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沙门氏菌鞭毛蛋白 FliI 的正电荷区域对于 ATP 酶的形成和有效的鞭毛蛋白输出是必需的。

A positive charge region of Salmonella FliI is required for ATPase formation and efficient flagellar protein export.

机构信息

Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan.

RIKEN SPring-8 Center and Center for Biosystems Dynamics Research, Suita, Osaka, Japan.

出版信息

Commun Biol. 2021 Apr 12;4(1):464. doi: 10.1038/s42003-021-01980-y.

DOI:10.1038/s42003-021-01980-y
PMID:33846530
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8041783/
Abstract

The FliHFliI complex is thought to pilot flagellar subunit proteins from the cytoplasm to the transmembrane export gate complex for flagellar assembly in Salmonella enterica. FliI also forms a homo-hexamer to hydrolyze ATP, thereby activating the export gate complex to become an active protein transporter. However, it remains unknown how this activation occurs. Here we report the role of a positively charged cluster formed by Arg-26, Arg-27, Arg-33, Arg-76 and Arg-93 of FliI in flagellar protein export. We show that Arg-33 and Arg-76 are involved in FliI ring formation and that the fliI(R26A/R27A/R33A/R76A/R93A) mutant requires the presence of FliH to fully exert its export function. We observed that gain-of-function mutations in FlhB increased the probability of substrate entry into the export gate complex, thereby restoring the export function of the ∆fliH fliI(R26A/R27A/R33A/R76A/R93A) mutant. We suggest that the positive charge cluster of FliI is responsible not only for well-regulated hexamer assembly but also for substrate entry into the gate complex.

摘要

FliHFliI 复合物被认为将鞭毛亚基蛋白从细胞质导向跨膜输出门复合物，以便在沙门氏菌中进行鞭毛组装。FliI 还形成同源六聚体以水解 ATP，从而激活输出门复合物成为活性蛋白转运体。然而，这种激活是如何发生的仍然未知。在这里，我们报告了 FliI 中的由 Arg-26、Arg-27、Arg-33、Arg-76 和 Arg-93 形成的正电荷簇在鞭毛蛋白输出中的作用。我们表明 Arg-33 和 Arg-76 参与了 FliI 环的形成，并且 fliI(R26A/R27A/R33A/R76A/R93A)突变体需要 FliH 的存在才能充分发挥其输出功能。我们观察到 FlhB 的功能获得性突变增加了底物进入输出门复合物的概率，从而恢复了 ∆fliH fliI(R26A/R27A/R33A/R76A/R93A)突变体的输出功能。我们认为 FliI 的正电荷簇不仅负责调节良好的六聚体组装，而且负责底物进入门复合物。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/0f6647c051a3/42003_2021_1980_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/67a691db2cbc/42003_2021_1980_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/9c0b359d6a70/42003_2021_1980_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/4f8134ac946e/42003_2021_1980_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/814336871879/42003_2021_1980_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/21beac1d1d52/42003_2021_1980_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/b6c1531137f1/42003_2021_1980_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/ceba933eedc5/42003_2021_1980_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/a33fff8034a8/42003_2021_1980_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/0f6647c051a3/42003_2021_1980_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/67a691db2cbc/42003_2021_1980_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/9c0b359d6a70/42003_2021_1980_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/4f8134ac946e/42003_2021_1980_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/814336871879/42003_2021_1980_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/21beac1d1d52/42003_2021_1980_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/b6c1531137f1/42003_2021_1980_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/ceba933eedc5/42003_2021_1980_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/a33fff8034a8/42003_2021_1980_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6c9f/8041783/0f6647c051a3/42003_2021_1980_Fig9_HTML.jpg

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