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Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus
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Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus
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Journal Article
Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus
2014
Overview
For construction of the bacterial flagellum, FliI ATPase forms the FliH
2
-FliI complex in the cytoplasm and localizes to the flagellar basal body (FBB) through the interaction of FliH with a C ring protein, FliN. FliI also assembles into a homo-hexamer to promote initial entry of export substrates into the export gate. The interaction of FliH with an export gate protein, FlhA, is required for stable anchoring of the FliI
6
ring to the gate. Here we report the stoichiometry and assembly dynamics of FliI-YFP by fluorescence microscopy with single molecule precision. More than six FliI-YFP molecules were associated with the FBB through interactions of FliH with FliN and FlhA. Single FliI-YFP molecule exchanges between the FBB-localized and free-diffusing ones were observed several times per minute. Neither the number of FliI-YFP associated with the FBB nor FliI-YFP turnover rate were affected by catalytic mutations in FliI, indicating that ATP hydrolysis by FliI does not drive the assembly-disassembly cycle of FliI during flagellar assembly. We propose that the FliH
2
FliI complex and FliI
6
ring function as a dynamic substrate carrier and a static substrate loader, respectively.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 14/63
/ Adenosine Triphosphate - metabolism
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Flagella
/ Humanities and Social Sciences
/ Luminescent Proteins - metabolism
/ Proton-Translocating ATPases - chemistry
/ Proton-Translocating ATPases - genetics
/ Proton-Translocating ATPases - metabolism
/ Science
