Extreme Diversity, Conservation, and Convergence of Spider Silk Fibroin Sequences

See allHide authors and affiliations

Science  30 Mar 2001:
Vol. 291, Issue 5513, pp. 2603-2605
DOI: 10.1126/science.1057561

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


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.

  • * Present address: Department of Biology, University of California, Riverside, CA 92521, USA.

  • These authors contributed equally to this work.

View Full Text