Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy.
Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy.
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DOI：
10.1021/acs.nanolett.5b04259
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发表时间：
2016-03-09
期刊：
影响因子：
10.8
通讯作者：
Liu LN
中科院分区：
文献类型：
--
作者：
Sutter M;Faulkner M;Aussignargues C;Paasch BC;Barrett S;Kerfeld CA;Liu LN
细菌微区室（bacterial microcompartments，BMCs）是广泛存在于细菌门中的蛋白质细胞器。它们将酶分隔在可选择性渗透的外壳内，并在CO2固定，发病机制和微生物生态学中发挥重要作用。在这里，我们结合联合收割机X射线晶体学和高速原子力显微镜表征，在分子分辨率，BMC壳面组件的结构和动力学。我们的研究结果表明，预先形成的六聚体组装成均匀取向的壳层，一个单一的六聚体厚。观察了壳体刻面装配的动态过程。壳六聚体可以从组装的片材中解离并并入组装的片材中，表明灵活的分子间相互作用。此外，我们证明了壳蛋白的自组装和动力学是由特定的接触壳蛋白的界面。我们的研究为BMC壳面的形成，相互作用和动力学提供了新的见解，这对于基于BMC架构的自组装生物纳米反应器和支架的设计和工程至关重要。
Bacterial microcompartments (BMCs) are proteinaceous organelles widespread among bacterial phyla. They compartmentalize enzymes within a selectively permeable shell and play important roles in CO2 fixation, pathogenesis, and microbial ecology. Here, we combine X-ray crystallography and high-speed atomic force microscopy to characterize, at molecular resolution, the structure and dynamics of BMC shell facet assembly. Our results show that preformed hexamers assemble into uniformly oriented shell layers, a single hexamer thick. We also observe the dynamic process of shell facet assembly. Shell hexamers can dissociate from and incorporate into assembled sheets, indicating a flexible intermolecular interaction. Furthermore, we demonstrate that the self-assembly and dynamics of shell proteins are governed by specific contacts at the interfaces of shell proteins. Our study provides novel insights into the formation, interactions, and dynamics of BMC shell facets, which are essential for the design and engineering of self-assembled biological nanoreactors and scaffolds based on BMC architectures.