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-Structure paper
Title | Mechanism of polyadenylation-independent RNA polymerase II termination. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 32, Issue 2, Page 339-345, Year 2025 |
Publish date | Oct 18, 2024 |
![]() | Srinivasan Rengachari / Thomas Hainthaler / Christiane Oberthuer / Michael Lidschreiber / Patrick Cramer / ![]() |
PubMed Abstract | The mechanisms underlying the initiation and elongation of RNA polymerase II (Pol II) transcription are well-studied, whereas termination remains poorly understood. Here we analyze the mechanism of ...The mechanisms underlying the initiation and elongation of RNA polymerase II (Pol II) transcription are well-studied, whereas termination remains poorly understood. Here we analyze the mechanism of polyadenylation-independent Pol II termination mediated by the yeast Sen1 helicase. Cryo-electron microscopy structures of two pretermination intermediates show that Sen1 binds to Pol II and uses its adenosine triphosphatase activity to pull on exiting RNA in the 5' direction. This is predicted to push Pol II forward, induce an unstable hypertranslocated state and destabilize the transcription bubble, thereby facilitating termination. This mechanism of transcription termination may be widely used because it is conceptually conserved in the bacterial transcription system. |
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Methods | EM (single particle) |
Resolution | 2.8 - 4.4 Å |
Structure data | EMDB-19019, PDB-8ram: EMDB-19020, PDB-8ran: EMDB-19021, PDB-8rao: EMDB-19022, PDB-8rap: |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-MG: ![]() ChemComp-ADP: ![]() ChemComp-BEF: |
Source |
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![]() | GENE REGULATION / RNA Polymerase II / Pol II / termination / Sen1 |