ArticleProceedings of the National Academy of Sciences of the United States of America2011
Protein induced fluorescence enhancement as a single molecule assay with short distance sensitivity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 155 papers.
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Who cites it
155 citing papers in PubMed.
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- Multiplexed single-molecule characterization at the library scale.Nature protocols · 2026Review
- Opposing roles of two R-loop associated G-quadruplexes in tuning transcription activity.Nucleic acids research · 2025Article
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- High-resolution fleezers reveal duplex opening and stepwise assembly by an oligomer of the DEAD-box helicase Ded1p.Nature communications · 2025Article
- Single-molecule DNA-flow stretching assay as a versatile hybrid tool for investigating DNA-protein interactions.BMB reports · 2025Review
- Single turnover transient state kinetics reveals processive protein unfolding catalyzed byeLife · 2024Article
- Protection of the Telomeric Junction by the Shelterin Complex.Journal of the American Chemical Society · 2024Article
- Protection of the Telomeric Junction by the Shelterin Complex.bioRxiv : the preprint server for biology · 2024Article
- Binding Behavior of Human Hepatoma-Derived Growth Factor onThe journal of physical chemistry. B · 2024Article
- Single-molecule fluorescence multiplexing by multi-parameter spectroscopic detection of nanostructured FRET labels.Nature nanotechnology · 2024Article
- REAL-TIME VISUALIZATION OF SPLICEOSOME ASSEMBLY REVEALS BASIC PRINCIPLES OF SPLICE SITE SELECTION.bioRxiv : the preprint server for biology · 2024Article
95 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors.
Funding
Abstract
Single-molecule FRET has been widely used for monitoring protein-nucleic acids interactions. Direct visualization of the interactions, however, often requires a site-specific labeling of the protein, which can be circuitous and inefficient. In addition, FRET is insensitive to distance changes in the 0-3-nm range. Here, we report a systematic calibration of a single molecule fluorescence assay termed protein induced fluorescence enhancement. This method circumvents protein labeling and displays a marked distance dependence below the 4-nm distance range. The enhancement of fluorescence is based on the photophysical phenomenon whereby the intensity of a fluorophore increases upon proximal binding of a protein. Our data reveals that the method can resolve as small as a single base pair distance at the extreme vicinity of the fluorophore, where the enhancement is maximized. We demonstrate the general applicability and distance sensitivity using (a) a finely spaced DNA ladder carrying a restriction site for BamHI, (b) RNA translocation by DExH enzyme RIG-I, and (c) filament dynamics of RecA on single-stranded DNA. The high spatio-temporal resolution data and sensitivity to short distances combined with the ability to bypass protein labeling makes this assay an effective alternative or a complement to FRET.
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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.