Previous research has demonstrated that ATP has an effect on YFP/CFP fluorescence intensities observed with CFP-YFP-based FRET sensors. This phenomenon was thought to take place by quenching during the energy transfer step, potentially coupled to energy-induced charge displacement in the phosphate groups.
Using different donor and acceptor pairs, the study found that changes in ATP concentrations affected only the CFP-YFP-based FRET sensors. Using time-resolved fluorescence spectroscopy, the results demonstrate that the effect of ATP is not due to quenching at the energy transfer step, but more likely by a direct interaction of ATP with the positively charged histidine residue at position 148 (His148) of CFP. Gaining a better understanding of the emissive properties of fluorescent proteins might be important for making improved designs of FRET sensors.
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Borst JW, Willemse M, Slijkhuis R, van der Krogt G, Laptenok SP, Jalink K, Wieringa B and Fransen JAM:
ATP Changes the Fluorescence Lifetime of Cyan Fluorescent Protein via an Interaction with His148
PLoS ONE 5 (11): e13862 (2010); doi: 10.1371/journal.pone.0013862
