Origin and Diversification of a Salamander Sex Pheromone System
Origin and Diversification of a Salamander Sex Pheromone System
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DOI：
10.1093/molbev/msu316
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发表时间：
2015-02-01
影响因子：
10.7
通讯作者：
Bossuyt, Franky
中科院分区：
文献类型：
--
作者：
Janssenswillen, Sunita;Vandebergh, Wim;Bossuyt, Franky
性信息素在动物王国的许多生物体中形成了生殖策略的重要方面。脊椎动物中已知的最古老的性信息素之一是Sodefrin前体样因子（SPF）系统的蛋白质，它在早期的蝾螈中已经具有求偶功能。蝾螈随后的进化的特点是多样化的求偶和繁殖，但很少有人知道SPF信息素系统如何多样化的求偶策略。在这里，我们结合转录组学，基因组学和系统发育分析，调查的SPF信息素系统的进化在9个蝾螈种不同的求爱显示。首先，我们发现SPF起源于脊椎动物的三指蛋白，并通过在蝾螈中的多个基因复制而多样化，而在青蛙中保持单一拷贝。接下来，我们证明，尾扇蝾螈保留了较高的系统发育多样性的SPF，而损失的尾扇已与泄殖腔区的SPF表达的重要性降低或损失。最后，我们表明，引诱剂十肽sodefrin是从较大的SPF前体，起源于一个62 bp的插入和随之而来的移码在祖先的Cynops血统裂解。这导致了一种新的十肽的诞生，它迅速进化出一种独立于未切割蛋白质的信息素功能。
Sex pheromones form an important facet of reproductive strategies in many organisms throughout the Animal Kingdom. One of the oldest known sex pheromones in vertebrates are proteins of the Sodefrin Precursor-like Factor (SPF) system, which already had a courtship function in early salamanders. The subsequent evolution of salamanders is characterized by a diversification in courtship and reproduction, but little is known on how the SPF pheromone system diversified in relation to changing courtship strategies. Here, we combined transcriptomic, genomic, and phylogenetic analyses to investigate the evolution of the SPF pheromone system in nine salamandrid species with distinct courtship displays. First, we show that SPF originated from vertebrate three-finger proteins and diversified through multiple gene duplications in salamanders, while remaining a single copy in frogs. Next, we demonstrate that tail-fanning newts have retained a high phylogenetic diversity of SPFs, whereas loss of tail-fanning has been associated with a reduced importance or loss of SPF expression in the cloacal region. Finally, we show that the attractant decapeptide sodefrin is cleaved from larger SPF precursors that originated by a 62 bp insertion and consequent frameshift in an ancestral Cynops lineage. This led to the birth of a new decapeptide that rapidly evolved a pheromone function independently from uncleaved proteins.