共查询到20条相似文献,搜索用时 31 毫秒
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The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation 总被引:11,自引:0,他引:11
Krogan NJ Dover J Wood A Schneider J Heidt J Boateng MA Dean K Ryan OW Golshani A Johnston M Greenblatt JF Shilatifard A 《Molecular cell》2003,11(3):721-729
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The Spt4p subunit of yeast DSIF stimulates association of the Paf1 complex with elongating RNA polymerase II 下载免费PDF全文
The Paf1 complex (Paf1C) interacts with RNA polymerase II (Pol II) and promotes histone methylation of transcribed coding sequences, but the mechanism of Paf1C recruitment is unknown. We show that Paf1C is not recruited directly by the activator Gcn4p but is dependent on preinitiation complex assembly and Ser5 carboxy-terminal domain phosphorylation for optimal association with ARG1 coding sequences. Importantly, Spt4p is required for Paf1C occupancy at ARG1 (and other genes) and for Paf1C association with Ser5-phosphorylated Pol II in cell extracts, whereas Spt4p-Pol II association is independent of Paf1C. Since spt4Delta does not reduce levels of Pol II at ARG1, Ser5 phosphorylation, or Paf1C expression, it appears that Spt4p (or its partner in DSIF, Spt5p) provides a platform on Pol II for recruiting Paf1C following Ser5 phosphorylation and promoter clearance. spt4Delta reduces trimethylation of Lys4 on histone H3, demonstrating a new role for yeast DSIF in promoting a Paf1C-dependent function in elongation. 相似文献
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Structure and DNA binding of the human Rtf1 Plus3 domain 总被引:1,自引:0,他引:1
de Jong RN Truffault V Diercks T Ab E Daniels MA Kaptein R Folkers GE 《Structure (London, England : 1993)》2008,16(1):149-159
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SHP2 tyrosine phosphatase converts parafibromin/Cdc73 from a tumor suppressor to an oncogenic driver
Takahashi A Tsutsumi R Kikuchi I Obuse C Saito Y Seidi A Karisch R Fernandez M Cho T Ohnishi N Rozenblatt-Rosen O Meyerson M Neel BG Hatakeyama M 《Molecular cell》2011,43(1):45-56
Deregulation of SHP2 is associated with malignant diseases as well as developmental disorders. Although SHP2 is required for full activation of RAS signaling, other potential roles in cell physiology have not been elucidated. Here we show that SHP2 dephosphorylates parafibromin/Cdc73, a core component of the RNA polymerase II-associated factor (PAF) complex. Parafibromin is known to act as a tumor suppressor that inhibits cyclin D1 and c-myc by recruiting SUV39H1 histone methyltransferase. However, parafibromin can also act in the opposing direction by binding β-catenin, thereby activating promitogenic/oncogenic Wnt signaling. We found that, on tyrosine dephosphorylation by SHP2, parafibromin acquires the ability to stably bind β-catenin. The parafibromin/β-catenin interaction overrides parafibromin/SUV39H1-mediated transrepression and induces expression of Wnt target genes, including cyclin D1 and c-myc. Hence, SHP2 governs the opposing functions of parafibromin, deregulation of which may cause the development of tumors or developmental malformations. 相似文献
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Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II 下载免费PDF全文
Krogan NJ Kim M Tong A Golshani A Cagney G Canadien V Richards DP Beattie BK Emili A Boone C Shilatifard A Buratowski S Greenblatt J 《Molecular and cellular biology》2003,23(12):4207-4218
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