The origin,diversity, and structure function relationships of insect luciferases |
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Authors: | V R Viviani |
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Institution: | (1) Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, Massachusetts 02138 (USA), Fax +1 617 496-8726, e-mail: viviani@fas.harvard.edu; bioluz@lycos.com, US |
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Abstract: | Luciferases are the enzymes that catalyze the reactions that produce light in bioluminescence. Whereas the oxidative mechanism
which leads to light emission is similar for most luciferases, these enzymes and their substrates are evolutionarily unrelated.
Among all bioluminescent groups, insects constitute one of the most diverse in terms of biochemistry. In the fungus-gnats
(Mycetophilidae: Diptera), for example, bioluminescence is generated by two biochemically distinct systems. Despite the diversity,
investigations on insect luciferases and biochemistry have been conducted mostly with fireflies. The luciferases from the
related phengodid beetles, which can produce green to red bioluminescence using the same chemistry as firefly luciferases,
have been recently investigated. Beetle luciferases originated from ancestral acyl-CoA ligases. Present data suggest that
conserved motifs among this class of ligases are involved in substrate adenylation. The three-dimensional structure of firefly
luciferase was recently solved and mutagenesis studies have been performed identifying putative residues involved in luciferin
binding and bioluminescence color determination in several beetle luciferases. The knowledge gained through these studies
is helping in the development of useful reporter gene tools for biotechnological and biomedical purposes.
Received 4 March 2002; received after revision 13 May 2002; accepted 21 May 2002 |
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Keywords: | , Luciferases, bioluminescence, Mycetophilidae, Lampyridae, Phengodidae, Elateridae, Staphylinidae, Collembola, Diptera,,,,,,Coleoptera, |
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