Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus
Por:
Minamino T., Yoshimura, SDJ, Morimoto Y.V., González-Pedrajo B., Kami-Ike N., Namba K.
Publicada:
1 dic 2009
Resumen:
P>Most bacterial flagellar proteins are exported by the flagellar type III protein export apparatus for their self-assembly. FliI ATPase forms a complex with its regulator FliH and facilitates initial entry of export substrates to the export gate composed of six integral membrane proteins. The FliH-FliI complex also binds to the C ring of the basal body through a FliH-FliN interaction for efficient export. However, it remains unclear how these reactions proceed within the cell. Here, we analysed subcellular localization of FliI-YFP by fluorescence microscopy. FliI-YFP was localized to the flagellar base, and its localization required both FliH and the C ring. The ATPase activity of FliI was not required for its localization. FliI-YFP formed a complex with FliH Delta 1 (missing residues 2-10) but the complex did not show any localization. FliH Delta 1 did not interact with FliN, and alanine-scanning mutagenesis revealed that only Trp-7 and Trp-10 of FliH are essential for the interactio
Filiaciones:
Minamino T.:
Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
PRESTO, JST, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan
Morimoto Y.V.:
Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
González-Pedrajo B.:
Univ Nacl Autonoma Mexico, Dept Mol Genet, Inst Fisiol Celular, Mexico City 04510, DF, Mexico
Kami-Ike N.:
Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
Namba K.:
Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan
Bronze
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