Abstract
Beetle luciferase, a mono-oxygenase within the AMP-binding superfamily, is synthesized by bioluminescent beetles in concentrated levels within specialised cells clustering in the abdominal light organs. In vivo expression of luciferase has been rarely investigated and little is known about the role of enhancers and promoters in the expression of this gene. In order to investigate the gene structure and potential control of gene expression the luciferase gene along with 6 kb of upstream genomic sequence was char- acterised from the European glow-worm Lampyris noctiluca. Three TATA box motifs and a CAAT repeat were identified, two of these were found to be conserved in two other species of bioluminescent beetle. Although no enhancer regions were identified in the upstream sequence a region coding for a putative transposase DDE domain was identified 686 bp from the start codon of the lucife- rase gene. Although disrupted, the open reading frame also shared extensive identity to an mRNA transcript from the mosquito Anopheles gambiae. The remnants of an ancient transposase provide support for an ancestral luciferase transposition/insertion event that may have occurred within the genome of bioluminescent beetles.
Highlights
Along with fireflies the European glow-worm Lampyris noctiluca (Linnaeus) is one of over 2000 bioluminescent beetle species belonging to the family Lampyridae
Luciferase (EC 1.13.12.7) from the American firefly species Photinus pyralis is a 62 kDa enzyme that catalyses the emission of yellow-green light (Omax 560 nm) upon reaction of D-luciferin, ATP, and molecular oxygen (McElroy et al, 1969; White et al, 1971; Deluca & McElroy, 1978)
When compared to the luc sequences from two other species of Lampyridae, Photinus pyralis and Luciola lateralis (Cho et al, 1999) exon/intron sites in luc from L. noctiluca were found to be completely conserved in both number and position
Summary
Along with fireflies the European glow-worm Lampyris noctiluca (Linnaeus) is one of over 2000 bioluminescent beetle species belonging to the family Lampyridae. The cloning and sequencing of luciferase cDNA from Photinus pyralis and many other bioluminescent beetle species has revealed that these enzymes are highly conserved proteins closely related to a large family of non-bioluminescent proteins that catalyse reactions of ATP with carboxylate substrates to form acyl-adenylates (Conti et al, 1996).
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