The design of silk fiber composition in moths has been conserved for more than 150 million years
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- aminokyselinové motivy MeSH
- čas MeSH
- druhová specificita MeSH
- fibroiny biosyntéza chemie genetika MeSH
- glykoproteiny genetika MeSH
- hedvábí biosyntéza MeSH
- hmyzí proteiny genetika MeSH
- komplementární DNA izolace a purifikace MeSH
- konzervovaná sekvence * MeSH
- molekulární evoluce * MeSH
- molekulární sekvence - údaje MeSH
- můry genetika metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvence nukleotidů MeSH
- sekvenční homologie aminokyselin MeSH
- sekvenční homologie nukleových kyselin MeSH
- strukturní homologie proteinů MeSH
- vztahy mezi strukturou a aktivitou MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- fibroiny MeSH
- glykoproteiny MeSH
- hedvábí MeSH
- hmyzí proteiny MeSH
- komplementární DNA MeSH
- L-chain, fibroin protein, insect MeSH Prohlížeč
- P25 protein, Galleria mellonella MeSH Prohlížeč
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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