The evolution of the adenylate-forming protein family in beetles: Multiple luciferase gene paralogues in fireflies and glow-worms

Bioluminescence in beetles is dependent upon the enzyme luciferase. It has been hypothesised luciferase evolved from a fatty acyl-CoA synthetase gene deriving a novel bioluminescent function (neofunctionalization) after a gene duplication event. We evaluated this hypothesis within a phylogenetic fra...

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Published inMolecular phylogenetics and evolution Vol. 50; no. 1; pp. 93 - 101
Main Authors Day, John C., Goodall, Tim I., Bailey, Mark J.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 2009
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Abstract Bioluminescence in beetles is dependent upon the enzyme luciferase. It has been hypothesised luciferase evolved from a fatty acyl-CoA synthetase gene deriving a novel bioluminescent function (neofunctionalization) after a gene duplication event. We evaluated this hypothesis within a phylogenetic framework using independent evidence obtained from the genome of Tribolium castaneum, published luciferase genes and novel luciferase and luciferase-like sequences. This phylogenetic study provides evidence for a large gene family of luciferase and luciferase-like paralogues in bioluminescent and non-bioluminescent beetles. All luciferase sequences formed a clade supporting a protoluciferase existing prior to the divergence of the Lampyridae, Elateridae and Phengodidae (Elateroidea). Multiple luciferase genes were identified from members of the Photurinae and the Luciolinae indicating complex gene duplication events within lampyrid genomes. The majority of luciferase residues were identified to be under purifying selection as opposed to positive selection. We conclude that beetle luciferase may have arisen from a process of subfunctionalization as opposed to neofunctionalization early on in the evolution of the Elateroidea.
AbstractList Bioluminescence in beetles is dependent upon the enzyme luciferase. It has been hypothesised luciferase evolved from a fatty acyl-CoA synthetase gene deriving a novel bioluminescent function (neofunctionalization) after a gene duplication event. We evaluated this hypothesis within a phylogenetic framework using independent evidence obtained from the genome of Tribolium castaneum, published luciferase genes and novel luciferase and luciferase- like sequences. This phylogenetic study provides evidence for a large gene family of luciferase and luciferase-like paralogues in bioluminescent and non-bioluminescent beetles. All luciferase sequences formed a clade supporting a protoluciferase existing prior to the divergence of the Lampyridae, Elateridae and Phengodidae (Elateroidea). Multiple luciferase genes were identified from members of the Photurinae and the Luciolinae indicating complex gene duplication events within lampyrid genomes. The majority of luciferase residues were identified to be under purifying selection as opposed to positive selection. We conclude that beetle luciferase may have arisen from a process of subfunctionalization as opposed to neofunctionalization early on in the evolution of the Elateroidea.
Bioluminescence in beetles is dependent upon the enzyme luciferase. It has been hypothesised luciferase evolved from a fatty acyl-CoA synthetase gene deriving a novel bioluminescent function (neofunctionalization) after a gene duplication event. We evaluated this hypothesis within a phylogenetic framework using independent evidence obtained from the genome of Tribolium castaneum, published luciferase genes and novel luciferase and luciferase-like sequences. This phylogenetic study provides evidence for a large gene family of luciferase and luciferase-like paralogues in bioluminescent and non-bioluminescent beetles. All luciferase sequences formed a clade supporting a protoluciferase existing prior to the divergence of the Lampyridae, Elateridae and Phengodidae (Elateroidea). Multiple luciferase genes were identified from members of the Photurinae and the Luciolinae indicating complex gene duplication events within lampyrid genomes. The majority of luciferase residues were identified to be under purifying selection as opposed to positive selection. We conclude that beetle luciferase may have arisen from a process of subfunctionalization as opposed to neofunctionalization early on in the evolution of the Elateroidea.
Author Bailey, Mark J.
Day, John C.
Goodall, Tim I.
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Issue 1
Keywords Subfunctionalization
Bioluminescence
Luciferase
Lampyridae
Tribolium castaneum
Adenylate-forming enzyme superfamily
Purifying selection
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Snippet Bioluminescence in beetles is dependent upon the enzyme luciferase. It has been hypothesised luciferase evolved from a fatty acyl-CoA synthetase gene deriving...
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StartPage 93
SubjectTerms Adenine - metabolism
Adenylate-forming enzyme superfamily
Amino Acid Sequence
Animals
Bioluminescence
Coleoptera - classification
Coleoptera - enzymology
Coleoptera - genetics
Elateridae
Elateroidea
Evolution, Molecular
Lampyridae
Luciferase
Luciferases - chemistry
Luciferases - classification
Luciferases - genetics
Luciferases - metabolism
Molecular Sequence Data
Phengodidae
Phylogeny
Purifying selection
Sequence Alignment
Subfunctionalization
Tribolium castaneum
Title The evolution of the adenylate-forming protein family in beetles: Multiple luciferase gene paralogues in fireflies and glow-worms
URI https://dx.doi.org/10.1016/j.ympev.2008.09.026
https://www.ncbi.nlm.nih.gov/pubmed/18951986
https://search.proquest.com/docview/20265381
https://search.proquest.com/docview/66755782
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