ArticleNature communications2020
DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 53 citations in OpenAlex.
- Free energy spectroscopy reveals the mechanistic landscape of chromatin compaction.Nucleic acids research · 2026Article
- Beyond the Single Molecule: Multiplexed Methods in Force Spectroscopy.Annual review of biophysics · 2026Review
- In-Situ ssDNA Isolation from dsDNA Sources as a Streamlined Pathway to DNA Origami Assembly and Testing.bioRxiv : the preprint server for biology · 2026Article
- Free energy spectroscopy reveals the mechanistic landscape of chromatin compaction.bioRxiv : the preprint server for biology · 2025Article
- Vertical DNA Nanostructure Arrays: Facilitating Functionalization on Macro-Scale Surfaces.ACS nano · 2025Article
- Recent Advances in DNA Origami-Enabled Optical Biosensors for Multi-Scenario Application.Nanomaterials (Basel, Switzerland) · 2024Review
- Recycling Materials for Sustainable DNA Origami Manufacturing.Nano letters · 2024Article
- Functionalizing DNA Origami by Triplex-Directed Site-Specific Photo-Cross-Linking.Journal of the American Chemical Society · 2024Article
- The motive forces in DNA-enabled nanomachinery.iScience · 2024Review
- An RNA origami robot that traps and releases a fluorescent aptamer.Science advances · 2024Article
- Cooperative control of a DNA origami force sensor.Scientific reports · 2024Article
- DNA origami: a tool to evaluate and harness transcription factors.Journal of molecular medicine (Berlin, Germany) · 2023Review
- Lab-on-a-DNA origami: nanoengineered single-molecule platforms.Chemical communications (Cambridge, England) · 2023Review
- Functionalizing DNA origami to investigate and interact with biological systems.Nature reviews. Materials · 2023Article
- Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate.International journal of molecular sciences · 2022Article
- Structural Studies of Eukaryotic RNA Polymerase I Using Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Massively Parallelized Molecular Force Manipulation with On-Demand Thermal and Optical Control.Journal of the American Chemical Society · 2021Article
- A nanoscale DNA force spectrometer capable of applying tension and compression on biomolecules.Nucleic acids research · 2021Article
- Emerging applications at the interface of DNA nanotechnology and cellular membranes: Perspectives from biology, engineering, and physics.APL bioengineering · 2020Review
- Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
Abstract
The TATA-binding protein (TBP) and a transcription factor (TF) IIB-like factor are important constituents of all eukaryotic initiation complexes. The reason for the emergence and strict requirement of the additional initiation factor Bdp1 in the RNA polymerase (RNAP) III system, however, remained elusive. A poorly studied aspect in this context is the effect of DNA strain arising from DNA compaction and transcriptional activity on initiation complex formation. We made use of a DNA origami-based force clamp to follow the assembly of human initiation complexes in the RNAP II and RNAP III systems at the single-molecule level under piconewton forces. We demonstrate that TBP-DNA complexes are force-sensitive and TFIIB is sufficient to stabilise TBP on a strained promoter. In contrast, Bdp1 is the pivotal component that ensures stable anchoring of initiation factors, and thus the polymerase itself, in the RNAP III system. Thereby, we offer an explanation for the crucial role of Bdp1 for the high transcriptional output of RNAP III.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.