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. 2012 Jan 10;2(12):957–972. doi: 10.1007/s13238-011-1118-y

Protein-protein complexation in bioluminescence

Maxim S Titushin 1, Yingang Feng 2, John Lee 3, Eugene S Vysotski 4, Zhi-Jie Liu 1,✉
PMCID: PMC4875246  PMID: 22231355

Abstract

In this review we summarize the progress made towards understanding the role of protein-protein interactions in the function of various bioluminescence systems of marine organisms, including bacteria, jellyfish and soft corals, with particular focus on methodology used to detect and characterize these interactions. In some bioluminescence systems, protein-protein interactions involve an “accessory protein” whereby a stored substrate is efficiently delivered to the bioluminescent enzyme luciferase. Other types of complexation mediate energy transfer to an “antenna protein” altering the color and quantum yield of a bioluminescence reaction. Spatial structures of the complexes reveal an important role of electrostatic forces in governing the corresponding weak interactions and define the nature of the interaction surfaces. The most reliable structural model is available for the protein-protein complex of the Ca2+-regulated photoprotein clytin and green-fluorescent protein (GFP) from the jellyfish Clytia gregaria, solved by means of Xray crystallography, NMR mapping and molecular docking. This provides an example of the potential strategies in studying the transient complexes involved in bioluminescence. It is emphasized that structural studies such as these can provide valuable insight into the detailed mechanism of bioluminescence.

Keywords: green-fluorescent protein (GFP), photoprotein, luciferase, lumazine protein, Förster resonance energy transfer (FRET), docking

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