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首页> 外文期刊>Journal of Molecular Biology >Dimer dynamics and filament organization of the bacterial cell division protein FtsA
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Dimer dynamics and filament organization of the bacterial cell division protein FtsA

机译：细菌细胞分裂蛋白FtsA的二聚体动力学和细丝组织

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摘要

FtsA is a bacterial actin homolog and one of the core proteins involved in cell division. While previous studies have demonstrated the capability of FtsA to polymerize, little is known about its polymerization state in vivo or if polymerization is necessary for FtsA function. Given that one function of FtsA is to tether FtsZ filaments to the membrane, in vivo polymerization of FtsA imposes geometric constraints and requires a specific polymer curvature direction. Here, we report a series of molecular dynamics simulations probing the structural dynamics of FtsA as a dimer and as a tetrameric single filament. We found that the FtsA polymer exhibits a preferred bending direction that would allow for its placement parallel with FtsZ polymers underneath the cytoplasmic membrane. We also identified key interfacial amino acids that mediate FtsA-FtsA interaction and propose that some amino acids play more critical roles than others. We performed in silico mutagenesis on FtsA and demonstrated that, while a moderate mutation at the polymerization interface does not significantly affect polymer properties such as bending direction and association strength, more drastic mutations change both features and could lead to non-functional FtsA.
机译：FtsA是一种细菌肌动蛋白同源物，是参与细胞分裂的核心蛋白之一。尽管先前的研究已经证明了FtsA聚合的能力，但对其在体内的聚合状态或FtsA功能是否需要聚合的了解很少。考虑到FtsA的功能之一是将FtsZ细丝束缚在膜上，FtsA的体内聚合受到几何约束，并且需要特定的聚合物曲率方向。在这里，我们报告了一系列的分子动力学模拟，探讨了FtsA作为二聚体和四聚体单丝的结构动力学。我们发现，FtsA聚合物表现出优选的弯曲方向，使其与细胞质膜下方的FtsZ聚合物平行放置。我们还确定了介导FtsA-FtsA相互作用的关键界面氨基酸，并提出某些氨基酸比其他氨基酸更重要。我们对FtsA进行了计算机诱变，结果表明，虽然聚合界面的中等突变不会显着影响聚合物的特性（例如弯曲方向和缔合强度），但更剧烈的突变会同时改变两个特征并可能导致无功能的FtsA。

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