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Fibroin, one of the major silk components, is composed of heavy chain proteins, light chain proteins, and P25, and is secreted by the posterior silkgland (PSG) [3], [4].
Here, we identify and analyze genes specifically expressed in silk glands, and thus represent candidates for silk components or involvement with silk synthesis, assembly or regulation.
We focused on discovering candidate genes encoding silk components (fibers and glues) and genes involved in silk synthesis, fiber assembly, or regulating silk gland specific expression.
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The central part of the protein comprises an extended sequence rich in glycine and glutamine residues whose repetitive motif QMQGCGQQXP (X is mostly methionine) shows high similarity to the elastic glycine-rich sequence of the major spider silk component from Nephila clavipes, Spidroin-2 [ 22].
Here it also functions to indicate the protein fibre component, silk.
Firstly, a sequence showing 78% identity with MSI60 from the silk fibroin matrix component could be retrieved.
Consistent with the hypothesis that gene duplication is important for the evolution of functional novelty, the primary protein components of silk fibers are encoded by members of a gene family called spidroins spider fibrous proteins (Hinman and Lewis 1992; Guerette et al. 1996; Gatesy et al. 2001).
Many (75%) of the SSTs were not assigned a functional annotation by association with a Gene Ontology (GO) term, possibly because they represent silk fiber or glue components that have not been assigned GO terms (e.g. spidroins and aggregate gland glues do not have GO terms).
Silk threads (and silk ribbons).
Sericin is a water-soluble component of silk and has been used as a biomaterial due to its antibacterial and ultraviolet radiation-resistant properties.
The chapter begins by examining the gene encoding for the main component of silk fibroin and the primary structure of the protein itself.
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