EMD-19022
Structure of Sen1-ADP.BeF3 bound RNA Polymerase II pre-termination complex
EMD-19022
Single-particle4.3 Å
![EMD-19022](https://www.ebi.ac.uk/emdb/images/entry/EMD-19022/400_19022.gif)
Map released: 30/10/2024
Last modified: 30/10/2024
Sample Organism:
Saccharomyces cerevisiae,
Human immunodeficiency virus 2
Sample: Tertiary complex of RNA Polymerase II with elongation factors Elf1, Spt4, Spt5 and the termination factor Sen1
Fitted models: 8rap (Avg. Q-score: 0.24)
Deposition Authors: Rengachari S
,
Lidscreiber M,
Cramer P
Sample: Tertiary complex of RNA Polymerase II with elongation factors Elf1, Spt4, Spt5 and the termination factor Sen1
Fitted models: 8rap (Avg. Q-score: 0.24)
Deposition Authors: Rengachari S
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![](http://www.ebi.ac.uk/web_guidelines/images/logos/orcid/orcid_16x16.png)
Mechanism of polyadenylation-independent RNA polymerase II termination.
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 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.
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.