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蜘蛛鞭毛状丝:蛋白质设计、基因结构与分子进化的经验教训。

Spider flagelliform silk: lessons in protein design, gene structure, and molecular evolution.

作者信息

Hayashi C Y, Lewis R V

机构信息

Department of Molecular Biology, University of Wyoming, Laramie, USA.

出版信息

Bioessays. 2001 Aug;23(8):750-6. doi: 10.1002/bies.1105.

Abstract

Spiders spin multiple types of silks that are renowned for their superb mechanical properties. Flagelliform silk, used in the capture spiral of an orb-web, is one of the few silks characterized by both cDNA and genomic DNA data. This fibroin is composed of repeating ensembles of three types of amino acid sequence motifs. The predominant subrepeat, GPGGX, likely forms a beta-turn, and tandem arrays of these turns are thought to create beta-spirals. These spring-like helices may be critical for the exceptional ability of capture silk to stretch and recoil. Each ensemble of motifs was found to correspond to a different exon within the flagelliform gene. The pattern of sequence similarity among exons indicates intragenic concerted evolution. Surprisingly, the introns between the iterated exons are also homogenized with each other. This unusual molecular architecture in the flagelliform silk gene has implications for the evolution and maintenance of spider silk proteins.

摘要

蜘蛛能纺出多种类型的蛛丝,这些蛛丝以其卓越的机械性能而闻名。用于圆网捕获螺旋的鞭毛状蛛丝,是少数同时具有cDNA和基因组DNA数据特征的蛛丝之一。这种丝心蛋白由三种氨基酸序列基序的重复组合构成。主要的亚重复序列GPGGX可能形成一个β-转角,这些转角的串联阵列被认为会形成β-螺旋。这些类似弹簧的螺旋结构可能对于捕获丝拉伸和回弹的非凡能力至关重要。发现每个基序组合对应于鞭毛状基因内的一个不同外显子。外显子之间的序列相似性模式表明基因内协同进化。令人惊讶的是,重复外显子之间的内含子彼此之间也趋于同质化。鞭毛状蛛丝基因中这种不寻常的分子结构对蜘蛛丝蛋白的进化和维持具有重要意义。

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