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首页> 外文期刊>Biochemistry >Mechanistic Insights into the Lipid Interaction of an Ancient Saposin-like Protein
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Mechanistic Insights into the Lipid Interaction of an Ancient Saposin-like Protein

机译：古老的鞘脂蛋白样蛋白的脂质相互作用的力学见解。

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摘要

The members of the expanding family of saposin-like proteins (SAPLIPs) have various biological functions in plants, animals, and humans. In addition to a similar protein backbone, these proteins have in common the fact that they interact with lipid membranes. According to their phylogenetic position, it has long been thought that amoeboid protozoans produce archetypes of SAPLIPs and that these are lytic proteins that can perforate membranes of prokaryotic and eukaryotic target cells. Here, we show that an amoebic SAPLIP from Entamoeba invadens does not form lytic pores in membranes but displays several characteristics that are known from human saposins. The protein named invaposin changes the conformation from a closed to an open form in the presence of lipid membranes, acts in a pH-dependent manner, selectively binds anionic lipids, aggregates lipid vesicles of the preferred composition, and dimerizes upon acidification. Our data indicate that the principal features of the lipid-binding saposins evolved long before the appearance of the vertebrate lineage and push the origin of saposins even deeper down the phylogenetic tree to unicellular organisms.
机译：扩展的鞘脂蛋白样蛋白（SAPLIPs）家族的成员在植物，动物和人类中具有多种生物学功能。除了类似的蛋白质骨架外，这些蛋白质还具有与脂质膜相互作用的事实。根据它们的系统发育位置，长期以来一直认为变形虫原虫产生SAPLIP的原型，并且这些是可以穿透原核和真核靶细胞膜的裂解蛋白。在这里，我们显示了来自Entamoeba invadens的一种厌氧SAPLIP不会在膜上形成裂解孔，而是显示出从人鞘脂蛋白酶已知的几个特征。在脂质膜存在的情况下，名为invaposin的蛋白质将构象从封闭形式改变为开放形式，以pH依赖性方式起作用，选择性结合阴离子脂质，聚集优选组成的脂质囊泡，并在酸化时二聚。我们的数据表明，脂质结合的脂多糖的主要特征在脊椎动物谱系出现之前就已经进化了很长时间，并将脂多糖的起源进一步推到了系统发育树的深处，成为单细胞生物。

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