Modulation of flagellar rotation in surface-attached bacteria: A pathway for rapid surface-sensing after flagellar attachment
Fig 2
The C ring component FliG interacts with FlhF.
FlhF interactions with flagellar proteins were assayed by bacterial two-hybrid assay. ω or Zif fusions were tested as indicated, with interactions resulting in beta-galactosidase expression and activity (reported in Miller units). Bars show mean ± S.D. (n = 3) for a representative experiment. FlhF (WT), which forms a homodimer, served as a positive control (black bar). FliG (G) interacted with wild-type FlhF (WT) (red bars), but gave no signal when co-expressed with either the ω or Zif domain alone (white bars). Other tested rotor components (red bars: FliF (F), FliM (M), or FliN (N)) and stator proteins (blue bars: MotA (A), MotB (B), MotC (C), or MotD (D)) did not show interactions with FlhF.