The bacterial flagellum is a supramolecular motility machine consisting of the basal body, the hook, and the filament. For construction of the flagellum beyond the cellular membranes, a type III protein export apparatus uses ATP and proton-motive force (PMF) across the cytoplasmic membrane as the energy sources to transport flagellar component proteins from the cytoplasm to the distal end of the growing flagellar structure. The protein export apparatus consists of a PMF-driven transmembrane export gate complex and a cytoplasmic ATPase complex. In addition, the basal body C ring acts as a sorting platform for the cytoplasmic ATPase complex that efficiently brings export substrates and type III export chaperone–substrate complexes from the cytoplasm to the export gate complex. In this book chapter, we will summarize our current understanding of molecular organization and assembly of the flagellar type III protein export apparatus.
CITATION STYLE
Minamino, T., Kawamoto, A., Kinoshita, M., & Namba, K. (2020). Molecular organization and assembly of the export apparatus of flagellar type III secretion systems. In Current Topics in Microbiology and Immunology (Vol. 427, pp. 91–107). Springer Science and Business Media Deutschland GmbH. https://doi.org/10.1007/82_2019_170
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