An energy transduction mechanism used in bacterial flagellar type III protein export.

An energy transduction mechanism used in bacterial flagellar type III protein export.
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细菌鞭毛III型蛋白质输出中使用的能量转导机制。

DOI:
10.1038/ncomms1488
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发表时间:
2011-09-20
影响因子:
16.6
通讯作者:
--
中科院分区:
综合性期刊1区
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--
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细菌的鞭毛蛋白由特定的输出装置输出。 FliI ATPase 与 FliH 和 FliJ 形成复合物,并护送底物从细胞质输出至输出门复合物,该复合物由六个膜蛋白组成。输出门复合体利用质子动力穿过细胞质膜进行蛋白质易位,但其机制仍不清楚。在这里,我们证明输出门复合物本身是一个质子-蛋白质逆向转运蛋白,它使用质子动力的两个组成部分,Δψ和ΔpH,用于蛋白质输出过程的不同步骤。然而,在 FliH、FliI 和 FliJ 存在的情况下,FliH-FliI 复合物会引起 FliJ 与输出门膜蛋白 FlhA 的特异性结合,从而将输出门变成高效、Δψ 驱动的蛋白质输出装置。细菌输出门复合体将鞭毛蛋白转运穿过细胞质膜,但这一过程的机制尚不清楚。在这里,输出门复合物被揭示为质子-蛋白质反向转运蛋白,它使用质子动力的不同组成部分来进行输出过程的不同步骤。
Flagellar proteins of bacteria are exported by a specific export apparatus. FliI ATPase forms a complex with FliH and FliJ and escorts export substrates from the cytoplasm to the export gate complex, which is made up of six membrane proteins. The export gate complex utilizes proton motive force across the cytoplasmic membrane for protein translocation, but the mechanism remains unknown. Here we show that the export gate complex by itself is a proton–protein antiporter that uses the two components of proton motive force, Δψ and ΔpH, for different steps of the protein export process. However, in the presence of FliH, FliI and FliJ, a specific binding of FliJ with an export gate membrane protein, FlhA, is brought about by the FliH–FliI complex, which turns the export gate into a highly efficient, Δψ-driven protein export apparatus. A bacterial export gate complex transports flagellar proteins across the cytoplasmic membrane, but the mechanism of this process is unclear. Here, the export gate complex is revealed as a proton–protein antiporter that uses separate components of the proton motive force for different steps of the export process.
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