Functional conservation and structural diversification of silk sericins in two moth species
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
23593923
DOI
10.1021/bm400249b
Knihovny.cz E-resources
- MeSH
- Species Specificity MeSH
- Silk chemistry MeSH
- Protein Conformation MeSH
- Molecular Sequence Data MeSH
- Moths chemistry MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Homology, Nucleic Acid MeSH
- Sericins chemistry genetics MeSH
- RNA Splicing MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Silk MeSH
- Sericins MeSH
Sericins are hydrophilic structural proteins produced by caterpillars in the middle section of silk glands and layered over fibroin proteins secreted in the posterior section. In the process of spinning, fibroins form strong solid filaments, while sericins seal the pair of filaments into a single fiber and glue the fiber into a cocoon. Galleria mellonella and the previously examined Bombyx mori harbor three sericin genes that encode proteins containing long repetitive regions. Galleria sericin genes are similar to each other and the protein repeats are built from short and extremely serine-rich motifs, while Bombyx sericin genes are diversified and encode proteins with long and complex repeats. Developmental changes in sericin properties are controlled at the level of gene expression and splicing. In Galleria , MG-1 sericin is produced throughout larval life until the wandering stage, while the production of MG-2 and MG-3 reaches a peak during cocoon spinning.
References provided by Crossref.org