Chemical, biological and evolutionary aspects of beetle bioluminescence

Etelvino J H Bechara,Clélia Ferreira,Marcelo P Barros,Moacir A Torres,Abner B Lallf,Vadim Viviani,Graham S Timmins,Walter R Terra,Cassius V Stevani,Cleide Costa,Pio Colepicolo

doi:10.3998/ark.5550190.0008.824

Etelvino J H Bechara, Clélia Ferreira + Show 9 more

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https://doi.org/10.3998/ark.5550190.0008.824

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Abstract

This work is dedicated to Prof. Waldemar Adam, an esteemed friend and eminent scientist who, for decades, generously shared knowledge, enthusiasm, and laboratory supplies with many Brazilian investigators, among them G. Cilento and myself. In 1980, Prof. Adam was elected Foreign Member of the Brazilian Academy of Sciences in recognition for his substantial contributions towards the development of Chemistry in Brazil. Abstract The hypothesis that luciferases evolved from ligases that acquired oxygenase and luminogenic activities, thereby contributing to the antioxidant machinery of bioluminescent organisms, is revisited here. Larvae of click beetle Pyrearinus termitilluminans (Coleoptera: Elateridae) live under conditions close to normoxia into tunnels dug into termite mounds, whereas other elaterid larvae inhabit tunnels in decaying logs, where pO2 is ~ 2-5%. Interestingly, the catalase and superoxide dismutase (SOD) activities in click beetle larvae were found to respond to the habitat pO2 and are significantly lower in non-luminescent elaterids. Exposure of larval P. termitilluminans larvae to hyperoxia induced SOD and catalase activities concomitantly with increments in luciferase and luciferin levels mainly in the prothorax, the brightest larval segment. Thoracic luciferase activity is 1000-fold higher than in the abdomen, while SOD activity is 2- fold higher. With larval development, an expected decline in antioxidant enzyme activities was apparently compensated by an increase in luciferase activity (2-3 fold) and in urate (40-fold), a major insect antioxidant. Finally, we found that the ligase-rich fat body of larval Tenebrio molitor, a non-luminescent beetle, contains a primal luciferase-like activity. Altogether, these data strengthen the hypothesis that various bioluminescent systems may have developed from potentially chemiluminescent metabolites and ligases that acquired a dioxygenase and luminogenic function over the course of evolution.

Highlights

Emission of visible and "cold" light by living organisms is called bioluminescence
That the bioluminescent reaction may contribute to minimize oxidative stress was indicated by concomitant induction of superoxide dismutase (SOD) and luciferase in luminescent Xenorhabdus luminescens bacteria when subjected to hyperoxia and by reported antioxidant properties of coelenterazine,[37] the luciferin of several marine organisms,[38] and of firefly luciferin towards chemical and biological targets.[39]
Noteworthy is that, in laboratory, the activity of larval P. termitilluminans luciferase peaks at about 19:30 h, when the larva start shining in the termite mounds to attract preys, and SOD levels were found to be maximal at early night and during the morning, when the larvae where observed digging tunnels in the soil substrate where they are raised.[45]

Summary

Introduction

Emission of visible and "cold" light by living organisms is called bioluminescence. It occurs mainly in deep-sea marine organisms and less frequently on land and serves as a means of intraspecies and inter-species communication, as in mating, predation, defense, warning, congregation and territoriality.

Results

Conclusion