ArticlemBio2026
The FliI ATPase couples ATP hydrolysis to substrate switching in bacterial flagellar type-III secretion.
Article in mBio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Structural basis for substrate specificity switching revealed by the FlhA(A489E) suppressor mutation.Biophysics and physicobiology · 2026Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial flagella are assembled by a specialized type-III secretion system that exports structural subunits in a defined order. While the ATPase FliI is known to couple ATP hydrolysis to substrate translocation, its role in the transition between early and late secretion stages has remained unclear. Here, we systematically analyzed IMPORTANCE: The ordered export of substrates by bacterial type-III secretion systems is essential for the assembly of complex surface structures such as the flagellum, yet the mechanisms that control the timing of substrate switching remain poorly understood. The flagellar type-III secretion system ATPase FliI has previously been implicated in coupling ATP hydrolysis to activation of the proton motive force-driven export apparatus, although its precise role in secretion remains incompletely understood. Here, we show that FliI contributes to the transition from early to late substrate export during flagellar biogenesis. Using mutants of the catalytic domain of FliI in
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