Extreme diversity, conservation, and convergence of spider silk fibroin sequences

被引：454

作者：

Gatesy, J ^{[1
]}

Hayashi, C ^{[1
]}

Motriuk, D ^{[1
]}

Woods, J ^{[1
]}

Lewis, R ^{[1
]}

机构：

[1] Univ Wyoming, Dept Mol Biol, Laramie, WY 82071 USA

来源：

SCIENCE | 2001年 / 291卷 / 5513期

关键词：

D O I：

10.1126/science.1057561

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 [理学]; 0710 [生物学]; 09 [农学];

摘要：

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.

引用

页码：2603 / 2605

页数：3

共 23 条

[1]

Evolution of repetitive proteins:: spider silks from Nephila clavipes (Tetragnathidae) and Araneus bicentenarius (Araneidae) [J].