CSIRO Ecosystem Sciences, Black Mountain Labs, GPO 1700, Canberra, ACT 2601, Australia.
Biology Department, Creighton University, 2500 California Plaza, Omaha, NE 68131, USA.
Insect Biochem Mol Biol. 2013 Dec;43(12):1181-1188. doi: 10.1016/j.ibmb.2013.09.008.
The silks of arthropods have an elementary role in the natural history of the organisms that spin them, yet they are coded by rapidly evolving genes leading some authors to speculate that silk proteins are non-homologous proteins co-opted multiple times independently for similar functions. However, some general structural patterns are emerging. In this work we identified three major silk gland proteins using a combined biochemical, proteomic, next-generation sequencing and bioinformatic approach. Biochemical characterization determined that they were phosphorylated with multiple isoforms and potentially differential phosphorylation. Structural characterization showed that their structure was more similar to silk proteins from distantly related aquatic Trichopteran species than more closely related terrestrial or aquatic Diptera. Overall, our approach is easily transferable to any non-model species and if used across a larger number of aquatic species, we will be able to better understand the processes involved in linking the secondary structure of silk proteins with their function between in an organisms and its habitat.
节肢动物的丝在其产生丝的生物体的自然历史中起着基本作用，但它们是由快速进化的基因编码的，这使得一些作者推测丝蛋白是非同源蛋白，多次独立地被篡夺用于相似的功能。然而，一些常见的结构模式正在出现。在这项工作中，我们使用了一种组合的生化、蛋白质组学、下一代测序和生物信息学方法，鉴定了三种主要的丝腺蛋白。生化特性确定它们具有多个同工型和潜在的差异磷酸化。结构特征表明，它们的结构与亲缘关系较远的水生蜉蝣目物种的丝蛋白更相似，而与亲缘关系较近的陆地或水生双翅目物种的丝蛋白不相似。总的来说，我们的方法很容易转移到任何非模式物种上，如果在更多的水生物种上使用，我们将能够更好地理解将丝蛋白的二级结构与其在生物体与其栖息地之间的功能联系起来的过程。
