Structure of activated transcription complex Pol II-DSIF-PAF-SPT6
| Autor: | Patrick Cramer, Lucas Farnung, Andreas Linden, Henning Urlaub, C. Wigge, Seychelle M. Vos, Marc Boehning |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Models Molecular Transcription Elongation Genetic Sus scrofa RNA polymerase II 03 medical and health sciences Transcription (biology) Animals Humans Positive Transcriptional Elongation Factor B Negative elongation factor P-TEFb Multidisciplinary biology Chemistry Cryoelectron Microscopy RNA Nuclear Proteins DNA DSIF Phosphoproteins Cell biology Elongation factor 030104 developmental biology Transcription preinitiation complex biology.protein RNA Polymerase II Transcriptional Elongation Factors Transcription Factors |
| Zdroj: | Nature |
| ISSN: | 1476-4687 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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