ArticleProceedings of the National Academy of Sciences of the United States of America2008
Single-molecule tracking of mRNA exiting from RNA polymerase II.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 110 citations in OpenAlex.
- Illuminating biomolecular assemblies in gene regulation.Biophysical reviews · 2025Review
- Single-molecule imaging for investigating the transcriptional control.Molecules and cells · 2025Review
- Single-molecule reconstruction of eukaryotic factor-dependent transcription termination.Nature communications · 2024Article
- An automated single-molecule FRET platform for high-content, multiwell plate screening of biomolecular conformations and dynamics.Nature communications · 2023Article
- Mechanism of transcription modulation by the transcription-repair coupling factor.Nucleic acids research · 2022Article
- Coupling of Transcription and Translation in Archaea: Cues From the Bacterial World.Frontiers in microbiology · 2021Article
- Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine.Nature communications · 2019Article
- Chemoselective Dual Labeling of Native and Recombinant Proteins.Bioconjugate chemistry · 2018Article
- Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.eLife · 2017Article
- Structural Information from Single-molecule FRET Experiments Using the Fast Nano-positioning System.Journal of visualized experiments : JoVE · 2017Article
- Single-molecule FRET-Rosetta reveals RNA structural rearrangements during human telomerase catalysis.RNA (New York, N.Y.) · 2017Article
- Single molecule microscopy reveals mechanistic insight into RNA polymerase II preinitiation complex assembly and transcriptional activity.Nucleic acids research · 2016Article
- The yeast transcription elongation factor Spt4/5 is a sequence-specific RNA binding protein.Protein science : a publication of the Protein Society · 2016Article
- Biochemical Analysis of Yeast Suppressor of Ty 4/5 (Spt4/5) Reveals the Importance of Nucleic Acid Interactions in the Prevention of RNA Polymerase II Arrest.The Journal of biological chemistry · 2016Article
- Complete architecture of the archaeal RNA polymerase open complex from single-molecule FRET and NPS.Nature communications · 2015Article
- A starting point for fluorescence-based single-molecule measurements in biomolecular research.Molecules (Basel, Switzerland) · 2014Review
- A genetic assay for transcription errors reveals multilayer control of RNA polymerase II fidelity.PLoS genetics · 2014Article
- Capsid protein VP4 of human rhinovirus induces membrane permeability by the formation of a size-selective multimeric pore.PLoS pathogens · 2014Article
- Coordinated DNA dynamics during the human telomerase catalytic cycle.Nature communications · 2014Article
- Coliphage HK022 Nun protein inhibits RNA polymerase translocation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-pair fluorescence resonance energy transfer was used to track RNA exiting from RNA polymerase II (Pol II) in elongation complexes. Measuring the distance between the RNA 5' end and three known locations within the elongation complex allows us determine its position by means of triangulation. RNA leaves the polymerase active center cleft via the previously proposed exit tunnel and then disengages from the enzyme surface. When the RNA reaches lengths of 26 and 29 nt, its 5' end associates with Pol II at the base of the dock domain. Because the initiation factor TFIIB binds to the dock domain and exit tunnel, exiting RNA may prevent TFIIB reassociation during elongation. RNA further extends toward the linker connecting to the polymerase C-terminal repeat domain (CTD), which binds the 5'-capping enzyme and other RNA processing factors.
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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.