PMID:16677309: Difference between revisions
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Revision as of 18:53, 1 September 2013
| Citation |
No author listed (2006) Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export. Mol. Microbiol. 60:984-98 |
|---|---|
| Abstract |
The flagellar switch proteins of Salmonella, FliG, FliM and FliN, participate in the switching of motor rotation, torque generation and flagellar assembly/export. FliN has been implicated in the flagellar export process. To address this possibility, we constructed 10-amino-acid scanning deletions and larger truncations over the C-terminal domain of FliN. Except for the last deletion variant, all other variants were unable to complement a fliN null strain or to restore the export of flagellar proteins. Most of the deletions showed strong negative dominance effects on wild-type cells. FliN was found to associate with FliH, a flagellar export component that regulates the ATPase activity of FliI. The binding of FliM to FliN does not interfere with this FliN-FliH interaction. Furthermore, a five-protein complex consisting of FliG, His-tagged FliM, FliN, FliH and FliI was purified by nickel-affinity chromatography. FliJ, a putative general chaperone, is bound to FliM even in the absence of FliH. The importance of the C ring as a possible docking site for export substrates, chaperones and FliI through FliH for their efficient delivery to membrane components of the export apparatus is discussed. |
| Links |
PubMed Online version:10.1111/j.1365-2958.2006.05149.x |
| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Flagella/metabolism; Genes, Dominant; Genetic Complementation Test; Membrane Proteins/genetics; Membrane Proteins/metabolism; Protein Interaction Mapping; Protein Transport; Salmonella/metabolism; Sequence Deletion |
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