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Yuichi Oba - One of the best experts on this subject based on the ideXlab platform.
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one pot non enzymatic formation of Firefly Luciferin in a neutral buffer from p benzoquinone and cysteine
Scientific Reports, 2016Co-Authors: Shusei Kanie, Yuichi Oba, Makoto Ojika, Toshio NishikawaAbstract:Firefly Luciferin, the substrate for the bioluminescence reaction of luminous beetles, possesses a benzothiazole ring, which is rare in nature. Here, we demonstrate a novel one-pot reaction to give Firefly Luciferin in a neutral buffer from p-benzoquinone and cysteine without any synthetic reagents or enzymes. The formation of Firefly Luciferin was low in yield in various neutral buffers, whereas it was inhibited or completely prevented in acidic or basic buffers, in organic solvents, or under a nitrogen atmosphere. Labelling analysis of the Firefly Luciferin using stable isotopic cysteines showed that the benzothiazole ring was formed via the decarboxylation and carbon-sulfur bond rearrangement of cysteine. These findings imply that the biosynthesis of Firefly Luciferin can be developed/evolved from the non-enzymatic production of Firefly Luciferin using common primary biosynthetic units, p-benzoquinone and cysteine.
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Biosynthesis of Firefly Luciferin in Adult Lantern: Decarboxylation of L-Cysteine Is a Key Step for Benzothiazole Ring Formation in Firefly Luciferin Synthesis
2013Co-Authors: Yuichi Oba, Makoto Ojika, Shusei Kanie, Naoki Yoshida, Satoshi InouyeAbstract:Background: Bioluminescence in fireflies and click beetles is produced by a luciferase-Luciferin reaction. The luminescence property and protein structure of Firefly luciferase have been investigated, and its cDNA has been used for various assay systems. The chemical structure of Firefly Luciferin was identified as the D-form in 1963 and studies on the biosynthesis of Firefly Luciferin began early in the 1970’s. Incorporation experiments using 14C-labeled compounds were performed, and cysteine and benzoquinone/hydroquinone were proposed to be biosynthetic component for Firefly Luciferin. However, there have been no clear conclusions regarding the biosynthetic components of Firefly Luciferin over 30 years. Methodology/Principal Findings: Incorporation studies were performed by injecting stable isotope-labeled compounds, including L-[U-13C3]-cysteine, L-[1-13C]-cysteine, L-[3-13C]-cysteine, 1,4-[D6]-hydroquinone, and p-[2,3,5,6-D]-benzoquinone, into the adult lantern of the living Japanese Firefly Luciola lateralis. After extracting Firefly Luciferin from the lantern, the incorporation of stable isotope-labeled compounds into Firefly Luciferin was identified by LC/ESI-TOF-MS. The positions of the stable isotope atoms in Firefly Luciferin were determined by the mass fragmentation of Firefly Luciferin. Conclusions: We demonstrated for the first time that D- and L-Firefly Luciferins are biosynthesized in the lantern of the adult Firefly from two L-cysteine molecules with p-benzoquinone/1,4-hydroquinone, accompanied by the decarboxylation of L
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Biosynthesis of Firefly Luciferin in Adult Lantern: Decarboxylation of L-Cysteine is a Key Step for Benzothiazole Ring Formation in Firefly Luciferin Synthesis
2013Co-Authors: Yuichi Oba, Makoto Ojika, Shusei Kanie, Naoki Yoshida, Satoshi InouyeAbstract:BackgroundBioluminescence in fireflies and click beetles is produced by a luciferase-Luciferin reaction. The luminescence property and protein structure of Firefly luciferase have been investigated, and its cDNA has been used for various assay systems. The chemical structure of Firefly Luciferin was identified as the D-form in 1963 and studies on the biosynthesis of Firefly Luciferin began early in the 1970’s. Incorporation experiments using 14C-labeled compounds were performed, and cysteine and benzoquinone/hydroquinone were proposed to be biosynthetic component for Firefly Luciferin. However, there have been no clear conclusions regarding the biosynthetic components of Firefly Luciferin over 30 years.Methodology/Principal FindingsIncorporation studies were performed by injecting stable isotope-labeled compounds, including L-[U-13C3]-cysteine, L-[1-13C]-cysteine, L-[3-13C]-cysteine, 1,4-[D6]-hydroquinone, and p-[2,3,5,6-D]-benzoquinone, into the adult lantern of the living Japanese Firefly Luciola lateralis. After extracting Firefly Luciferin from the lantern, the incorporation of stable isotope-labeled compounds into Firefly Luciferin was identified by LC/ESI-TOF-MS. The positions of the stable isotope atoms in Firefly Luciferin were determined by the mass fragmentation of Firefly Luciferin.ConclusionsWe demonstrated for the first time that D- and L-Firefly Luciferins are biosynthesized in the lantern of the adult Firefly from two L-cysteine molecules with p-benzoquinone/1,4-hydroquinone, accompanied by the decarboxylation of L-cysteine.
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Mass spectrum of D-Firefly Luciferin by ESI-TOF-MS analysis.
2013Co-Authors: Yuichi Oba, Makoto Ojika, Shusei Kanie, Naoki Yoshida, Satoshi InouyeAbstract:A. The structure of D-Firefly Luciferin and the predicted mass fragment ions. The parent ion of D-Luciferin at m/z 281 (M+H)+ (a), and its fragment ions at m/z 235 (b) and 177 (c). B. ESI-TOF-MS analysis of synthetic D-Firefly Luciferin.
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Proposed biosynthetic pathway of Firefly Luciferin in the lantern of adult Firefly.
2013Co-Authors: Yuichi Oba, Makoto Ojika, Shusei Kanie, Naoki Yoshida, Satoshi InouyeAbstract:Proposed biosynthetic pathway of Firefly Luciferin in the lantern of adult Firefly.
Darrin T Schultz - One of the best experts on this subject based on the ideXlab platform.
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laboratory culture of the california sea Firefly vargula tsujii ostracoda cypridinidae developing a model system for the evolution of marine bioluminescence
Scientific Reports, 2020Co-Authors: Jessica A Goodheart, Geetanjali Minsky, Mira N Brynjegardbialik, Michael S Drummond, David J Munoz, Timothy R Fallon, Darrin T SchultzAbstract:Bioluminescence, or the production of light by living organisms via chemical reaction, is widespread across Metazoa. Laboratory culture of bioluminescent organisms from diverse taxonomic groups is important for determining the biosynthetic pathways of bioluminescent substrates, which may lead to new tools for biotechnology and biomedicine. Some bioluminescent groups may be cultured, including some cnidarians, ctenophores, and brittle stars, but those use luminescent substrates (Luciferins) obtained from their diets, and therefore are not informative for determination of the biosynthetic pathways of the Luciferins. Other groups, including terrestrial fireflies, do synthesize their own Luciferin, but culturing them is difficult and the biosynthetic pathway for Firefly Luciferin remains unclear. An additional independent origin of endogenous bioluminescence is found within ostracods from the family Cypridinidae, which use their luminescence for defense and, in Caribbean species, for courtship displays. Here, we report the first complete life cycle of a luminous ostracod (Vargula tsujii Kornicker & Baker, 1977, the California Sea Firefly) in the laboratory. We also describe the late-stage embryogenesis of Vargula tsujii and discuss the size classes of instar development. We find embryogenesis in V. tsujii ranges from 25-38 days, and this species appears to have five instar stages, consistent with ontogeny in other cypridinid lineages. We estimate a complete life cycle at 3-4 months. We also present the first complete mitochondrial genome for Vargula tsujii. Bringing a luminous ostracod into laboratory culture sets the stage for many potential avenues of study, including learning the biosynthetic pathway of cypridinid Luciferin and genomic manipulation of an autogenic bioluminescent system.
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laboratory culture of the california sea Firefly vargula tsujii ostracoda cypridinidae developing a model system for the evolution of marine bioluminescence
bioRxiv, 2019Co-Authors: Jessica A Goodheart, Geetanjali Minsky, Mira N Brynjegardbialik, Michael S Drummond, David J Munoz, Timothy R Fallon, Darrin T Schultz, Jingke Weng, Elizabeth TorresAbstract:Bioluminescence, or the production of light by living organisms via chemical reaction, is widespread across Metazoa. Culturing bioluminescent organisms from diverse taxonomic groups is important for determining the biosynthetic pathways of bioluminescent substrates, which may lead to new tools for biotechnology and biomedicine. Although some previously cultured luminescent groups represent independent origins of bioluminescence, cnidarians, ctenophores, and brittle stars use luminescent substrates (Luciferins) obtained from their diets, and therefore are not informative for determination of the biosynthethic pathways of the Luciferins. Terrestrial fireflies do synthesize their own Luciferin, but the biosynthetic pathway for Firefly Luciferin remains unclear. An additional independent origin of endogenous bioluminescence is found within ostracods from the family Cypridinidae, which use their luminescence for defense and, in Caribbean species, for courtship displays. Here, we report the first complete life cycle of a luminous ostracod (Vargula tsujii, the California Sea Firefly) in the laboratory. We also describe the embryonic development of Vargula tsujii and discuss the size classes of instar development. We find embryogenesis in V. tsujii ranges between 25-38 days, and this species appears to have five instar stages, consistent with ontogeny in other cypridinid lineages. We estimate a complete life cycle at 3-4 months. We present the first complete mitochondrial genome for Vargula tsujii. Finally, we find no evidence of significant population genetic structure or cryptic species throughout the southern California range of V. tsujii. Bringing a luminous ostracod into laboratory culture sets the stage for many potential avenues of study, including the biosynthetic pathway of cypridinid Luciferin and genomic manipulation of an autogenic bioluminescent system.
Bruce R. Branchini - One of the best experts on this subject based on the ideXlab platform.
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novel heterocyclic analogues of Firefly Luciferin
Biochemistry, 2012Co-Authors: Carolyn C Woodroofe, Tara L Southworth, Curran E Behney, Poncho Meisenheimer, Dieter Klaubert, Yumi Kovic, Justin C Rosenberg, Bruce R. BranchiniAbstract:Five novel Firefly Luciferin analogues in which the benzothiazole ring system of the natural substrate was replaced with benzimidazole, benzofuran, benzothiophene, benzoxazole, and indole were synthesized. The fluorescence, bioluminescence, and kinetic properties of the compounds were evaluated with recombinant Photinus pyralis wild type luciferase. With the exception of indole, all of the substrates containing heterocycle substitutions produced readily measurable flashes of light with luciferase. Compared to that of Luciferin, the intensities ranged from 0.3 to 4.4% in reactions with varying pH optima and times to reach maximal intensity. The heteroatom changes influenced both the fluorescence and bioluminescence emission spectra, which displayed maxima of 479–528 and 518–574 nm, respectively. While there were some interesting trends in the spectroscopic and bioluminescence properties of this group of structurally similar substrate analogues, the most significant findings were associated with the benzoth...
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Novel Heterocyclic Analogues of Firefly Luciferin
2012Co-Authors: Carolyn C Woodroofe, Tara L Southworth, Curran E Behney, Poncho Meisenheimer, Dieter Klaubert, Yumi Kovic, Justin C Rosenberg, Bruce R. BranchiniAbstract:Five novel Firefly Luciferin analogues in which the benzothiazole ring system of the natural substrate was replaced with benzimidazole, benzofuran, benzothiophene, benzoxazole, and indole were synthesized. The fluorescence, bioluminescence, and kinetic properties of the compounds were evaluated with recombinant Photinus pyralis wild type luciferase. With the exception of indole, all of the substrates containing heterocycle substitutions produced readily measurable flashes of light with luciferase. Compared to that of Luciferin, the intensities ranged from 0.3 to 4.4% in reactions with varying pH optima and times to reach maximal intensity. The heteroatom changes influenced both the fluorescence and bioluminescence emission spectra, which displayed maxima of 479–528 and 518–574 nm, respectively. While there were some interesting trends in the spectroscopic and bioluminescence properties of this group of structurally similar substrate analogues, the most significant findings were associated with the benzothiophene-containing compound. This synthetic substrate produced slow decay glow kinetics that increased the total light-based specific activity of luciferase more than 4-fold versus the Luciferin value. Moreover, over the pH range of 6.2–9.4, the emission maximum is 523 nm, an unusual 37 nm blue shift compared to that of the natural substrate. The extraordinary bioluminescence properties of the benzothiophene Luciferin should translate into greater sensitivity for analyte detection in a wide variety of luciferase-based applications
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an alternative mechanism of bioluminescence color determination in Firefly luciferase
Biochemistry, 2004Co-Authors: Bruce R. Branchini, Tara L Southworth, Martha H Murtiashaw, Rachelle A Magyar, Susan A Gonzalez, Maria C Ruggiero, Justin G StrohAbstract:Beetle luciferases (including those of the Firefly) use the same Luciferin substrate to naturally display light ranging in color from green (λmax ∼530 nm) to red (λmax ∼635 nm). In a recent communication, we reported (Branchini, B. R., Murtiashaw, M. H., Magyar, R. A., Portier, N. C., Ruggiero, M. C., and Stroh, J. G. (2002) J. Am. Chem. Soc. 124, 2112−2113) that the synthetic adenylate of Firefly Luciferin analogue d-5,5-dimethylLuciferin was transformed into the emitter 5,5-dimethyloxyLuciferin in bioluminescence reactions catalyzed by luciferases from Photinus pyralis and the click beetle Pyrophorus plagiophthalamus. 5,5-DimethyloxyLuciferin is constrained to exist in the keto form and fluoresces mainly in the red. However, bioluminescence spectra revealed that green light emission was produced by the Firefly enzyme, and red light was observed with the click beetle protein. These results, augmented with steady-state kinetic studies, were taken as experimental support for mechanisms of Firefly biolumine...
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an alternative mechanism of bioluminescence color determination in Firefly luciferase
Biochemistry, 2004Co-Authors: Bruce R. Branchini, Tara L Southworth, Martha H Murtiashaw, Rachelle A Magyar, Susan A Gonzalez, Maria C Ruggiero, Justin G StrohAbstract:Beetle luciferases (including those of the Firefly) use the same Luciferin substrate to naturally display light ranging in color from green (lambda(max) approximately 530 nm) to red (lambda(max) approximately 635 nm). In a recent communication, we reported (Branchini, B. R., Murtiashaw, M. H., Magyar, R. A., Portier, N. C., Ruggiero, M. C., and Stroh, J. G. (2002) J. Am. Chem. Soc. 124, 2112-2113) that the synthetic adenylate of Firefly Luciferin analogue D-5,5-dimethylLuciferin was transformed into the emitter 5,5-dimethyloxyLuciferin in bioluminescence reactions catalyzed by luciferases from Photinus pyralis and the click beetle Pyrophorus plagiophthalamus. 5,5-DimethyloxyLuciferin is constrained to exist in the keto form and fluoresces mainly in the red. However, bioluminescence spectra revealed that green light emission was produced by the Firefly enzyme, and red light was observed with the click beetle protein. These results, augmented with steady-state kinetic studies, were taken as experimental support for mechanisms of Firefly bioluminescence color that require only a single keto form of oxyLuciferin. We report here the results of mutagenesis studies designed to determine the basis of the observed differences in bioluminescence color with the analogue adenylate. Mutants of P. pyralis luciferase putative active site residues Gly246 and Phe250, as well as corresponding click beetle residues Ala243 and Ser247 were constructed and characterized using bioluminescence emission spectroscopy and steady state kinetics with adenylate substrates. Based on an analysis of these and recently reported (Branchini, B. R., Southworth, T. L., Murtiashaw, M. H., Boije, H., and Fleet, S. E. (2003) Biochemistry 42, 10429-10436) data, we have developed an alternative mechanism of bioluminescence color. The basis of the mechanism is that luciferase modulates emission color by controlling the resonance-based charge delocalization of the anionic keto form of the oxyLuciferin excited state.
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a mutagenesis study of the putative Luciferin binding site residues of Firefly luciferase
Biochemistry, 2003Co-Authors: Bruce R. Branchini, Tara L Southworth, Martha H Murtiashaw, Henrik Boije, Sarah E FleetAbstract:Firefly luciferase catalyzes the highly efficient emission of yellow-green light from substrate Firefly Luciferin by a sequence of reactions that require Mg-ATP and molecular oxygen. We had previously developed [Branchini, B. R., Magyar, R. A., Murtiashaw, M. H., Anderson, S. M., and Zimmer, M. (1998) Biochemistry 37, 15311−15319] a molecular graphics-based working model of the luciferase active site starting with the first X-ray structure [Conti, E., Franks, N. P., and Brick, P. (1996) Structure 4, 287−298] of the enzyme without bound substrates. In our model, the Luciferin binding site contains 15 residues that are within 5 A of the substrate. Using site-directed mutagenesis, we made changes at all of these residues and report here the characterization of the corresponding expressed and purified proteins. Of the 15 residues studied, 12 had a significantly (≥4-fold Km difference) altered binding affinity for Luciferin and seven residues, spanning the primary sequence region Arg218−Ala348, had substantial...
Shojiro Maki - One of the best experts on this subject based on the ideXlab platform.
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development of near infrared Firefly Luciferin analogue reacted with wild type and mutant luciferases
Chirality, 2020Co-Authors: Nobuo Kitada, Takashi Hirano, Satoshi Iwano, Rika Obata, Atsushi Miyawaki, Ryohei Saito, Kazuma Karube, Shojiro MakiAbstract:Interestingly, only the D-form of Firefly Luciferin produces light by Luciferin-luciferase (L-L) reaction. Certain Firefly Luciferin analogues with modified structures maintain bioluminescence (BL) activity; however, all L-form Luciferin analogues show no BL activity. To this date, our group has developed Luciferin analogues with moderate BL activity that produce light of various wavelengths. For in vivo bioluminescence imaging, one of the important factors for detection sensitivity is tissue permeability of the number of photons emitted by L-L reaction, and the wavelengths of light in the near-infrared (NIR) range (700-900 nm) are most appropriate for the purpose. Some NIR Luciferin analogues by us had performance for in vivo experiments to make it possible to detect photons from deep target tissues in mice with high sensitivity, whereas only a few of them can produce NIR light by the L-L reactions with wild-type luciferase and/or mutant luciferase. Based on the structure-activity relationships, we designed and synthesized here a Luciferin analogue with the 5-allyl-6-dimethylamino-2-naphthylethenyl moiety. This analogue exhibited NIR BL emissions with wild-type luciferase (λmax = 705 nm) and mutant luciferase AlaLuc (λmax = 655 nm).
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synthesis and luminescence properties of near infrared n heterocyclic Luciferin analogues for in vivo optical imaging
Bulletin of the Chemical Society of Japan, 2019Co-Authors: Ryohei Saito, Takashi Hirano, Satoshi Iwano, Rika Obata, Masahiro Kiyama, Takahiro Kuchimaru, Shoko Higashi, Shinae Kizakakondoh, Shojiro MakiAbstract:As a means of achieving highly sensitive bioluminescence imaging of deep tissues utilizing the Firefly Luciferin-luciferase (L-L) reaction, we previously reported a Luciferin analogue, AkaLumine, w...
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an allylated Firefly Luciferin analogue with luciferase specific response in living cells
Chemical Communications, 2018Co-Authors: Yuma Ikeda, Nobuo Kitada, Tsuyoshi Saitoh, Shigeru Nishiyama, Shojiro Maki, Daniel Citterio, Kazuki Niwa, Takahiro Nakajima, Moritoshi Sato, Koji SuzukiAbstract:An allylated Firefly Luciferin was successfully synthesized and its bioluminescence properties were evaluated. When applied to cellular imaging in combination with Eluc, which is one of the commercially available luciferases, this analogue displayed a luciferase-specific bioluminescence signal with prolonged emission (>100 min).
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quantum yield improvement of red light emitting Firefly Luciferin analogues for in vivo bioluminescence imaging
Tetrahedron, 2017Co-Authors: Masahiro Kiyama, Takashi Hirano, Satoshi Iwano, Rika Obata, Atsushi Miyawaki, Satoshi Otsuka, Shojiro MakiAbstract:Abstract The dimethylamino group of AkaLumine ((4S)-2-[(1E,3E)-4-[4-(dimethylamino)phenyl]-1,3-butadien-1-yl]-4,5-dihydro-4-thiazolecarboxylic acid), a red-light-emitting Firefly Luciferin analogue, was replaced by cyclic amino groups (1-pyrrolidinyl, 1-piperidino, 1-azepanyl, and 4-morpholino) to give AkaLumine analogues exhibiting desirable bioluminescence with emission maxima in the red region (656–667 nm). In particular, a bioluminescence reaction of 1-pyrrolidinyl analogue with a recombinant Photinus pyralis luciferase showed a higher quantum yield than that with AkaLumine, giving an improved bioluminescence intensity. The 1-pyrrolidinyl analogue also showed the strongest luminescence in whole-body luciferase-expressing mice among the analogues, indicating that a quantum yield improvement of a Luciferin analogue is effective to increase bioluminescence imaging intensity.
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synthesis and luminescence properties of biphenyl type Firefly Luciferin analogs with a new near infrared light emitting bioluminophore
Tetrahedron, 2013Co-Authors: Chihiro Miura, Takashi Hirano, Satoshi Iwano, Rika Obata, Shojiro Maki, Masahiro Kiyama, Kazuto Ito, Haruki NiwaAbstract:Abstract New Firefly Luciferin analogs of the 4,4′-substituted biphenyl-type were synthesized. One analog with a 4′-dimethylamino group possessed bioluminescence activity, emitting near-infrared biological window light at 675 nm suitable for deep-site bioimaging of living animals. The chemiluminescence light-emission maximum of the corresponding methyl ester of the bioluminescence active analog was 500 nm, implying that biphenyl and thiazolinone rings in the light emitter might be placed in a coplanar conformation at the polar luciferase active site.
Timothy R Fallon - One of the best experts on this subject based on the ideXlab platform.
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laboratory culture of the california sea Firefly vargula tsujii ostracoda cypridinidae developing a model system for the evolution of marine bioluminescence
Scientific Reports, 2020Co-Authors: Jessica A Goodheart, Geetanjali Minsky, Mira N Brynjegardbialik, Michael S Drummond, David J Munoz, Timothy R Fallon, Darrin T SchultzAbstract:Bioluminescence, or the production of light by living organisms via chemical reaction, is widespread across Metazoa. Laboratory culture of bioluminescent organisms from diverse taxonomic groups is important for determining the biosynthetic pathways of bioluminescent substrates, which may lead to new tools for biotechnology and biomedicine. Some bioluminescent groups may be cultured, including some cnidarians, ctenophores, and brittle stars, but those use luminescent substrates (Luciferins) obtained from their diets, and therefore are not informative for determination of the biosynthetic pathways of the Luciferins. Other groups, including terrestrial fireflies, do synthesize their own Luciferin, but culturing them is difficult and the biosynthetic pathway for Firefly Luciferin remains unclear. An additional independent origin of endogenous bioluminescence is found within ostracods from the family Cypridinidae, which use their luminescence for defense and, in Caribbean species, for courtship displays. Here, we report the first complete life cycle of a luminous ostracod (Vargula tsujii Kornicker & Baker, 1977, the California Sea Firefly) in the laboratory. We also describe the late-stage embryogenesis of Vargula tsujii and discuss the size classes of instar development. We find embryogenesis in V. tsujii ranges from 25-38 days, and this species appears to have five instar stages, consistent with ontogeny in other cypridinid lineages. We estimate a complete life cycle at 3-4 months. We also present the first complete mitochondrial genome for Vargula tsujii. Bringing a luminous ostracod into laboratory culture sets the stage for many potential avenues of study, including learning the biosynthetic pathway of cypridinid Luciferin and genomic manipulation of an autogenic bioluminescent system.
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laboratory culture of the california sea Firefly vargula tsujii ostracoda cypridinidae developing a model system for the evolution of marine bioluminescence
bioRxiv, 2019Co-Authors: Jessica A Goodheart, Geetanjali Minsky, Mira N Brynjegardbialik, Michael S Drummond, David J Munoz, Timothy R Fallon, Darrin T Schultz, Jingke Weng, Elizabeth TorresAbstract:Bioluminescence, or the production of light by living organisms via chemical reaction, is widespread across Metazoa. Culturing bioluminescent organisms from diverse taxonomic groups is important for determining the biosynthetic pathways of bioluminescent substrates, which may lead to new tools for biotechnology and biomedicine. Although some previously cultured luminescent groups represent independent origins of bioluminescence, cnidarians, ctenophores, and brittle stars use luminescent substrates (Luciferins) obtained from their diets, and therefore are not informative for determination of the biosynthethic pathways of the Luciferins. Terrestrial fireflies do synthesize their own Luciferin, but the biosynthetic pathway for Firefly Luciferin remains unclear. An additional independent origin of endogenous bioluminescence is found within ostracods from the family Cypridinidae, which use their luminescence for defense and, in Caribbean species, for courtship displays. Here, we report the first complete life cycle of a luminous ostracod (Vargula tsujii, the California Sea Firefly) in the laboratory. We also describe the embryonic development of Vargula tsujii and discuss the size classes of instar development. We find embryogenesis in V. tsujii ranges between 25-38 days, and this species appears to have five instar stages, consistent with ontogeny in other cypridinid lineages. We estimate a complete life cycle at 3-4 months. We present the first complete mitochondrial genome for Vargula tsujii. Finally, we find no evidence of significant population genetic structure or cryptic species throughout the southern California range of V. tsujii. Bringing a luminous ostracod into laboratory culture sets the stage for many potential avenues of study, including the biosynthetic pathway of cypridinid Luciferin and genomic manipulation of an autogenic bioluminescent system.
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SulfoLuciferin is Biosynthesized by a Specialized Luciferin Sulfotransferase in Fireflies.
Biochemistry, 2016Co-Authors: Timothy R Fallon, Maria A. Vicent, Jingke WengAbstract:Firefly Luciferin is a specialized metabolite restricted to fireflies (family Lampyridae) and other select families of beetles (order Coleoptera). Firefly Luciferin undergoes luciferase-catalyzed oxidation to produce light, thereby enabling the luminous mating signals essential for reproductive success in most bioluminescent beetles. Although Firefly Luciferin and luciferase have become widely used biotechnological tools, questions remain regarding the physiology and biochemistry of Firefly bioluminescence. Here we report sulfoLuciferin to be an in vivo derivative of Firefly Luciferin in fireflies and report the cloning of Luciferin sulfotransferase (LST) from the North American Firefly Photinus pyralis. LST catalyzes the production of sulfoLuciferin from Firefly Luciferin and the sulfo-donor PAPS. SulfoLuciferin is abundant in several surveyed Firefly genera as well as in the bioluminescent elaterid beetle Pyrophorus luminosus at a low level. We propose that sulfoLuciferin could serve as a Luciferin storage molecule in fireflies and that LST may find use as a new tool to modulate existing biotechnological applications of the Firefly bioluminescent system.