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- Title
Role of the N-terminal domain of FliI ATPase in bacterial flagellar protein export
- Authors
Okabe, Mayuko; Minamino, Tohru; Imada, Katsumi; Namba, Keiichi; Kihara, May
- Abstract
Abstract: FliI, the ATPase involved in bacterial flagellar protein export, forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins. The extreme N-terminal region of FliI is involved not only in its interaction with FliH but also in its oligomerization, but the regulatory mechanism of oligomerization remains unclear. Using in-frame 10-residue deletions within the 100 residues of the N-terminal domain, we demonstrate that the first 20 residues are required for FliH binding and that the conformation of the N-terminal domain is sensitive to the export function, even though the oligomerization and FliH-binding ability are retained and the ATPase activity is maintained in most of the deletion variants.
- Subjects
ADENOSINE triphosphatase; BACTERIAL proteins; FLAGELLA (Microbiology); MEMBRANE proteins; PROTEIN binding; CONFORMATIONAL analysis
- Publication
FEBS Letters, 2009, Vol 583, Issue 4, p743
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.01.026