Bioluminescent resonance energy transfer

(A) Principle of the BRET and BRET ² .
(B) Emission spectra of donor and acceptor for BRET and BRET ² .

The bioluminescence resonance energy transfer (Engl. Bioluminescence resonance energy transfer , shortly BRET ) is a physical process of the non radiative energy transfer , which on the Förster resonance energy transfer is based (FRET). In this process, bioluminescent energy is transferred without radiation to a fluorescent dye (acceptor fluorophore). Since the intensity of the bioluminescence resonance energy transfer depends, among other things, on the distance between the bioluminescence source and the acceptor fluorophore, bioluminescence resonance energy transfer is often used as an alternative to fluorescence resonance energy transfer as an "optical nanometer scale", particularly in biochemistry and cell biology . The enzyme Rluc , a luciferase from the sea feather species Renilla reniformis (common sea feather), using its substrate coelenterazine h and the yellow fluorescent protein YFP as an acceptor fluorophore are used as the bioluminescence source . A further development of this classic BRET method is the BRET ² method, which is based on the use of the substrate Coelenterazin 400a (DeepBlue C) and the acceptor GFP ² .

Individual evidence

↑ Pfleger KD, Eidne KA (2006): Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET). In: Nat. Methods. 3: 165-174. PMID 16489332 doi : 10.1038 / nmeth841
↑ Dionne P., Mireille C., Labonte A., Carter-Allen K., Houle B., Joly E., Taylor SC, Menard L. (2002): BRET2: Efficient energy transfer from Renilla Luciferase to GFP2 to measure protein –Protein interactions and intracellular signaling events in live cells. In: Luminescence Biotechnology: Instruments and Applications. (van Dyke K., van Dyke C., Woodfork K., ed), pp. 539-555, CRC Press, Boca Raton, USA.

[1] Pfleger KD, Eidne KA (2006): Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET). In: Nat. Methods. 3: 165-174. PMID 16489332 doi : 10.1038 / nmeth841

[2] Dionne P., Mireille C., Labonte A., Carter-Allen K., Houle B., Joly E., Taylor SC, Menard L. (2002): BRET2: Efficient energy transfer from Renilla Luciferase to GFP2 to measure protein –Protein interactions and intracellular signaling events in live cells. In: Luminescence Biotechnology: Instruments and Applications. (van Dyke K., van Dyke C., Woodfork K., ed), pp. 539-555, CRC Press, Boca Raton, USA.