Reconstructed evolutionary history of the yeast septins Cdc11 and Shs1.
Reconstructed evolutionary history of the yeast septins Cdc11 and Shs1.
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DOI：
10.1093/g3journal/jkaa006
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发表时间：
2021-01-18
期刊：
影响因子：
--
通讯作者：
Finnigan GC
中科院分区：
文献类型：
--
作者：
Takagi J;Cho C;Duvalyan A;Yan Y;Halloran M;Hanson-Smith V;Thorner J;Finnigan GC
Septins是在后生动物中保守的GTP结合蛋白。它们可以聚合成延伸的细丝，因此被认为是细胞骨架的一个组成部分。在整个生命树上，各个隔质的数量是不同的--酵母有7个不同的亚基，线虫(秀丽线虫)有2个，人类有13个。然而，总的几何单位(一个非极异八异构体和由其组装的细丝)是保守的。为了了解Septin的进化变异，我们专注于一对相关的酵母亚单位(CDc11和Shs1)，它们似乎是由真菌分支中的基因复制引起的。CDC11或Shs1在杂八聚体中占据末端位置，但CDc11对Septin功能和细胞活力是必不可少的，而Shs1不是。为了弄清这种差异的分子基础，我们利用祖先基因重建来预测、合成并实验检测CDC11和Shs1的最新共同祖先(Anc.11-S)。S能够占据八聚体的末端位置，就像现代的亚基一样。虽然Anc.11-S提供了CDC11的许多已知功能，但它无法取代Shs1的独特功能(S)。为了进一步评估Shs1的历史，沿着从Anc.11-S到酵母Shs1的建议轨迹，产生并测试了其他中间体。我们证明了Shs1目前的特性是多个事件造成的：(1)Shs1-Shs1在复制后早期失去自结合，(2)相邻异八聚体之间异型CDC11-Shs1相互作用的共同进化，以及(3)其C端延伸域的新功能的最终重新定位和获得(S)。因此，一对复制的蛋白质，尽管受到组装成高度保守的多亚基结构的限制，仍可以通过复杂的进化途径进化出新的功能。
Septins are GTP-binding proteins conserved across metazoans. They can polymerize into extended filaments and, hence, are considered a component of the cytoskeleton. The number of individual septins varies across the tree of life—yeast (Saccharomyces cerevisiae) has seven distinct subunits, a nematode (Caenorhabditis elegans) has two, and humans have 13. However, the overall geometric unit (an apolar hetero-octameric protomer and filaments assembled there from) has been conserved. To understand septin evolutionary variation, we focused on a related pair of yeast subunits (Cdc11 and Shs1) that appear to have arisen from gene duplication within the fungal clade. Either Cdc11 or Shs1 occupies the terminal position within a hetero-octamer, yet Cdc11 is essential for septin function and cell viability, whereas Shs1 is not. To discern the molecular basis of this divergence, we utilized ancestral gene reconstruction to predict, synthesize, and experimentally examine the most recent common ancestor (“Anc.11-S”) of Cdc11 and Shs1. Anc.11-S was able to occupy the terminal position within an octamer, just like the modern subunits. Although Anc.11-S supplied many of the known functions of Cdc11, it was unable to replace the distinct function(s) of Shs1. To further evaluate the history of Shs1, additional intermediates along a proposed trajectory from Anc.11-S to yeast Shs1 were generated and tested. We demonstrate that multiple events contributed to the current properties of Shs1: (1) loss of Shs1–Shs1 self-association early after duplication, (2) co-evolution of heterotypic Cdc11–Shs1 interaction between neighboring hetero-octamers, and (3) eventual repurposing and acquisition of novel function(s) for its C-terminal extension domain. Thus, a pair of duplicated proteins, despite constraints imposed by assembly into a highly conserved multi-subunit structure, could evolve new functionality via a complex evolutionary pathway.
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影响因子：
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作者：
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