GEPHE SUMMARY
Gephebase Gene
Entry Status
Published
GepheID
GP00000348
Main curator
Martin
PHENOTYPIC CHANGE
Trait #1
Trait Category
Trait State in Taxon A
Other lepidopterans
Trait State in Taxon B
Tyria jacobaeae and other arctiidae
Trait #2
Trait Category
Trait State in Taxon A
-
Trait State in Taxon B
-
Ancestral State
Data not curated
Taxonomic Status
Taxon A
Latin Name
Common Name
butterflies and moths
Synonyms
butterflies and moths; moths
Rank
order
Lineage
Show more ... hokonta; Metazoa; Eumetazoa; Bilateria; Protostomia; Ecdysozoa; Panarthropoda; Arthropoda; Mandibulata; Pancrustacea; Hexapoda; Insecta; Dicondylia; Pterygota; Neoptera; Holometabola; Amphiesmenoptera
NCBI Taxonomy ID
is Taxon A an Infraspecies?
No
Taxon B
Common Name
cinnabar moth
Synonyms
cinnabar moth; Tyria jacobaeae (Linnaeus, 1758)
Rank
species
Lineage
Show more ... a; Insecta; Dicondylia; Pterygota; Neoptera; Holometabola; Amphiesmenoptera; Lepidoptera; Glossata; Neolepidoptera; Heteroneura; Ditrysia; Obtectomera; Noctuoidea; Erebidae; Arctiinae; Arctiini; Tyria
NCBI Taxonomy ID
is Taxon B an Infraspecies?
No
GENOTYPIC CHANGE
Generic Gene Name
Fmo-1
Synonyms
CG3006; Dmel\CG3006; DmFMO-1; Dmfmo1; FMO-1; Dmel_CG3006
Sequence Similarities
Belongs to the FMO family.
GO - Biological Process
-
UniProtKB
Drosophila melanogaster
GenebankID or UniProtKB
Presumptive Null
No
Molecular Type
Aberration Type
Molecular Details of the Mutation
Gene duplication
Experimental Evidence
Authors
Sehlmeyer S; Wang L; Langel D; Heckel DG; Mohagheghi H; Petschenka G; Ober D
Abstract
Insects experience a wide array of chemical pressures from plant allelochemicals and pesticides and have developed several effective counterstrategies to cope with such toxins. Among these, cytochrome P450 monooxygenases are crucial in plant-insect interactions. Flavin-dependent monooxygenases (FMOs) seem not to play a central role in xenobiotic detoxification in insects, in contrast to mammals. However, the previously identified senecionine N-oxygenase of the arctiid moth Tyria jacobaeae (Lepidoptera) indicates that FMOs have been recruited during the adaptation of this insect to plants that accumulate toxic pyrrolizidine alkaloids. Identification of related FMO-like sequences of various arctiids and other Lepidoptera and their combination with expressed sequence tag (EST) data and sequences emerging from the Bombyx mori genome project show that FMOs in Lepidoptera form a gene family with three members (FMO1 to FMO3). Phylogenetic analyses suggest that FMO3 is only distantly related to lepidopteran FMO1 and FMO2 that originated from a more recent gene duplication event. Within the FMO1 gene cluster, an additional gene duplication early in the arctiid lineage provided the basis for the evolution of the highly specific biochemical, physiological, and behavioral adaptations of these butterflies to pyrrolizidine-alkaloid-producing plants. The genes encoding pyrrolizidine-alkaloid-N-oxygenizing enzymes (PNOs) are transcribed in the fat body and the head of the larvae. An N-terminal signal peptide mediates the transport of the soluble proteins into the hemolymph where PNOs efficiently convert pro-toxic pyrrolizidine alkaloids into their non-toxic N-oxide derivatives. Heterologous expression of a PNO of the generalist arctiid Grammia geneura produced an N-oxygenizing enzyme that shows noticeably expanded substrate specificity compared with the related enzyme of the specialist Tyria jacobaeae. The data about the evolution of FMOs within lepidopteran insects and the functional characterization of a further member of this enzyme family shed light on this almost uncharacterized detoxification system in insects.
Additional References
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