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The Drosophila H3K4me3 histone demethylase, LID, is shown to be required for induction of Myc-target genes and LID, and its mammalian orthologs JARID1A/Rbp-2 and JARID1B/PLU-1 interact with Myc through their Jmj domain. Binding to Myc to the Jmj domain inhibits H3K4me3 demethylase activity and induces high levels of H3K4me3 and binding of Myc to chromatin.
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Secombe J., Li L., Carlos L., and Eisenman R.N. The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth. Genes Dev 21 (2007) 537-551. The Drosophila H3K4me3 histone demethylase, LID, is shown to be required for induction of Myc-target genes and LID, and its mammalian orthologs JARID1A/Rbp-2 and JARID1B/PLU-1 interact with Myc through their Jmj domain. Binding to Myc to the Jmj domain inhibits H3K4me3 demethylase activity and induces high levels of H3K4me3 and binding of Myc to chromatin.
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Secombe, J.1
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The function and regulation of the JARID1 family of histone H3 lysine 4 demethylases: the Myc connection
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Secombe J., and Eisenman R.N. The function and regulation of the JARID1 family of histone H3 lysine 4 demethylases: the Myc connection. Cell Cycle 6 (2007) 1324-1328
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Folk P., Puta F., and Skruzny M. Transcriptional coregulator SNW/SKIP: the concealed tie of dissimilar pathways. Cell Mol Life Sci 61 (2004) 629-640
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Emerging insights into the coactivator role of NCoA62/SKIP in Vitamin D-mediated transcription
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MacDonald P.N., Dowd D.R., Zhang C., and Gu C. Emerging insights into the coactivator role of NCoA62/SKIP in Vitamin D-mediated transcription. J Steroid Biochem Mol Biol 89-90 (2004) 179-186
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A human splicing factor, SKIP, associates with P-TEFb and enhances transcription elongation by HIV-1 Tat
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SKIP, a splicing and transcription factor, is shown to associate with P-TEFb, enhance HIV-1 Tat transactivation and stimulate transcription elongation in vitro. SKIP is recruited to the HIV-1 promoter independently of U5snRNPs, suggesting distinct roles in transcription and splicing.
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Bres V., Gomes N., Pickle L., and Jones K.A. A human splicing factor, SKIP, associates with P-TEFb and enhances transcription elongation by HIV-1 Tat. Genes Dev 19 (2005) 1211-1226. SKIP, a splicing and transcription factor, is shown to associate with P-TEFb, enhance HIV-1 Tat transactivation and stimulate transcription elongation in vitro. SKIP is recruited to the HIV-1 promoter independently of U5snRNPs, suggesting distinct roles in transcription and splicing.
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Bres, V.1
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Definition of global and transcript-specific mRNA export pathways in metazoans
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Farny N.G., Hurt J.A., and Silver P.A. Definition of global and transcript-specific mRNA export pathways in metazoans. Genes Dev 22 (2008) 66-78
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Silver, P.A.3
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CHD1 motor protein is required for deposition of histone variant H3.3 into chromatin in vivo
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CHD1 is shown to be required for the genome-wide replication-independent incorporation of histone H3.3 in Drosophila chromatin. Elimination of CHD1 in zygotes blocked H3.3 incorporation and inhibited mitosis.
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Konev A.Y., Tribus M., Park S.Y., Podhraski V., Lim C.Y., Emelyanov A.V., Vershilova E., Pirrotta V., Kadonaga J.T., Lusser A., et al. CHD1 motor protein is required for deposition of histone variant H3.3 into chromatin in vivo. Science 317 (2007) 1087-1090. CHD1 is shown to be required for the genome-wide replication-independent incorporation of histone H3.3 in Drosophila chromatin. Elimination of CHD1 in zygotes blocked H3.3 incorporation and inhibited mitosis.
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Science
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Konev, A.Y.1
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Emelyanov, A.V.6
Vershilova, E.7
Pirrotta, V.8
Kadonaga, J.T.9
Lusser, A.10
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48
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Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing
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CHD1 bound to H3K4me3 was shown to associate with splicing factors and was required for pre-mRNA splicing in vitro. In vivo, CHD1 was required for optimal splicing efficiency and loading of U2snRNPs at genes. These data link CHD1 and H3K4me3 to the early assembly of splicing complexes.
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Sims III R.J., Millhouse S., Chen C.F., Lewis B.A., Erdjument-Bromage H., Tempst P., Manley J.L., and Reinberg D. Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing. Mol Cell 28 (2007) 665-676. CHD1 bound to H3K4me3 was shown to associate with splicing factors and was required for pre-mRNA splicing in vitro. In vivo, CHD1 was required for optimal splicing efficiency and loading of U2snRNPs at genes. These data link CHD1 and H3K4me3 to the early assembly of splicing complexes.
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Mol Cell
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Sims III, R.J.1
Millhouse, S.2
Chen, C.F.3
Lewis, B.A.4
Erdjument-Bromage, H.5
Tempst, P.6
Manley, J.L.7
Reinberg, D.8
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49
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10744233477
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Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery
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Sus1 is shown to associate with SAGA complexes and the Sac3-Thp1 complex and promote mRNA export with nuclear pore proteins at the nuclear basket.
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Rodriguez-Navarro S., Fischer T., Luo M.J., Antunez O., Brettschneider S., Lechner J., Perez-Ortin J.E., Reed R., and Hurt E. Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell 116 (2004) 75-86. Sus1 is shown to associate with SAGA complexes and the Sac3-Thp1 complex and promote mRNA export with nuclear pore proteins at the nuclear basket.
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Cell
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Rodriguez-Navarro, S.1
Fischer, T.2
Luo, M.J.3
Antunez, O.4
Brettschneider, S.5
Lechner, J.6
Perez-Ortin, J.E.7
Reed, R.8
Hurt, E.9
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50
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Transcriptional activators are dispensable for transcription in the absence of Spt6-mediated chromatin reassembly of promoter regions
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Spt6, a histone H3-H4 chaperone and transcription elongation factor, is shown to be required for histone reassembly and displacement of TBP and RNAPII upon transcription repression. Failure to execute Spt6-mediated histone reassembly enables transcription to persist despite in the absence of DNA-binding activators.
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Adkins M.W., and Tyler J.K. Transcriptional activators are dispensable for transcription in the absence of Spt6-mediated chromatin reassembly of promoter regions. Mol Cell 21 (2006) 405-416. Spt6, a histone H3-H4 chaperone and transcription elongation factor, is shown to be required for histone reassembly and displacement of TBP and RNAPII upon transcription repression. Failure to execute Spt6-mediated histone reassembly enables transcription to persist despite in the absence of DNA-binding activators.
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Mol Cell
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Adkins, M.W.1
Tyler, J.K.2
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Drosophila Paf1 modulates chromatin structure at actively transcribed genes
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Adelman K., Wei W., Ardehali M.B., Werner J., Zhu B., Reinberg D., and Lis J.T. Drosophila Paf1 modulates chromatin structure at actively transcribed genes. Mol Cell Biol 26 (2006) 250-260
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Mol Cell Biol
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Adelman, K.1
Wei, W.2
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Werner, J.4
Zhu, B.5
Reinberg, D.6
Lis, J.T.7
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54
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The interaction between cap-binding complex and RNA export factor is required for intronless mRNA export
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This paper reports an association between CBP20 and REF1/Aly that is splicing-independent and required for export of intronless mRNAs.
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Nojima T., Hirose T., Kimura H., and Hagiwara M. The interaction between cap-binding complex and RNA export factor is required for intronless mRNA export. J Biol Chem 282 (2007) 15645-15651. This paper reports an association between CBP20 and REF1/Aly that is splicing-independent and required for export of intronless mRNAs.
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J Biol Chem
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Nojima, T.1
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Hagiwara, M.4
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The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila
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Andrulis E.D., Werner J., Nazarian A., Erdjument-Bromage H., Tempst P., and Lis J.T. The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila. Nature 420 (2002) 837-841
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Nature
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Andrulis, E.D.1
Werner, J.2
Nazarian, A.3
Erdjument-Bromage, H.4
Tempst, P.5
Lis, J.T.6
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Spn1 regulates the recruitment of Spt6 and the Swi/Snf complex during transcriptional activation by RNA polymerase II
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Zhang L., Fletcher A.G., Cheung V., Winston F., and Stargell L.A. Spn1 regulates the recruitment of Spt6 and the Swi/Snf complex during transcriptional activation by RNA polymerase II. Mol Cell Biol 28 (2008) 1393-1403
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Zhang, L.1
Fletcher, A.G.2
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Facts about FACT and transcript elongation through chromatin
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Belotserkovskaya R., and Reinberg D. Facts about FACT and transcript elongation through chromatin. Curr Opin Genet Dev 14 (2004) 139-146
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Transcription. Histones face the FACT
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Svejstrup J.Q. Transcription. Histones face the FACT. Science 301 (2003) 1053-1055
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Svejstrup, J.Q.1
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59
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34249099730
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Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin
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This paper defines the structural domains of Rpd3 required for binding to H3K36me3 chromatin and recruiting HDACs to reset the chromatin to a hypoacetylated state that blocks cryptic transcription.
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Li B., Gogol M., Carey M., Lee D., Seidel C., and Workman J.L. Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin. Science 316 (2007) 1050-1054. This paper defines the structural domains of Rpd3 required for binding to H3K36me3 chromatin and recruiting HDACs to reset the chromatin to a hypoacetylated state that blocks cryptic transcription.
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Science
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Li, B.1
Gogol, M.2
Carey, M.3
Lee, D.4
Seidel, C.5
Workman, J.L.6
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60
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MSL complex is attracted to genes marked by H3K36 trimethylation using a sequence-independent mechanism
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H3K36me3 chromatin, found in actively transcribed regions, is shown to direct the MSL complex to the male X chromosome to upregulate transcription. This targeting is mediated by MSL3, which binds H3K36me3 directly.
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Larschan E., Alekseyenko A.A., Gortchakov A.A., Peng S., Li B., Yang P., Workman J.L., Park P.J., and Kuroda M.I. MSL complex is attracted to genes marked by H3K36 trimethylation using a sequence-independent mechanism. Mol Cell 28 (2007) 121-133. H3K36me3 chromatin, found in actively transcribed regions, is shown to direct the MSL complex to the male X chromosome to upregulate transcription. This targeting is mediated by MSL3, which binds H3K36me3 directly.
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Mol Cell
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Larschan, E.1
Alekseyenko, A.A.2
Gortchakov, A.A.3
Peng, S.4
Li, B.5
Yang, P.6
Workman, J.L.7
Park, P.J.8
Kuroda, M.I.9
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61
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Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation
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Edmunds J.W., Mahadevan L.C., and Clayton A.L. Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation. EMBO J 27 (2008) 406-420
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Edmunds, J.W.1
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Drosophila UTX is a histone H3 Lys27 demethylase that colocalizes with the elongating form of RNA polymerase II
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Smith E.R., Lee M.G., Winter B., Droz N.M., Eissenberg J.C., Shiekhattar R., and Shilatifard A. Drosophila UTX is a histone H3 Lys27 demethylase that colocalizes with the elongating form of RNA polymerase II. Mol Cell Biol 28 (2008) 1041-1046
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Mol Cell Biol
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Smith, E.R.1
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Shiekhattar, R.6
Shilatifard, A.7
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63
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The RNA polymerase II CTD kinase Ctk1 functions in translation elongation
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P-TEFb/Ctk1 is shown to associate with polysomes and stimulate mRNA translation in yeast, acting partly through phosphorylation of Rps2 small ribosome subunit.
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Rother S., and Strasser K. The RNA polymerase II CTD kinase Ctk1 functions in translation elongation. Genes Dev 21 (2007) 1409-1421. P-TEFb/Ctk1 is shown to associate with polysomes and stimulate mRNA translation in yeast, acting partly through phosphorylation of Rps2 small ribosome subunit.
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Genes Dev
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Rother, S.1
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Hurt E., Luo M.J., Rother S., Reed R., and Strasser K. Cotranscriptional recruitment of the serine-arginine-rich (SR)-like proteins Gbp2 and Hrb1 to nascent mRNA via the TREX complex. Proc Natl Acad Sci USA 101 (2004) 1858-1862
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Hurt, E.1
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