Molecular cloning and expression of the cDNAs encoding luciferin-regenerating enzyme from Luciola cruciata and Luciola lateralis

Gomi, Keiko; Hirokawa, Kozo; Kajiyama, Naoki

doi:10.1016/s0378-1119(02)00764-3

Cited by 32 publications

(42 citation statements)

References 30 publications

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“…The only clear evidence is that cysteine is a synthetic unit of firefly luciferin [63,66]. In 2001, a luciferin-regeneration enzyme of firefly luciferin from oxyluciferin was reported [67,68]. Later, it was found that the protein has high amino acid sequence similarity to the senescence marker protein-30, that is a hydrolase, gluconolactonase (EC.…”

Section: Biosynthesis Of Firefly Luciferin In Vivomentioning

confidence: 99%

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Inouye

2009

Cell. Mol. Life Sci.

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Firefly luciferase is a member of the acyl-adenylate/thioester-forming superfamily of enzymes and catalyzes the oxidation of firefly luciferin with molecular oxygen to emit light. Knowledge of the luminescence mechanism catalyzed by firefly luciferase has been gathered, leading to the discovery of a novel catalytic function of luciferase. Recently, we demonstrated that firefly luciferase has a catalytic function of fatty acyl-CoA synthesis from fatty acids in the presence of ATP, Mg(2+) and coenzyme A. Based on identification of fatty acyl-CoA genes in firefly, Drosophila, and non-luminous click beetles, we then proposed that the evolutionary origin of firefly luciferase is a fatty acyl-CoA synthetase in insects. Further, we succeeded in converting the fatty acyl-CoA synthetase of non-luminous insects into functional luciferase showing luminescence activity by site-directed mutagenesis.

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Section: Biosynthesis Of Firefly Luciferin In Vivomentioning

confidence: 99%

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Inouye

2009

Cell. Mol. Life Sci.

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“…Regucalcin was discovered in 1978 as a Ca 2+ -binding protein that does not contain an EF-hand motif of Ca 2+ -binding domain, and which is involved in regulation of intracellular signaling pathways [17,67]. Using the next similar sequence from S. cerevisiae, a 105 kDa protein known to be associated with the polyadenylation factor from S. cerevisiae, as outgroup, it can be seen that the sponge luciferin-regenerating enzyme falls in the group of those luciferin-recycling enzymes [32,36]; Fig. 8B.…”

Section: Determination Of Activity Of Recombinant Luciferasementioning

confidence: 99%

“…In turn, oxyluciferin displays a strong inhibitory effect on the firefly luciferase reaction in a competitive manner [33]. Hence, intensive screening for luciferin-regenerating system(s) started [34,35] and resulted in the identification and molecular cloning of a luciferin-regenerating enzyme from P. pyralis and related insects [32,36,37]. This enzyme converts oxyluciferin in the presence of d-cysteine to the intermediate 2-cyano-6-hydroxybenzothiazole [32].…”

Section: Introductionmentioning

confidence: 99%

Luciferase a light source for the silica-based optical waveguides (spicules) in the demosponge Suberites domuncula

Müller

Kasueske

Wang³

et al. 2008

Cell. Mol. Life Sci.

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Two classes of sponges (animal phylum Porifera) possess a siliceous skeleton which is composed of spicules. Studying the optical fiber-mechanical properties of large spicules from hexactinellid sponges (> 5 cm) it was demonstrated that they are effective light-collecting optical fibers. Here, we report that the demosponge Suberites domuncula is provided with a biosensor system composed of the (organic) light producing luciferase and the (inorganic) light transducing silica spicules. The light transmission feature of these smaller spicules (200 microm) has been demonstrated and the ability of sponge tissue to generate light has been proven. Screening for a luciferase gene in S. domuncula was successful; the recombinant luciferase was prepared and shown to be bioactive. The luciferase protein is abundantly present in the close neighborhood of the spicules. The expression of the luciferase gene is under the control of light.

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“…Within the Lampyridae, Photinus and Luciola species are probably the most phylogenetically divergent genera (26,76) and thus it is likely that this enzyme is found in all bioluminescent members of this family. The firefly LRE amino acid sequences share 56-57% identity with each other but, more interestingly, appear to be related to a group of senescence marker proteins (SMP-30) and anterior fat proteins (AFP) (77,78). Thus, LRE may have a dual function within the beetle or may have recently evolved to develop a specific role in bioluminescence.…”

Section: Structure and Biosynthesis Of Beetle Luciferinmentioning

confidence: 99%

Evolution of beetle bioluminescence: the origin of beetle luciferin

2004

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Bioluminescence, the conversion of chemical energy into light in living organisms, is dependent on two principal components, an enzyme luciferase and the substrate luciferin. In beetles, the enzyme luciferase has been extensively studied, with significant enzymological, sequence and structural data now available. Furthermore, the enzyme has been employed in a remarkable number of important applications, from microbial detection and medical imaging to GM gene expression studies. However, there is little information regarding the biosynthesis of beetle luciferin, and here we review the literature and speculate as to its evolutionary origins. Luciferin consists of a benzothiazole moiety attached to a thiazole carboxylic acid moiety, the former being rarely observed in nature but the latter being observed in a broad range of biologically derived molecules. Benzothiazoles are, however, observed in melanogenesis and we speculate as to whether this may be relevant to the understanding of luciferin biosynthesis in beetles. This review examines recent novel insights into beetle luciferin recycling and we assess a range of possible biosynthetic mechanisms.

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Molecular cloning and expression of the cDNAs encoding luciferin-regenerating enzyme from Luciola cruciata and Luciola lateralis

Cited by 32 publications

References 30 publications

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions

Luciferase a light source for the silica-based optical waveguides (spicules) in the demosponge Suberites domuncula

Evolution of beetle bioluminescence: the origin of beetle luciferin

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