ArticleNucleic acids research2012
Towards characterization of DNA structure under physiological conditions in vivo at the single-molecule level using single-pair FRET.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- tttrlib: modular software for integrating fluorescence spectroscopy, imaging, and molecular modeling.Bioinformatics (Oxford, England) · 2025Article
- RNA ensembles from in vitro to in vivo: Toward predictive models of RNA cellular function.Current opinion in structural biology · 2024Review
- Article
- Towards Profiling of the G-Quadruplex Targeting Drugs in the Living Human Cells Using NMR Spectroscopy.International journal of molecular sciences · 2021Article
- Compaction of RNA Duplexes in the Cell*.Angewandte Chemie (International ed. in English) · 2020Article
- From single bacterial cell imaging towardsEssays in biochemistry · 2019Review
- Investigation of higher-order RNA G-quadruplex structures in vitro and in living cells byNature protocols · 2018Article
- Toward dynamic structural biology: Two decades of single-molecule Förster resonance energy transfer.Science (New York, N.Y.) · 2018Review
- Fluorescent RNA cytosine analogue - an internal probe for detailed structure and dynamics investigations.Scientific reports · 2017Article
- High Precision FRET at Single-molecule Level for Biomolecule Structure Determination.Journal of visualized experiments : JoVE · 2017Article
- Watching cellular machinery in action, one molecule at a time.The Journal of cell biology · 2017Review
- Optimized delivery of fluorescently labeled proteins in live bacteria using electroporation.Histochemistry and cell biology · 2014Article
Corrections and comments
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6 authors.
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Abstract
Fluorescence resonance energy transfer (FRET) under in vivo conditions is a well-established technique for the evaluation of populations of protein bound/unbound nucleic acid (NA) molecules or NA hybridization kinetics. However, in vivo FRET has not been applied to in vivo quantitative conformational analysis of NA thus far. Here we explored parameters critical for characterization of NA structure using single-pair (sp)FRET in the complex cellular environment of a living Escherichia coli cell. Our measurements showed that the fluorophore properties in the cellular environment differed from those acquired under in vitro conditions. The precision for the interprobe distance determination from FRET efficiency values acquired in vivo was found lower (≈ 31%) compared to that acquired in diluted buffers (13%). Our numerical simulations suggest that despite its low precision, the in-cell FRET measurements can be successfully applied to discriminate among various structural models. The main advantage of the in-cell spFRET setup presented here over other established techniques allowing conformational analysis in vivo is that it allows investigation of NA structure in various cell types and in a native cellular environment, which is not disturbed by either introduced bulk NA or by the use of chemical transfectants.
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