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FliH and FliI ensure efficient energy coupling of flagellar type III protein export in Salmonella

机译：FliH和FliI确保沙门氏菌中鞭毛III型蛋白出口的有效能量耦合

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Abstract For construction of the bacterial flagellum, flagellar proteins are exported via its specific export apparatus from the cytoplasm to the distal end of the growing flagellar structure. The flagellar export apparatus consists of a transmembrane (TM) export gate complex and a cytoplasmic ATPase complex consisting of FliH, FliI, and FliJ. FlhA is a TM export gate protein and plays important roles in energy coupling of protein translocation. However, the energy coupling mechanism remains unknown. Here, we performed a cross-complementation assay to measure robustness of the energy transduction system of the export apparatus against genetic perturbations. Vibrio FlhA restored motility of a Salmonella ???? flhA mutant but not that of a ???? fliH-fliI flhB(P28T) ???? flhA mutant. The flgM mutations significantly increased flagellar gene expression levels, allowing Vibrio FlhA to exert its export activity in the ???? fliH-fliI flhB(P28T) ???? flhA mutant. Pull-down assays revealed that the binding affinities of Vibrio FlhA for FliJ and the FlgN?￠????FlgK chaperone?￠????substrate complex were much lower than those of Salmonella FlhA. These suggest that Vibrio FlhA requires the support of FliH and FliI to efficiently and properly interact with FliJ and the FlgN?￠????FlgK complex. We propose that FliH and FliI ensure robust and efficient energy coupling of protein export during flagellar assembly.
机译：摘要对于细菌鞭毛的构建，鞭毛蛋白通过其特定的输出设备从细胞质输出到生长的鞭毛结构的远端。鞭毛输出设备由跨膜（TM）输出门复合物和由FliH，FliI和FliJ组成的胞质ATPase复合物组成。 FlhA是一种TM出口门蛋白，在蛋白易位的能量耦合中起重要作用。然而，能量耦合机制仍然未知。在这里，我们进行了交叉互补分析，以测量出口设备的能量转换系统对遗传干扰的鲁棒性。弧菌FlhA恢复了沙门氏菌的活力flhA突变体，但不是????的突变体fliH-fliI flhB（P28T）???? flhA突变体。 flgM突变显着增加鞭毛基因的表达水平，使FlhA弧菌能在??????中发挥其出口活性。 fliH-fliI flhB（P28T）???? flhA突变体。下拉测定法表明，弧菌FlhA对FliJ和FlgNΔβΔFlgK分子伴侣ΔβΔ底物复合物的结合亲和力远低于沙门氏菌FlhA。这些表明弧菌FlhA需要FliH和FliI的支持才能有效和适当地与FliJ和FlgNΔFgK复合物相互作用。我们建议FliH和FliI确保鞭毛装配过程中蛋白质输出的鲁棒和有效的能量耦合。

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