ArticleNature communications2024
Single-molecule reconstruction of eukaryotic factor-dependent transcription termination.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Human RNA polymerase III termination favors decomposition over facilitated recycling.Nature communications · 2026Article
- Density transitions in the regulation of transcription.Molecular cell · 2026Review
- Structure-to-function relationships of RNA polymerases: recent advances in bacterial transcription termination.Transcription · 2026Review
- Unraveling gene expression: a beginner's guide from chromatin modifications to mRNA export inNucleus (Austin, Tex.) · 2025Review
- Single-molecule imaging for investigating the transcriptional control.Molecules and cells · 2025Review
- Single-mode termination of phage transcriptions, disclosing bacterial adaptation for facilitated reinitiations.Nucleic acids research · 2024Article
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Authors and funding
14 authors.
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Abstract
Factor-dependent termination uses molecular motors to remodel transcription machineries, but the associated mechanisms, especially in eukaryotes, are poorly understood. Here we use single-molecule fluorescence assays to characterize in real time the composition and the catalytic states of Saccharomyces cerevisiae transcription termination complexes remodeled by Sen1 helicase. We confirm that Sen1 takes the RNA transcript as its substrate and translocates along it by hydrolyzing multiple ATPs to form an intermediate with a stalled RNA polymerase II (Pol II) transcription elongation complex (TEC). We show that this intermediate dissociates upon hydrolysis of a single ATP leading to dissociation of Sen1 and RNA, after which Sen1 remains bound to the RNA. We find that Pol II ends up in a variety of states: dissociating from the DNA substrate, which is facilitated by transcription bubble rewinding, being retained to the DNA substrate, or diffusing along the DNA substrate. Our results provide a complete quantitative framework for understanding the mechanism of Sen1-dependent transcription termination in eukaryotes.
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