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Science 30 March 2001: Vol. 291. no. 5513, pp. 2603 - 2605 DOI: 10.1126/science.1057561
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Reports
Extreme Diversity, Conservation, and Convergence of Spider Silk Fibroin Sequences
John Gatesy,*
Cheryl Hayashi,*
Dagmara Motriuk,
Justin Woods,
Randolph Lewis
Spiders (Araneae) spin high-performance silks from liquid fibroin
proteins. Fibroin sequences from basal spider lineages reveal mosaics
of amino acid motifs that differ radically from previously described
spider silk sequences. The silk fibers of Araneae are constructed from
many protein designs. Yet, the repetitive sequences of fibroins from
orb-weaving spiders have been maintained, presumably by stabilizing
selection, over 125 million years of evolutionary history. The
retention of these conserved motifs since the Mesozoic and their
convergent evolution in other structural superproteins imply that these
sequences are central to understanding the exceptional mechanical
properties of orb weaver silks.
Department of Molecular Biology, University of Wyoming, Laramie,
WY 82071, USA.
*
Present address: Department of Biology, University of
California, Riverside, CA 92521, USA.
These authors contributed equally to this work.
To whom correspondence should be addressed.
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