MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly
MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly
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DOI：
10.1073/pnas.1419388112
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发表时间：
2015-03
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通讯作者：
J. Schuhmacher;F. Rossmann;Felix Dempwolff;C. Knauer;F. Altegoer;Wieland Steinchen;Anja K. Dörrich;A. Klingl;Milena Stephan;U. Linne;K. Thormann;G. Bange
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作者：
J. Schuhmacher;F. Rossmann;Felix Dempwolff;C. Knauer;F. Altegoer;Wieland Steinchen;Anja K. Dörrich;A. Klingl;Milena Stephan;U. Linne;K. Thormann;G. Bange
意义 鞭毛是细菌运动的细胞器。鞭毛的数量和位置（鞭毛模式）是物种特异性的，代表了微生物学中最早的分类标准之一。在每一轮细胞分裂期间，细菌都会复制其鞭毛模式。 FlhG 对于多种鞭毛模式（例如极性、横向）至关重要，其机制尚不清楚。我们发现 FlhG 是一种类似 MinD 的 ATP 酶，它以不依赖于核苷酸的方式与鞭毛 C 环蛋白 FliM/FliY 相互作用。 FlhG 激活 FliM/FliY 与 C 环蛋白 FliG 组装。 ATP 和脂质强烈增强 FlhG 驱动的 FliM/FliY/FliG 复合物组装。我们发现鞭毛构件的结构多样性被低估了，这些构件有助于形成不同的鞭毛模式。鞭毛（细菌运动的细胞器）的数量和位置是物种特异性的，并且以规则的模式出现，代表了微生物学中最早的分类标准之一。然而，人们对在每一轮细胞分裂期间可重复地建立这些模式的机制知之甚少。 FlhG（以前称为 YlxH）是各种鞭毛模式的主要决定因素。在这里，我们证明 FlhG 是 ATPase MinD 的结构同源物，其用于细胞分裂位点的确定。与 MinD 一样，FlhG 形成依赖于 ATP 和脂质的同二聚体。它与革兰氏阳性、周鞭毛枯草芽孢杆菌和革兰氏阴性、极性鞭毛腐败希瓦氏菌中的鞭毛 C 环蛋白 FliM 和 FliY（也称为 FliN）复合物相互作用。 FlhG 以不依赖于核苷酸的方式与 FliM/FliY 相互作用，并在体外激活 FliM/FliY 与 C 环蛋白 FliG 组装。 ATP 和脂质强烈增强 FlhG 驱动的 FliM/FliY/FliG 复合物组装。该蛋白在细胞质和鞭毛基体之间显示出高度动态的亚细胞分布，表明 FlhG 在 C 环组装过程中影响鞭毛的位置和数量。我们描述了 MinD 样 ATP 酶向鞭毛模式效应器的分子进化，并表明 C 环蛋白的结构多样性未被充分认识，可能有助于不同鞭毛模式的形成。
Significance Flagella are bacterial organelles of locomotion. The number and location of flagella (flagellation pattern) are species specific and represent one of the earliest taxonomic criteria in microbiology. During each round of cell division, bacteria reproduce their flagellation pattern. FlhG is essential to a variety of flagellation patterns (e.g., polar, lateral) by yet-unknown mechanisms. We show that FlhG is an MinD-like ATPase that interacts with the flagellar C-ring proteins FliM/FliY in a nucleotide-independent manner. FlhG activates FliM/FliY to assemble with the C-ring protein FliG. FlhG-driven assembly of the FliM/FliY/FliG complex is strongly enhanced by ATP and lipids. We identify an underappreciated structural diversity of flagellar building blocks that contribute to formation of different flagellation patterns. The number and location of flagella, bacterial organelles of locomotion, are species specific and appear in regular patterns that represent one of the earliest taxonomic criteria in microbiology. However, the mechanisms that reproducibly establish these patterns during each round of cell division are poorly understood. FlhG (previously YlxH) is a major determinant for a variety of flagellation patterns. Here, we show that FlhG is a structural homolog of the ATPase MinD, which serves in cell-division site determination. Like MinD, FlhG forms homodimers that are dependent on ATP and lipids. It interacts with a complex of the flagellar C-ring proteins FliM and FliY (also FliN) in the Gram-positive, peritrichous-flagellated Bacillus subtilis and the Gram-negative, polar-flagellated Shewanella putrefaciens. FlhG interacts with FliM/FliY in a nucleotide-independent manner and activates FliM/FliY to assemble with the C-ring protein FliG in vitro. FlhG-driven assembly of the FliM/FliY/FliG complex is strongly enhanced by ATP and lipids. The protein shows a highly dynamic subcellular distribution between cytoplasm and flagellar basal bodies, suggesting that FlhG effects flagellar location and number during assembly of the C-ring. We describe the molecular evolution of a MinD-like ATPase into a flagellation pattern effector and suggest that the underappreciated structural diversity of the C-ring proteins might contribute to the formation of different flagellation patterns.