Functional conservation and structural diversification of silk sericins in two moth species
| Autor: | František Sehnal, Michal Zurovec, Barbara Kludkiewicz, Jitka Sulitkova, Václav Mach, Robert Fedic, Lucie Kucerova |
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| Rok vydání: | 2013 |
| Předmět: |
Polymers and Plastics
Protein Conformation RNA Splicing Molecular Sequence Data Silk Fibroin Bioengineering Moths Sericin Biomaterials Protein structure Species Specificity Bombyx mori Sequence Homology Nucleic Acid Botany Materials Chemistry Animals Amino Acid Sequence Sericins Peptide sequence Bombyx biology Base Sequence fungi biology.organism_classification Cell biology Galleria mellonella SILK |
| Zdroj: | Biomacromolecules. 14(6) |
| ISSN: | 1526-4602 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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