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-Structure paper
タイトル | Structure of activated transcription complex Pol II-DSIF-PAF-SPT6. |
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ジャーナル・号・ページ | Nature, Vol. 560, Issue 7720, Page 607-612, Year 2018 |
掲載日 | 2018年8月22日 |
著者 | Seychelle M Vos / Lucas Farnung / Marc Boehning / Christoph Wigge / Andreas Linden / Henning Urlaub / Patrick Cramer / |
PubMed 要旨 | Gene regulation involves activation of RNA polymerase II (Pol II) that is paused and bound by the protein complexes DRB sensitivity-inducing factor (DSIF) and negative elongation factor (NELF). Here ...Gene regulation involves activation of RNA polymerase II (Pol II) that is paused and bound by the protein complexes DRB sensitivity-inducing factor (DSIF) and negative elongation factor (NELF). Here we show that formation of an activated Pol II elongation complex in vitro requires the kinase function of the positive transcription elongation factor b (P-TEFb) and the elongation factors PAF1 complex (PAF) and SPT6. The cryo-EM structure of an activated elongation complex of Sus scrofa Pol II and Homo sapiens DSIF, PAF and SPT6 was determined at 3.1 Å resolution and compared to the structure of the paused elongation complex formed by Pol II, DSIF and NELF. PAF displaces NELF from the Pol II funnel for pause release. P-TEFb phosphorylates the Pol II linker to the C-terminal domain. SPT6 binds to the phosphorylated C-terminal-domain linker and opens the RNA clamp formed by DSIF. These results provide the molecular basis for Pol II pause release and elongation activation. |
リンク | Nature / PubMed:30135578 |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.802 - 3.49 Å |
構造データ | EMDB-0030: EMDB-0031: Structure of activated transcription complex Pol II-DSIF-PAF-SPT6 (Map A) EMDB-0032: EMDB-0033: EMDB-0034: EMDB-0035: EMDB-0036: EMDB-0037: PDB-6gme: |
化合物 | ChemComp-HOH: ChemComp-ZN: ChemComp-MG: |
由来 |
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キーワード | TRANSCRIPTION / SH2 domain / Pol II interaction / Kinase target / Transcription factor / DNA / RNA Polymerase / DSIF / PAF1c / SPT6 |