Extreme diversity, conservation, and convergence of spider silk fibroin sequences
Extreme diversity, conservation, and convergence of spider silk fibroin sequences
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DOI：
10.1126/science.1057561
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发表时间：
2001-03-30
期刊：
影响因子：
56.9
通讯作者：
Lewis, R
中科院分区：
文献类型：
--
作者：
Gatesy, J;Hayashi, C;Lewis, R
蜘蛛（蜘蛛目）从液态丝素蛋白中纺出高性能的丝。丝心蛋白序列从基础蜘蛛血统揭示马赛克的氨基酸基序，从根本上不同于先前描述的蜘蛛丝序列。蜘蛛目的丝纤维由许多蛋白质设计构成。然而，在超过1.25亿年的进化历史中，来自圆织蜘蛛的丝心蛋白的重复序列一直保持着，大概是通过稳定选择。保留这些保守的图案，因为中生代和他们的趋同进化在其他结构超蛋白意味着这些序列是理解特殊的机械性能的球织丝绸的核心。
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.