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Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

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Protein export through the bacterial flagellar type III export pathway.

Tohru Minamino¹

¹Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.

Biochimica Et Biophysica Acta

|September 26, 2013

Summary

The bacterial flagellum

Area of Science:

Bacterial motility and flagellar assembly
Protein secretion systems
Molecular mechanisms of transport

Background:

The bacterial flagellum is crucial for motility.
Its assembly relies on a type III export apparatus.
This apparatus uses energy from ATP and proton motive force.

Purpose of the Study:

To elucidate the molecular mechanisms of the flagellar type III export apparatus.
To understand how energy sources drive flagellar protein export.
To detail the roles of chaperones and export gate components.

Main Methods:

Analysis of protein-protein interactions within the export apparatus.
Investigating the roles of chaperones (FlgN, FliS, FliT).
Characterizing the function of the export gate (FlhA, FlhB, etc.) and ATPase ring (FliH, FliI, FliJ).

Keywords:

ATPase Bacterial flagellum Chaperone Flagellar assembly Proton motive force Type III protein export

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Main Results:

The export apparatus comprises a membrane-embedded gate and a soluble ATPase ring.
Chaperones protect and deliver substrates to the export gate.
The export gate functions as a proton-protein antiporter, utilizing proton motive force.
ATP hydrolysis drives the ATPase ring's assembly-disassembly cycle for efficient export.

Conclusions:

The flagellar type III export apparatus is a sophisticated machine.
It efficiently exports flagellar proteins using both ATP and proton motive force.
Specific interactions between components like FlhA and FliJ are key for energy transduction.