Isolation of a clone encoding a second dragline silk fibroin. Nephila clavipes dragline silk is a two-protein fiber.
Spider dragline silk is a unique protein fiber possessing both high tensile strength and high elasticity. A partial cDNA clone for one dragline silk protein (Spidroin 1) was previously isolated. However, the predicted amino acid sequence could not account for the amino acid composition of dragline silk. We have isolated a partial cDNA clone for another dragline silk protein (Spidroin 2), demonstrating that dragline silk is composed of multiple proteins. The amino acid sequence exhibits an entirely different repetitive motif than Spidroin 1. Spidroin 2 is predicted to consist of linked beta-turns in proline-rich regions which alternate with beta-sheet regions composed of polyalanine segments. This structure for Spidroin 2 provides a model for dragline silk structure and function.
Hinman
M B
MB
Department of Molecular Biology, University of Wyoming, Laramie 82071.
Lewis
R V
RV
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003062:Codon; D005349:Fibroins; D019476:Insect Proteins; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000235:genetics*; D016415:Sequence Alignment; D047011:Silk; D012995:Solubility; D013112:Spiders / Q000737:chemistry*
D003062:Codon; D019476:Insect Proteins; D011506:Proteins; D047011:Silk; C076815:spidroin 2; D005349:Fibroins