Recombinant Ca2+-regulated photoproteins of ctenophores: current knowledge and application prospects

被引:14
作者
Burakova, Lyudmila P. [1 ]
Vysotski, Eugene S. [1 ]
机构
[1] RAS, Fed Res Ctr, Krasnoyarsk Sci Ctr, Photobiol Lab,Inst Biophys,SB, Krasnoyarsk 660036, Russia
基金
俄罗斯基础研究基金会;
关键词
Bioluminescence; Coelenterazine; Photoinactivation; Intracellular calcium; CALCIUM-ACTIVATED PHOTOPROTEINS; LIGHT-SENSITIVE PHOTOPROTEIN; CRYSTAL-STRUCTURES; SEQUENCE-ANALYSIS; COELENTERAZINE-BINDING; CA2+-BINDING LOOPS; MNEMIOPSIS-LEIDYI; SPATIAL STRUCTURE; BEROE ABYSSICOLA; QUANTUM YIELD;
D O I
10.1007/s00253-019-09939-0
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Bright bioluminescence of ctenophores is conditioned by Ca2+-regulated photoproteins. Although they share many properties characteristic of hydromedusan Ca2+-regulated photoproteins responsible for light emission of marine animals belonging to phylum Cnidaria, a substantial distinction still exists. The ctenophore photoproteins appeared to be extremely sensitive to light-they lose the ability for bioluminescence on exposure to light over the entire absorption spectrum. Inactivation is irreversible because keeping the inactivated photoprotein in the dark does not recover its activity. The capability to emit light can be restored only by incubation of inactivated photoprotein with coelenterazine in the dark at alkaline pH in the presence of oxygen. Although these photoproteins were discovered many years ago, only the cloning of cDNAs encoding these unique bioluminescent proteins in the early 2000s has provided a new impetus for their studies. To date, cDNAs encoding Ca2+-regulated photoproteins from four different species of luminous ctenophores have been cloned. The amino acid sequences of ctenophore photoproteins turned out to completely differ from those of hydromedusan photoproteins (identity less than 29%) though also similar to them having three EF-hand Ca2+-binding sites. At the same time, these photoproteins reveal the same two-domain scaffold characteristic of hydromedusan photoproteins. This review is an attempt to systemize and critically evaluate the data scattered through various articles regarding the structural features of recombinant light-sensitive Ca2+-regulated photoproteins of ctenophores and their bioluminescent and physicochemical properties as well as to compare them with those of hydromedusan photoproteins. In addition, we also discuss the prospects of their biotechnology applications.
引用
收藏
页码:5929 / 5946
页数:18
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