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细菌鞭毛的自组装及III型蛋白质输出

Self-assembly and type III protein export of the bacterial flagellum.

作者信息

Minamino Tohru, Namba Keiichi

机构信息

Dynamic NanoMachine Project, ICORP, JST, Osaka, Japan.

出版信息

J Mol Microbiol Biotechnol. 2004;7(1-2):5-17. doi: 10.1159/000077865.

Abstract

The bacterial flagellum is a supramolecular structure consisting of a basal body, a hook and a filament. Most of the flagellar components are translocated across the cytoplasmic membrane by the flagellar type III protein export apparatus in the vicinity of the flagellar base, diffuse down the narrow channel through the nascent structure and self-assemble at its distal end with the help of a cap structure. Flagellar proteins synthesized in the cytoplasm are targeted to the export apparatus with the help of flagellum-specific chaperones and pushed into the channel by an ATPase, whose activity is controlled by its regulator to enable the energy of ATP hydrolysis to be efficiently coupled to the translocation reaction. The export apparatus switches its substrate specificity by monitoring the state of flagellar assembly in the cell exterior, allowing this huge and complex macromolecular assembly to be built efficiently by a highly ordered and well-regulated assembly process.

摘要

细菌鞭毛是一种超分子结构,由基体、钩形鞘和鞭毛丝组成。大多数鞭毛成分通过鞭毛基部附近的III型蛋白质输出装置转运穿过细胞质膜,沿着狭窄通道扩散通过新生结构,并在帽状结构的帮助下在其远端自我组装。在细胞质中合成的鞭毛蛋白在鞭毛特异性伴侣蛋白的帮助下靶向输出装置,并由ATP酶推入通道,该ATP酶的活性由其调节因子控制,以使ATP水解的能量有效地与转运反应偶联。输出装置通过监测细胞外部鞭毛组装的状态来切换其底物特异性,从而使这个巨大而复杂的大分子组装体能够通过高度有序且调控良好的组装过程高效构建。

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