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Vol. 7, No. 1-2, 2004
Issue release date: May 2004
J Mol Microbiol Biotechnol 2004;7:5–17
(DOI:10.1159/000077865)

Self-Assembly and Type III Protein Export of the Bacterial Flagellum

Minamino T. · Namba K.
aDynamic NanoMachine Project, ICORP, JST, bGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan

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Abstract

The bacterial flagellum is a supramolecular structure consisting of a basal body, a hook and a filament. Most of the flagellar components are translocated across the cytoplasmic membrane by the flagellar type III protein export apparatus in the vicinity of the flagellar base, diffuse down the narrow channel through the nascent structure and self-assemble at its distal end with the help of a cap structure. Flagellar proteins synthesized in the cytoplasm are targeted to the export apparatus with the help of flagellum-specific chaperones and pushed into the channel by an ATPase, whose activity is controlled by its regulator to enable the energy of ATP hydrolysis to be efficiently coupled to the translocation reaction. The export apparatus switches its substrate specificity by monitoring the state of flagellar assembly in the cell exterior, allowing this huge and complex macromolecular assembly to be built efficiently by a highly ordered and well-regulated assembly process.



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