Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells

Müller S, Galliardt H, Schneider J, Barisas BG, Seidel T (2013)
Frontiers in Plant Science 4: 413.

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Abstract
Förster resonance energy transfer (FRET) describes excitation energy exchange between two adjacent molecules typically in distances ranging from 2 to 10 nm. The process depends on dipole-dipole coupling of the molecules and its probability of occurrence cannot be proven directly. Mostly, fluorescence is employed for quantification as it represents a concurring process of relaxation of the excited singlet state S1 so that the probability of fluorescence decreases as the probability of FRET increases. This reflects closer proximity of the molecules or an orientation of donor and acceptor transition dipoles that facilitates FRET. Monitoring sensitized emission by 3-Filter-FRET allows for fast image acquisition and is suitable for quantifying FRET in dynamic systems such as living cells. In recent years, several calibration protocols were established to overcome to previous difficulties in measuring FRET-efficiencies. Thus, we can now obtain by 3-filter FRET FRET-efficiencies that are comparable to results from sophisticated fluorescence lifetime measurements. With the discovery of fluorescent proteins and their improvement toward spectral variants and usability in plant cells, the tool box for in vivo FRET-analyses in plant cells was provided and FRET became applicable for the in vivo detection of protein-protein interactions and for monitoring conformational dynamics. The latter opened the door toward a multitude of FRET-sensors such as the widely applied Ca(2+)-sensor Cameleon. Recently, FRET-couples of two fluorescent proteins were supplemented by additional fluorescent proteins toward FRET-cascades in order to monitor more complex arrangements. Novel FRET-couples involving switchable fluorescent proteins promise to increase the utility of FRET through combination with photoactivation-based super-resolution microscopy.
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Müller S, Galliardt H, Schneider J, Barisas BG, Seidel T. Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells. Frontiers in Plant Science. 2013;4: 413.
Müller, S., Galliardt, H., Schneider, J., Barisas, B. G., & Seidel, T. (2013). Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells. Frontiers in Plant Science, 4: 413.
Müller, S., Galliardt, H., Schneider, J., Barisas, B. G., and Seidel, T. (2013). Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells. Frontiers in Plant Science 4:413.
Müller, S., et al., 2013. Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells. Frontiers in Plant Science, 4: 413.
S. Müller, et al., “Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells”, Frontiers in Plant Science, vol. 4, 2013, : 413.
Müller, S., Galliardt, H., Schneider, J., Barisas, B.G., Seidel, T.: Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells. Frontiers in Plant Science. 4, : 413 (2013).
Müller, Sara, Galliardt, Helena, Schneider, Jessica, Barisas, B. George, and Seidel, Thorsten. “Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells”. Frontiers in Plant Science 4 (2013): 413.
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Fluorescent proteins as genetically encoded FRET biosensors in life sciences.
Hochreiter B, Garcia AP, Schmid JA., Sensors (Basel) 15(10), 2015
PMID: 26501285
ClearSee: a rapid optical clearing reagent for whole-plant fluorescence imaging.
Kurihara D, Mizuta Y, Sato Y, Higashiyama T., Development 142(23), 2015
PMID: 26493404
Understanding FRET as a research tool for cellular studies.
Shrestha D, Jenei A, Nagy P, Vereb G, Szollosi J., Int J Mol Sci 16(4), 2015
PMID: 25815593
Two-photon imaging with longer wavelength excitation in intact Arabidopsis tissues.
Mizuta Y, Kurihara D, Higashiyama T., Protoplasma 252(5), 2015
PMID: 25588923
Functional imaging in living plants-cell biology meets physiology.
Littlejohn GR, Meckel T, Schwarzlander M, Costa A., Front Plant Sci 5(), 2014
PMID: 25566307
Noninvasive high-throughput single-cell analysis of HIV protease activity using ratiometric flow cytometry.
Gaber R, Majerle A, Jerala R, Bencina M., Sensors (Basel) 13(12), 2013
PMID: 24287545

130 References

Data provided by Europe PubMed Central.

Fluorescence fluctuation spectroscopy of mCherry in living cells.
Wu B, Chen Y, Muller JD., Biophys. J. 96(6), 2009
PMID: 19289064
The molecular structure of green fluorescent protein.
Yang F, Moss LG, Phillips GN Jr., Nat. Biotechnol. 14(10), 1996
PMID: 9631087
Photobleaching-corrected FRET efficiency imaging of live cells.
Zal T, Gascoigne NR., Biophys. J. 86(6), 2004
PMID: 15189889
Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP.
Zapata-Hommer O, Griesbeck O., BMC Biotechnol. 3(), 2003
PMID: 12769828

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