The design of silk fiber composition in moths has been conserved for more than 150 million years
Language English Country Germany Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Amino Acid Motifs MeSH
- Time MeSH
- Species Specificity MeSH
- Fibroins biosynthesis chemistry genetics MeSH
- Glycoproteins genetics MeSH
- Silk biosynthesis MeSH
- Insect Proteins genetics MeSH
- DNA, Complementary isolation & purification MeSH
- Conserved Sequence * MeSH
- Evolution, Molecular * MeSH
- Molecular Sequence Data MeSH
- Moths genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Sequence Homology, Nucleic Acid MeSH
- Structural Homology, Protein MeSH
- Structure-Activity Relationship MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Fibroins MeSH
- Glycoproteins MeSH
- Silk MeSH
- Insect Proteins MeSH
- DNA, Complementary MeSH
- L-chain, fibroin protein, insect MeSH Browser
- P25 protein, Galleria mellonella MeSH Browser
The silk of caterpillars is secreted in the labial glands, stored as a gel in their lumen, and converted into a solid filament during spinning. Heavy chain fibroin (H-fibroin), light chain fibroin (L-fibroin), and P25 protein constitute the filament core in a few species that have been analyzed. Identification of these proteins in Yponomeuta evonymella, a moth from a family which diverged from the rest of Lepidoptera about 150 million years ago, reveals that the mode of filament construction is highly conserved. It is proposed that association of the three proteins is suited for long storage of hydrated silk dope and its rapid conversion to filament. Interactions underlying these processes depend on conserved spacing of critical amino acid residues that are dispersed through the L-fibroin and P25 and assembled in the short ends of the H-fibroin molecule. Strength, elasticity, and other physical properties of the filament are determined by simple amino acid motifs arranged in repetitive modules that build up most of the H-fibroin. H-Fibroin synergy with L-fibroin and P25 does not interfere with motif diversification by which the filament acquires new properties. Several types of motifs in complex repeats occur in the silks used for larval cobwebs and pupal cocoons. Restriction of silk use to cocoon construction in some lepidopteran families has been accompanied by simplification of H-fibroin repeats. An extreme deviation of the silk structure occurs in the Saturniidae silkmoths, which possess modified H-fibroin and lack L-fibroin and P25.
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