TFIIS-affinity matrix to purify components of the holoenzyme and uses extremely truncated CTD molecules to map the biological effects in cells. A key conclusion of this study is that the polyadenylation factors are found as components of the holoenzyme.
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(1997)
Nature
, vol.385
, pp. 357-361
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-
McCracken, S.1
Fong, N.2
Yankulov, K.3
Ballantyne, S.4
Pan, G.5
Greenblatt, J.6
Patterson, S.D.7
Wickens, M.8
Bentley, D.L.9
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23
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0030936115
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Affinity purification of a human RNA polymerase II complex using monoclonal antibodies against transcription factor IIF
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Cho H, Maldonado E, Reinberg D. Affinity purification of a human RNA polymerase II complex using monoclonal antibodies against transcription factor IIF. J Biol Chem. 272:1997;11495-11502.
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J Biol Chem
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Cho, H.1
Maldonado, E.2
Reinberg, D.3
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24
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0025988495
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Activation of class II gene transcription by regulatory factors is potentiated by a novel activity
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Meisterernst M, Roy AL, Lieu HM, Roeder RG. Activation of class II gene transcription by regulatory factors is potentiated by a novel activity. CEll. 66:1991;981-993.
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25
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0027433708
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Phosphorylated CREB binds specifically to the nuclear protein CBP
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Chrivia JC, Kwok RP, Lamb N, Hagiwara M, Montminy MR, Goodman RH. Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature. 365:1993;855-859.
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Goodman, R.H.6
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26
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0022589970
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Association of adenovirus early-region 1A proteins with cellular polypeptides
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Harlow E, Whyte P, Franza BR Jr, Schley C. Association of adenovirus early-region 1A proteins with cellular polypeptides. Mol Cell Biol. 6:1986;1579-1589.
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Harlow, E.1
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27
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0028296414
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Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor
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Eckner R, Ewen ME, Newsome D, Gerdes M, DeCaprio JA, Lawrence JB, Livingston DM. Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 8:1994;869-884.
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Genes Dev
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Eckner, R.1
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Gerdes, M.4
DeCaprio, J.A.5
Lawrence, J.B.6
Livingston, D.M.7
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28
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0028060030
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Activation of cAMP and mitogen responsive genes relies on a common nuclear factor
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Arias J, Alberts AS, Brindle P, Claret FX, Smeal T, Karin M, Feramisco J, Montminy M. Activation of cAMP and mitogen responsive genes relies on a common nuclear factor. Nature. 370:1994;226-229.
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Nature
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Arias, J.1
Alberts, A.S.2
Brindle, P.3
Claret, F.X.4
Smeal, T.5
Karin, M.6
Feramisco, J.7
Montminy, M.8
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29
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0028060029
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Nuclear protein CBP is a coactivator for the transcription factor CREB
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Kwok RP, Lundblad JR, Chrivia JC, Richards JP, Bachinger HP, Brennan RG, Roberts SG, Green MR, Goodman RH. Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature. 370:1994;223-226.
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Nature
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Kwok, R.P.1
Lundblad, J.R.2
Chrivia, J.C.3
Richards, J.P.4
Bachinger, H.P.5
Brennan, R.G.6
Roberts, S.G.7
Green, M.R.8
Goodman, R.H.9
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30
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0242587820
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A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors
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Kamei Y, Xu L, Heinzel T, Torchia J, Kurokawa R, Gloss B, Lin SC, Heyman RA, Rose DW, Glass CK, et al. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell. 85:1996;403-414.
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Cell
, vol.85
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Kamei, Y.1
Xu, L.2
Heinzel, T.3
Torchia, J.4
Kurokawa, R.5
Gloss, B.6
Lin, S.C.7
Heyman, R.A.8
Rose, D.W.9
Glass, C.K.10
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31
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0029767462
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Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha
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Bhattacharya S, Eckner R, Grossman S, Oldread E, Arany Z, D'Andrea A, Livingston DM. Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha. Nature. 383:1996;344-347.
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(1996)
Nature
, vol.383
, pp. 344-347
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Bhattacharya, S.1
Eckner, R.2
Grossman, S.3
Oldread, E.4
Arany, Z.5
D'Andrea, A.6
Livingston, D.M.7
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32
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0029817669
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Role of CBP/P300 in nuclear receptor signalling
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Chakravarti D, LaMorte VJ, Nelson MC, Nakajima T, Schulman IG, Juguilon H, Montminy M, Evans RM. Role of CBP/P300 in nuclear receptor signalling. Nature. 383:1996;99-103.
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Nature
, vol.383
, pp. 99-103
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Chakravarti, D.1
LaMorte, V.J.2
Nelson, M.C.3
Nakajima, T.4
Schulman, I.G.5
Juguilon, H.6
Montminy, M.7
Evans, R.M.8
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33
-
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0029858911
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P300 is a component of an estrogen receptor coactivator complex
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Hanstein B, Eckner R, DiRenzo J, Halachmi S, Liu H, Searcy B, Kurokawa R, Brown M. p300 is a component of an estrogen receptor coactivator complex. Proc Natl Acad Sci USA. 93:1996;11540-11545.
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(1996)
Proc Natl Acad Sci USA
, vol.93
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Hanstein, B.1
Eckner, R.2
DiRenzo, J.3
Halachmi, S.4
Liu, H.5
Searcy, B.6
Kurokawa, R.7
Brown, M.8
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34
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0030914691
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CREB-binding protein/p300 are transcriptional coactivators of p65
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of special interest. This study shows that transfection of CBP potentiated the gene activation due to transfected NF-κB subunit p65. This potentiation of transcriptional activation was inhibited by E1A protein. Two-hybrid assays and in vitro binding assays map the contacts between p65 and CBP.
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Gerritsen ME, Williams AJ, Neish AS, Moore S, Shi Y, Collins T. CREB-binding protein/p300 are transcriptional coactivators of p65. of special interest Proc Natl Acad Sci USA. 94:1997;2927-2932 This study shows that transfection of CBP potentiated the gene activation due to transfected NF-κB subunit p65. This potentiation of transcriptional activation was inhibited by E1A protein. Two-hybrid assays and in vitro binding assays map the contacts between p65 and CBP.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 2927-2932
-
-
Gerritsen, M.E.1
Williams, A.J.2
Neish, A.S.3
Moore, S.4
Shi, Y.5
Collins, T.6
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35
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0032541068
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Lineage-specific signaling in melanocytes: C-Kit stimulation recruits p300/CBP to microphthalmia
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of special interest. The disease-related microphthalmia (Mi) transcriptional regulator is found to bind to p300 following an ERK-mediated phosphorylation of the Mi protein. The transcriptional activation is inhibited by E1A.
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Price ER, Ding HF, Badalian T, Bhattacharyal S, Takemoto C, Yao TP, Hemesath TJ, Fisher DE. Lineage-specific signaling in melanocytes: c-Kit stimulation recruits p300/CBP to microphthalmia. of special interest J Biol Chem. 373:1998;17983-17986 The disease-related microphthalmia (Mi) transcriptional regulator is found to bind to p300 following an ERK-mediated phosphorylation of the Mi protein. The transcriptional activation is inhibited by E1A.
-
(1998)
J Biol Chem
, vol.373
, pp. 17983-17986
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-
Price, E.R.1
Ding, H.F.2
Badalian, T.3
Bhattacharyal, S.4
Takemoto, C.5
Yao, T.P.6
Hemesath, T.J.7
Fisher, D.E.8
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36
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0029585553
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Stimulation of c-Jun activity by CBP: C-Jun residues Ser63/73 are required for CBP induced stimulation in vivo and CBP binding in vitro
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Bannister AJ, Oehler T, Wilhelm D, Angel P, Kouzarides T. Stimulation of c-Jun activity by CBP: c-Jun residues Ser63/73 are required for CBP induced stimulation in vivo and CBP binding in vitro. Oncogene. 11:1995;2509-2514.
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(1995)
Oncogene
, vol.11
, pp. 2509-2514
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Bannister, A.J.1
Oehler, T.2
Wilhelm, D.3
Angel, P.4
Kouzarides, T.5
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37
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0030996361
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Synergistic activation of transcription by CBP and p53
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of special interest. Among the growing list of regulators acting via CBP, this study demonstrates that the key tumor suppressor protein, p53, is functioning via CBP. Transfection of CBP potentiated the gene activation due to p53, and in vitro binding assays demonstrated a direct interaction between CBP and the p53 transcriptional activation domain.
-
Gu W, Shi XL, Roeder RG. Synergistic activation of transcription by CBP and p53. of special interest Nature. 387:1997;819-823 Among the growing list of regulators acting via CBP, this study demonstrates that the key tumor suppressor protein, p53, is functioning via CBP. Transfection of CBP potentiated the gene activation due to p53, and in vitro binding assays demonstrated a direct interaction between CBP and the p53 transcriptional activation domain.
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Nature
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Gu, W.1
Shi, X.L.2
Roeder, R.G.3
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38
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Virus infection induces the assembly of coordinately activated transcription factors on the IFN-beta enhancer in vivo
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Wathelet MG, Lin CH, Parekh BS, Ronco LV, Howley PM, Maniatis T. Virus infection induces the assembly of coordinately activated transcription factors on the IFN-beta enhancer in vivo. Mol Cell. 1:1998;507-518.
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Wathelet, M.G.1
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Maniatis, T.6
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39
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0030902507
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Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors
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of outstanding interest. This study is the first to demonstrate that the previously identified CBP coactivator is, in fact, a holoenzyme component and that phosphorylated CREB activates transcription in vitro in an holoenzyme-specific fashion. For activation, the recruitment of holoenzyme via phospho-CREB is insufficient but a second signal via the 'Q2' domain of CREB to TFIID is required. This study forms the basis for our redefining CBP as an holoenzyme-bound regulatory target.
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Nakajima T, Uchida C, Anderson SF, Parvin JD, Montminy M. Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors. of outstanding interest Genes Dev. 11:1997;738-747 This study is the first to demonstrate that the previously identified CBP coactivator is, in fact, a holoenzyme component and that phosphorylated CREB activates transcription in vitro in an holoenzyme-specific fashion. For activation, the recruitment of holoenzyme via phospho-CREB is insufficient but a second signal via the 'Q2' domain of CREB to TFIID is required. This study forms the basis for our redefining CBP as an holoenzyme-bound regulatory target.
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Genes Dev
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Nakajima, T.1
Uchida, C.2
Anderson, S.F.3
Parvin, J.D.4
Montminy, M.5
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40
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0028876839
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A family of transcriptional adaptor proteins targeted by the E1A oncoprotein
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Arany Z, Newsome D, Oldread E, Livingston DM, Eckner R. A family of transcriptional adaptor proteins targeted by the E1A oncoprotein. Nature. 374:1995;81-84.
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Arany, Z.1
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41
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0030480969
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The CBP co-activator is a histone acetyltransferase
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Bannister AJ, Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature. 384:1996;641-643.
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Bannister, A.J.1
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42
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The transcriptional coactivators p300 and CBP are histone acetyltransferases
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Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 87:1996;953-959.
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43
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A CBP/p300 homolog specifies multiple differentiation pathways in Caenorhabditis elegans
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Shi Y, Mello C. A CBP/p300 homolog specifies multiple differentiation pathways in Caenorhabditis elegans. Genes Dev. 12:1998;943-955.
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Shi, Y.1
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44
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0031007189
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Histone deacetylase activity is required for full transcriptional repression by mSin3A
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Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE. Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell. 89:1997;341-347.
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Hassig, C.A.1
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45
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0030969516
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Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression
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Laherty, C.D.1
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Eisenman, R.N.6
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46
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0029665857
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A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
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Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature. 382:1996;319-324.
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Yang, X.J.1
Ogryzko, V.V.2
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Nakatani, Y.5
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47
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0030967951
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RNA helicase A mediates association of CBP with RNA polymerase II
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of special interest. Previous work had identified the CBP domain which interacts with the holoenzyme [39]. In this study, this polypeptide domain of CBP was used as a probe in far-western blots of the holoenzyme purification, and a 140 kd protein bound specifically to this probe and copurified with the holoenzyme. This protein was then applied to screening a library and the 140 kd RHA protein was found to interact with CBP. The RHA amino terminus and CBP interact and the E1A protein blocked this interaction. Truncation mutations of RHA blocked phospho-CREB activation of transcription demonstrating the functional importance of the CBP-RHA interaction within the holoenzyme complex.
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Nakajima T, Uchida C, Anderson SF, Lee CG, Hurwitz J, Parvin JD, Montminy M. RNA helicase A mediates association of CBP with RNA polymerase II. of special interest Cell. 90:1997;1107-1112 Previous work had identified the CBP domain which interacts with the holoenzyme [39]. In this study, this polypeptide domain of CBP was used as a probe in far-western blots of the holoenzyme purification, and a 140 kd protein bound specifically to this probe and copurified with the holoenzyme. This protein was then applied to screening a library and the 140 kd RHA protein was found to interact with CBP. The RHA amino terminus and CBP interact and the E1A protein blocked this interaction. Truncation mutations of RHA blocked phospho-CREB activation of transcription demonstrating the functional importance of the CBP-RHA interaction within the holoenzyme complex.
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Cell
, vol.90
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Nakajima, T.1
Uchida, C.2
Anderson, S.F.3
Lee, C.G.4
Hurwitz, J.5
Parvin, J.D.6
Montminy, M.7
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48
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0029022770
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Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP
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Petrij F, Giles RH, Dauwerse HG, Saris JJ, Hennekam RC, Masuno M, Tommerup N, van Ommen GJ, Goodman RH, Peters DJ, et al. Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature. 376:1995;348-351.
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Nature
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Petrij, F.1
Giles, R.H.2
Dauwerse, H.G.3
Saris, J.J.4
Hennekam, R.C.5
Masuno, M.6
Tommerup, N.7
Van Ommen, G.J.8
Goodman, R.H.9
Peters, D.J.10
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49
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0031830844
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BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A
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of special interest. This study demonstrates that BRCA1 binds to the RHA polypeptide, as does CBP, except via a separate domain than is bound by CBP, supporting the function of BRCA1 as a target with some similarity to CBP.
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Anderson SF, Schlegel BP, Nakajima T, Wolpin ES, Parvin JD. BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A. of special interest Nat Genet. 19:1998;254-256 This study demonstrates that BRCA1 binds to the RHA polypeptide, as does CBP, except via a separate domain than is bound by CBP, supporting the function of BRCA1 as a target with some similarity to CBP.
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(1998)
Nat Genet
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Anderson, S.F.1
Schlegel, B.P.2
Nakajima, T.3
Wolpin, E.S.4
Parvin, J.D.5
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50
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0032478085
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BRCA1 regulates p53-dependent gene expression
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Ouchi T, Monteiro ANA, August A, Aaronson SA, Hanafusa H. BRCA1 regulates p53-dependent gene expression. Proc Natl Acad Sci USA. 95:1998;2302-2306.
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Proc Natl Acad Sci USA
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Ouchi, T.1
Monteiro, A.N.A.2
August, A.3
Aaronson, S.A.4
Hanafusa, H.5
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51
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0032473879
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BRCA1 physically associates with p53 and stimulates its transcriptional activity
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of special interest. The functional comparison between BRCA1 and CBP is strengthened in this study as p53 is shown to bind to the former. The transcriptional activation domain of p53 is linked to CBP whereas a different domain of p53 is linked to BRCA1; it will be important to determine the situations under which the BRCA1-interacting domain regulates transcription.
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Zhang H, Somasundaram K, Peng Y, Tian H, Zhang H, Bi D, Weber BL, El-Deiry WS. BRCA1 physically associates with p53 and stimulates its transcriptional activity. of special interest Oncogene. 16:1998;1713-1721 The functional comparison between BRCA1 and CBP is strengthened in this study as p53 is shown to bind to the former. The transcriptional activation domain of p53 is linked to CBP whereas a different domain of p53 is linked to BRCA1; it will be important to determine the situations under which the BRCA1-interacting domain regulates transcription.
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(1998)
Oncogene
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Zhang, H.1
Somasundaram, K.2
Peng, Y.3
Tian, H.4
Zhang, H.5
Bi, D.6
Weber, B.L.7
El-Deiry, W.S.8
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52
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0030759895
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Arrest of the cell cycle by the tumour-suppressor BRCA1 requires the CDK-inhibitor p21WAF1/CiP1
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Somasundaram K, Zhang H, Zeng YX, Houvras Y, Peng Y, Zhang H, Wu GS, Licht JD, Weber BL, El-Deiry WS. Arrest of the cell cycle by the tumour-suppressor BRCA1 requires the CDK-inhibitor p21WAF1/CiP1. Nature. 389:1997;187-190.
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Nature
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Somasundaram, K.1
Zhang, H.2
Zeng, Y.X.3
Houvras, Y.4
Peng, Y.5
Zhang, H.6
Wu, G.S.7
Licht, J.D.8
Weber, B.L.9
El-Deiry, W.S.10
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53
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2642647094
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Truncating mutations of hSNF5/INI1 in aggressive paediatric cancer
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Versteege I, Sevenet N, Lange J, Rousseau-Merck MF, Ambros A, Delattre O. Truncating mutations of hSNF5/INI1 in aggressive paediatric cancer. Nature. 394:1998;203-206.
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(1998)
Nature
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Versteege, I.1
Sevenet, N.2
Lange, J.3
Rousseau-Merck, M.F.4
Ambros, A.5
Delattre, O.6
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54
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0030447943
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The TAFII250 subunit of TFIID has histone acetyltransferase activity
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Mizzen C, Yang X, Kokubo T, Brownell J, Bannister A, Owen-Hughes T, Workman J, Wang L, Berger S, Kouzarides T, et al. The TAFII250 subunit of TFIID has histone acetyltransferase activity. Cell. 87:1996;1261-1270.
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Cell
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Mizzen, C.1
Yang, X.2
Kokubo, T.3
Brownell, J.4
Bannister, A.5
Owen-Hughes, T.6
Workman, J.7
Wang, L.8
Berger, S.9
Kouzarides, T.10
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55
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0032504040
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Histone-like TAFs within the PCAF histone acetylase complex
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Ogryzko VV, Kotani T, Zhang X, Schiltz RL, Howard T, Yang XJ, Howard BH, Qin J, Nakatani Y. Histone-like TAFs within the PCAF histone acetylase complex. Cell. 94:1998;35-44.
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Cell
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Ogryzko, V.V.1
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Zhang, X.3
Schiltz, R.L.4
Howard, T.5
Yang, X.J.6
Howard, B.H.7
Qin, J.8
Nakatani, Y.9
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56
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0032504104
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A subset of TAFIIs are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulations
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Grant PA, Schieltz D, Pray-Grant MG, Steger DJ, Reesse JC, Yates JR, Workman JL: A subset of TAFIIs are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulations. Cell 94:45-53.
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Cell
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Grant, P.A.1
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Steger, D.J.4
Reesse, J.C.5
Yates, J.R.6
Workman, J.L.7
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57
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0000735813
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Synergistic recruitment of TFIIB and CBP-RNA polymerase II complexes by an interferon-b enhanceosome in vitro
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of outstanding interest
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Kim TK, Kim TH, Maniatis T. Synergistic recruitment of TFIIB and CBP-RNA polymerase II complexes by an interferon-b enhanceosome in vitro. of outstanding interest Proc Natl Acad Sci USA. 1998; The regulation of transcription by the stereospecific assembly of five different transcriptional activator proteins and an architectural protein HMG I(Y) (Figure 1b) were reconstituted using purified factors and holoenzyme. The highly structured enhanceosome complex recruited TFIIB to a preassembled TFIID/TFIIA/USA complex, and the factors in the enhanceosome subsequently recruited the Pol II holoenzyme via CBP. The data reveal that the enhanceosome functions in generating synergy by combining multiple interactions into a powerful signal to TFIIB and to the holoenzyme.
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(1998)
Proc Natl Acad Sci USA
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Kim, T.K.1
Kim, T.H.2
Maniatis, T.3
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58
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0031841947
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A human RNA polymerase II complex containing factors that modify chromatin structure
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of outstanding interest. The human holoenzyme complex was purified by conventional means, and upon gel filtration the SRB proteins were resolved into two peaks. One complex with an apparent molecular mass of ~4 MDa contained SRB proteins, Pol II. SWI/SNF, CBP/p300 and PCAF. The other complex, with a mass of about 1.5 MDa, contained SRB proteins, Pol II, and basal factors. The higher mass complex appeared to have two populations: one containing CBP/p300 and unphosphorylated Pol II and one containing PCAF and phosphorylated Pol II. As the phosphorylated Pol II is associated with the elongation stage of transcription, this study suggests that there exists an initiation form of holoenzyme containing CBP/p300 and an elongation form containing PCAF.
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Cho H, Orphanides G, Sun X, Yang XJ, Ogryzko V, Lees E, Nakatani Y, Reinberg D. A human RNA polymerase II complex containing factors that modify chromatin structure. of outstanding interest Mol Cell Biol. 18:1998;5355-5363 The human holoenzyme complex was purified by conventional means, and upon gel filtration the SRB proteins were resolved into two peaks. One complex with an apparent molecular mass of ~4 MDa contained SRB proteins, Pol II. SWI/SNF, CBP/p300 and PCAF. The other complex, with a mass of about 1.5 MDa, contained SRB proteins, Pol II, and basal factors. The higher mass complex appeared to have two populations: one containing CBP/p300 and unphosphorylated Pol II and one containing PCAF and phosphorylated Pol II. As the phosphorylated Pol II is associated with the elongation stage of transcription, this study suggests that there exists an initiation form of holoenzyme containing CBP/p300 and an elongation form containing PCAF.
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(1998)
Mol Cell Biol
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Cho, H.1
Orphanides, G.2
Sun, X.3
Yang, X.J.4
Ogryzko, V.5
Lees, E.6
Nakatani, Y.7
Reinberg, D.8
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