Protein-protein complexation in bioluminescence  

作　　者：Maxim S.Titushin Yingang Feng John Lee Eugene S.Vysotski Zhi-Jie Liu 

机构地区：[1]National Laboratory of Biomacromolecules,Institute of Biophysics,Chinese Academy of Sciences,Beijing 100101,China [2]Qingdao Institute of Bioenergy and Bioprocess Technology,Chinese Academy of Sciences,Qingdao 266101,China [3]Department of Biochemistry and Molecular Biology,University of Georgia,Athens,GA 30602,USA [4]Laboratory of Photobiology,Institute of Biophysics Russian Academy of Sciences,Siberian Branch,Krasnoyarsk 660036,Russia

出　　处：《Protein & Cell》2011年第12期957-972,共16页蛋白质与细胞（英文版）

基　　金：by“Fellowship for Young International Scientists”of Chinese Academy of Sciences;This work was supported by the National Natural Science Foundation of China(Grant Nos:30870483,31070660,31021062 and 81072449);Ministry of Science and Technology of China(Nos.2009DFB30310,2009CB918803 and 2011CB911103);CAS Research Grants(Nos.YZ200839 and KSCX2-EW-J-3).

摘　　要：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.

关 键 词：green-fluorescent protein(GFP) PHOTOPROTEIN LUCIFERASE lumazine protein Förster resonance energy transfer(FRET) DOCKING 

分 类 号：O62[理学—有机化学]