BRET, Bioluminescent resonance energy

Pfleger, K. D. and Eidne, K. A. (2006). Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET). Nat. Methods 3, 165-74. 

Xu, X., Soutto, M., Xie, Q., Servick, S., Subramanian, C., von Arnim, A. G. and Johnson, C. H. (2007). Imaging protein interactions with bioluminescence resonance energy transfer (BRET) in plant and mammalian cells and tissues. Proc. Natl. Acad. Sci. USA 104, 10264-9. 

Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. USA 97, 3684-3689. 

Angers, S., Salahpour, A., Joly, E., Hilairet, S., Chelsky, D., Dennis, M. and Bouvier, M. (2000). Detection of b2 -adrenergic receptors dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proceedings of the National Academy of Sciences, USA, 97, 3684-3689. 

Like FRET, bioluminescence resonance energy transfer (BRET) is based on non-radiative energy transfer between a donor and an acceptor. However, in BRET, the donor is a luminescent molecule, excited by the enzyme Renilla Luciferase (Rluc), and not a fluorescent molecule. The BRET acceptor can be a fluorescent protein like green fluorescent protein (GFP) or YFR If the enzyme and the fluorescent protein are in close proximity (d < 10 nm), an energy transfer will occur between the Rluc substrate (coelanterazine) and the fluorescent protein, leading to emission from the later. 

There are two main types of RET, bioluminescence resonance energy transfer (BRET) and fluorescence resonance energy transfer (FRET). In the former, the donor molecule is luminescent (27,28)... 

---