Marine Bioluminescence with Dehydrocoelenterazine, an Imidazopyrazinone Compound

Kuse, Masaki

doi:10.1007/7081_2020_41

Cited by 4 publications

(3 citation statements)

References 71 publications

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“…Based on current data, it has been observed that A. filiformis does not possess any storage forms of coelenterazine, unlike other bioluminescent species that use such forms 13 , 14 . Enol sulfate coelenterazine has been found in the liver and light organs of Gymnoscopelus braueri , and squid species such as Watasenia scintillans, Eucleoteuthis luminosa, or Symplectoteuthis oualaniensis possess the dehydrocoelenterazine form 13 , 36 . These modified forms serve to stabilize and limit the oxidation of coelenterazine oxidation 14 , 37 , 38 .…”

Section: Discussionmentioning

confidence: 99%

Maintain the light, long-term seasonal monitoring of luminous capabilities in the brittle star Amphiura filiformis

Coubris,

Duchatelet,

Delroisse

et al. 2024

Sci Rep

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The European brittle star Amphiura filiformis emits blue light, via a Renilla-like luciferase, which depends on the dietary acquisition of coelenterazine. Questions remain regarding luciferin availability across seasons and the persistence of luminous capabilities after a single boost of coelenterazine. To date, no study has explored the seasonal, long-term monitoring of these luminous capabilities or the tracking of luciferase expression in photogenic tissues. Through multidisciplinary analysis, we demonstrate that luminous capabilities evolve according to the exogenous acquisition of coelenterazine throughout adult life. Moreover, no coelenterazine storage forms are detected within the arms tissues. Luciferase expression persists throughout the seasons, and coelenterazine's presence in the brittle star diet is the only limiting factor for the bioluminescent reaction. No seasonal variation is observed, involving a continuous presence of prey containing coelenterazine. The ultrastructure description provides a morphological context to investigate the green autofluorescence signal attributed to coelenterazine during luciferin acquisition. Finally, histological analyses support the hypothesis of a pigmented sheath leading light to the tip of the spine. These insights improve our understanding of the bioluminescence phenomenon in this burrowing brittle star.

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Section: Discussionmentioning

confidence: 99%

Maintain the light, long-term seasonal monitoring of luminous capabilities in the brittle star Amphiura filiformis

Coubris,

Duchatelet,

Delroisse

et al. 2024

Sci Rep

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“…The biochemistry of the Pholas bioluminescence was studied in depth in the 1970s (Henry and Michelson, 1973;Michelson, 1978). The term Pholasin was initially dedicated to the luciferin before Pholasin was confirmed to be a photoprotein (Henry and Michelson, 1973;Knight and Campbell, 1987;Kuse, 2020). Dunstan et al (2000) cloned the gene coding for the Pholasin apoprotein.…”

Section: Sthenoteuthis-type Photoproteins or Symplectin (Group Vii)mentioning

confidence: 99%

Leaving the Dark Side? Insights Into the Evolution of Luciferases

et al. 2021

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Bioluminescence—i.e., the emission of visible light by living organisms—is defined as a biochemical reaction involving, at least, a luciferin substrate, an oxygen derivative, and a specialised luciferase enzyme. In some cases, the enzyme and the substrate are durably associated and form a photoprotein. While this terminology is educatively useful to explain bioluminescence, it gives a false idea that all luminous organisms are using identical or homologous molecular tools to achieve light emission. As usually observed in biology, reality is more complex. To date, at least 11 different luciferins have indeed been discovered, and several non-homologous luciferases lato sensu have been identified which, all together, confirms that bioluminescence emerged independently multiple times during the evolution of living organisms. While some phylogenetically related organisms may use non-homologous luciferases (e.g., at least four convergent luciferases are found in Pancrustacea), it has also been observed that phylogenetically distant organisms may use homologous luciferases (e.g., parallel evolution observed in some cnidarians, tunicates and echinoderms that are sharing a homologous luciferase-based system). The evolution of luciferases then appears puzzling. The present review takes stock of the diversity of known “bioluminescent proteins,” their evolution and potential evolutionary origins. A total of 134 luciferase and photoprotein sequences have been investigated (from 75 species and 11 phyla), and our analyses identified 12 distinct types—defined as a group of homologous bioluminescent proteins. The literature review indicated that genes coding for luciferases and photoproteins have potentially emerged as new genes or have been co-opted from ancestral non-luciferase/photoprotein genes. In this latter case, the homologous gene’s co-options may occur independently in phylogenetically distant organisms.

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“…The biochemistry of the Pholas bioluminescence was studied in depth in the seventies (Henry and Michelson, 1973;Michelson, 1978). The term Pholasin was initially dedicated to the luciferin before Pholasin was confirmed to be a photoprotein (Henry and Michelson, 1973;Robert et al, 1987;Kuse, 2020). Dunstan et al (2000) cloned the gene coding for the Pholasin apoprotein.…”

Section: The Sthenoteuthis-type Photoprotein or Symplectin (Group Vii)mentioning

confidence: 99%

Leaving the Dark Side? Insights Into the Evolution of Luciferases

Delroisse¹,

Duchatelet²,

Flammang³

et al. 2021

Preprint

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Bioluminescence – i.e., the emission of visible light by living organisms - is defined as a biochemical reaction involving, at least, a luciferin substrate, an oxygen derivative, and a specialised luciferase enzyme. In some cases, the enzyme and the substrate are durably associated and form a photoprotein. While this terminology is educatively useful to explain bioluminescence, it gives a false idea that all luminous organisms are using identical or homologous molecular tools to achieve light emission. As usually observed in biology, reality is more complex. To date, 11 different luciferins have indeed been discovered, and several non-homologous luciferases lato sensu have been identified which, all together, confirms that bioluminescence emerged independently multiple times during the evolution of living organisms. While some phylogenetically related organisms may use non-homologous luciferases (e.g., at least four convergent luciferases are found in Pancrustacea), it has also been observed that phylogenetically distant organisms may use homologous luciferases (e.g., parallel evolution observed in some cnidarians, tunicates and echinoderms that are sharing a homologous luciferase-based system). The evolution of luciferases then appears puzzling. The present review takes stock of the diversity of known “bioluminescent proteins”, their evolution and potential evolutionary origins. A total of 134 luciferase and photoprotein sequences have been investigated (from 75 species and 11 phyla), and our analyses identified 12 distinct types – defined as a group of homologous bioluminescent proteins. The literature review indicated that genes coding for luciferases and photoproteins have potentially emerged as new genes or have been co-opted from ancestral non-luciferase/photoprotein genes. In this latter case, the homologous gene’s co-options may occur independently in phylogenetically distant organisms.

show abstract

Marine Bioluminescence with Dehydrocoelenterazine, an Imidazopyrazinone Compound

Cited by 4 publications

References 71 publications

Maintain the light, long-term seasonal monitoring of luminous capabilities in the brittle star Amphiura filiformis

Maintain the light, long-term seasonal monitoring of luminous capabilities in the brittle star Amphiura filiformis

Leaving the Dark Side? Insights Into the Evolution of Luciferases

Leaving the Dark Side? Insights Into the Evolution of Luciferases

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