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首页> 外文期刊>Journal of bacteriology >An Actin Homolog of the Archaeon Thermoplasma acidophilum That Retains the Ancient Characteristics of Eukaryotic Actin
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An Actin Homolog of the Archaeon Thermoplasma acidophilum That Retains the Ancient Characteristics of Eukaryotic Actin

机译：嗜酸性古生菌古菌的肌动蛋白同源物，保留了真核肌动蛋白的古代特征

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摘要

Actin, a central component of the eukaryotic cytoskeleton, plays a crucial role in determining cell shape in addition to several other functions. Recently, the structure of the archaeal actin homolog Ta0583, isolated from the archaeon Thermoplasma acidophilum, which lacks a cell wall, was reported by Roeben et al. (J. Mol. Biol. >358:145-156, 2006). Here we show that Ta0583 assembles into bundles of filaments similar to those formed by eukaryotic actin. Specifically, Ta0583 forms a helix with a filament width of 5.5 nm and an axial repeating unit of 5.5 nm, both of which are comparable to those of eukaryotic actin. Eukaryotic actin shows a greater resemblance to Ta0583 than to bacterial MreB and ParM in terms of polymerization characteristics, such as the requirement for Mg2+, critical concentration, and repeating unit size. Furthermore, phylogenetic analysis also showed a closer relationship between Ta0583 and eukaryotic actin than between MreB or ParM and actin. However, the low specificity of Ta0583 for nucleotide triphosphates indicates that Ta0583 is more primitive than eukaryotic actin. Taken together, our results suggest that Ta0583 retains the ancient characteristics of eukaryotic actin.
机译：肌动蛋白是真核细胞骨架的重要组成部分，除其他几个功能外，在决定细胞形状方面也起着至关重要的作用。最近，Roeben等人报道了从缺乏细胞壁的古细菌嗜酸嗜热菌分离的古细菌肌动蛋白同源物Ta0583的结构。 （J.Mol.Biol。> 358： 145-156，2006年）。在这里，我们显示Ta0583组装成类似于真核肌动蛋白形成的细丝束。具体地，Ta0583形成丝线宽度为5.5nm和轴向重复单元为5.5nm的螺旋，两者均与真核肌动蛋白相当。就聚合特性而言，如对Mg 2 + 的要求，临界浓度和重复单元大小，真核肌动蛋白与Ta0583的相似性比与细菌MreB和ParM的相似。此外，系统发育分析还显示，Ta0583与真核肌动蛋白之间的关系比MreB或ParM与肌动蛋白之间的关系更紧密。然而，Ta0583对三磷酸核苷酸的低特异性表明Ta0583比真核肌动蛋白更原始。两者合计，我们的结果表明Ta0583保留了真核生物肌动蛋白的古老特征。

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