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Characterization of Small HSPs from Anemonia viridis Reveals Insights into Molecular Evolution of Alpha Crystallin Genes among Cnidarians

机译:表征从小海葵的小HSPs揭示洞察的阿尔法Crystallin基因的分子进化。

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摘要

Gene family encoding small Heat-Shock Proteins (sHSPs containing α-crystallin domain) are found both in prokaryotic and eukaryotic organisms; however, there is limited knowledge of their evolution. In this study, two small HSP genes termed AvHSP28.6 and AvHSP27, both organized in one intron and two exons, were characterised in the Mediterranean snakelocks anemone Anemonia viridis. The release of the genome sequence of Hydra magnipapillata and Nematostella vectensis enabled a comprehensive study of the molecular evolution of α-crystallin gene family among cnidarians. Most of the H. magnipapillata sHSP genes share the same gene organization described for AvHSP28.6 and AvHSP27, differing from the sHSP genes of N. vectensis which mainly show an intronless architecture. The different genomic organization of sHSPs, the phylogenetic analyses based on protein sequences, and the relationships among Cnidarians, suggest that the A.viridis sHSPs represent the common ancestor from which H. magnipapillata genes directly evolved through segmental genome duplication. Additionally retroposition events may be considered responsible for the divergence of sHSP genes of N. vectensis from A. viridis. Analyses of transcriptional expression profile showed that AvHSP28.6 was constitutively expressed among different tissues from both ectodermal and endodermal layers of the adult sea anemones, under normal physiological conditions and also under different stress condition. Specifically, we profiled the transcriptional activation of AvHSP28.6 after challenges with different abiotic/biotic stresses showing induction by extreme temperatures, heavy metals exposure and immune stimulation. Conversely, no AvHSP27 transcript was detected in such dissected tissues, in adult whole body cDNA library or under stress conditions. Hence, the involvement of AvHSP28.6 gene in the sea anemone defensome is strongly suggested.
机译:在原核生物和真核生物中均发现了编码小的热休克蛋白(含有α-晶状蛋白结构域的sHSP)的基因家族。但是,关于它们的进化的知识很少。在这项研究中,被称为AvHSP28.6和AvHSP27的两个小的HSP基因,都组织在一个内含子和两个外显子中,在地中海蛇lock海葵Anemonia viridis中得到了表征。九头蛇和V. Nematostella vectensis的基因组序列的释放,使对虫中α-晶状体蛋白基因家族的分子进化有了全面的研究。大部分的magnipapillata sHSP基因都具有与AvHSP28.6和AvHSP27所述相同的基因组织,不同于主要表现出无内含子结构的N. vectensis sHSP基因。 sHSPs的不同基因组组织,基于蛋白质序列的系统发育分析以及Cnidarians之间的关系表明,拟南芥sHSPs代表了通过片段基因组复制直接从中进化出的magnipapillata基因的共同祖先。另外,可认为逆转录事件是造成绿葡萄球菌的sHSP基因与绿假丝酵母的差异的原因。转录表达谱分析表明,AvHSP28.6在正常生理条件下以及在不同胁迫条件下,在成年海葵的外胚层和内胚层各层之间组成性表达。具体来说,我们描述了在具有不同非生物/生物胁迫的攻击后,AvHSP28.6的转录激活,这些非生物/生物胁迫显示了极端温度,重金属暴露和免疫刺激的诱导。相反,在这种解剖组织,成人全身cDNA文库中或在压力条件下均未检测到AvHSP27转录本。因此,强烈建议AvHSP28.6基因参与海葵防御体。

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