ArticleProceedings of the National Academy of Sciences of the United States of America2012
Protein-flexibility mediated coupling between photoswitching kinetics and surrounding viscosity of a photochromic fluorescent protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Genetically-encoded temperature indicators for thermal biology.Biophysics and physicobiology · 2025Article
- Genetically encoded photo-switchable molecular sensors for optoacoustic and super-resolution imaging.Nature biotechnology · 2022Article
- Extra kinetic dimensions for label discrimination.Nature communications · 2022Article
- Toward photoswitchable electronic pre-resonance stimulated Raman probes.The Journal of chemical physics · 2021Article
- NMR Reveals Light-Induced Changes in the Dynamics of a Photoswitchable Fluorescent Protein.Biophysical journal · 2019Article
- Structural Evidence of Photoisomerization Pathways in Fluorescent Proteins.Journal of the American Chemical Society · 2019Article
- Role of Hydrogen Bonding in Green Fluorescent Protein-like Chromophore Emission.Scientific reports · 2019Article
- Directed evolution of excited state lifetime and brightness in FusionRed using a microfluidic sorter.Integrative biology : quantitative biosciences from nano to macro · 2018Article
- Mechanism and bottlenecks in strand photodissociation of split green fluorescent proteins (GFPs).Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Improved Fluorescent Protein Contrast and Discrimination by Optically Controlling Dark State Lifetimes.The journal of physical chemistry letters · 2017Article
- Article
- Dependence of fluorescent protein brightness on protein concentration in solution and enhancement of it.Scientific reports · 2016Article
- Applications of phototransformable fluorescent proteins for tracking the dynamics of cellular components.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2015Review
- Room temperature crystal structure of the fast switching M159T mutant of the fluorescent protein dronpa.Proteins · 2015Article
- Accounting for photophysical processes and specific signal intensity changes in fluorescence-detected sedimentation velocity.Analytical chemistry · 2014Article
- Phototransformable fluorescent proteins: which one for which application?Histochemistry and cell biology · 2014Review
- Quantitatively mapping cellular viscosity with detailed organelle information via a designed PET fluorescent probe.Scientific reports · 2014Article
- Article
- Photoswitchable fluorescent proteins: ten years of colorful chemistry and exciting applications.Current opinion in chemical biology · 2013Review
- Focal switching of photochromic fluorescent proteins enables multiphoton microscopy with superior image contrast.Biomedical optics express · 2012Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent advances in fluorescent proteins (FPs) have generated a remarkable family of optical highlighters with special light responses. Among them, Dronpa exhibits a unique capability of reversible light-regulated on-off switching. However, the environmental dependence of this photochromism is largely unexplored. Herein we report that the photoswitching kinetics of the chromophore inside Dronpa is actually slowed down by increasing medium viscosity outside Dronpa. This finding is a special example of an FP where the environment can exert a hydrodynamic effect on the internal chromophore. We attribute this effect to protein-flexibility mediated coupling where the chromophore's cis-trans isomerization during photoswitching is accompanied by conformational motion of a part of the protein β-barrel whose dynamics should be hindered by medium friction. Consistent with this mechanism, the photoswitching kinetics of Dronpa-3, a structurally more flexible mutant, is found to exhibit a more pronounced viscosity dependence. Furthermore, we mapped out spatial distributions of microviscosity in live cells experienced by a histone protein using the photoswitching kinetics of Dronpa-3 fusion as a contrast mechanism. This unique reporter should provide protein-specific information about the crowded intracellular environments by offering a genetically encoded microviscosity probe, which did not exist with normal FPs before.
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