EMD-19022

Single-particle
4.3 Å
EMD-19022 Deposition: 01/12/2023
Map released: 30/10/2024
Last modified: 30/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-19022

Structure of Sen1-ADP.BeF3 bound RNA Polymerase II pre-termination complex

EMD-19022

Single-particle
4.3 Å
EMD-19022 Deposition: 01/12/2023
Map released: 30/10/2024
Last modified: 30/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
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
Mechanism of polyadenylation-independent RNA polymerase II termination.
Rengachari S , Hainthaler T, Oberthuer C, Lidschreiber M , Cramer P
(2024) Nat Struct Mol Biol
PUBMED: 39424994
DOI: doi:10.1038/s41594-024-01409-0
ISSN: 1545-9985
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.