Modulation of flagellar rotation in surface-attached bacteria: A pathway for rapid surface-sensing after flagellar attachment
Fig 3
FimV(L7P) is a suppressor of FlhF(R251G).
(A) FimV constructs. The predicted signal sequence (SS, red), LysM domain (white), periplasmic region (grey), transmembrane helix (TM, black) and tetratricopeptide repeats (TPR) (blue) are diagrammed. ω or Zif fusions for bacterial 2-hybrid screen are also shown (B2H, green). (B) Loss of FimV function suppresses FlhF(R251G). Swimming zone diameters of PAK (black), PAK fimV(L7P) (red), PA14 (blue) and PA14 fimV::Tn (green) harboring either pUCP (vector control (VC)) or pFlhF(R251G) (open) are shown; each symbol is a biological replicate (line indicates mean). Disruption of fimV significantly alters swimming behavior of FlhF(R251G)-overexpressing bacteria (***, p < 0.001; 2 way ANOVA followed by Bonferroni posttest). (C) Pil/Chp system mutants associated with low intracellular [cAMP] do not suppress FlhF(R251G). Wild-type and transposon mutant bacteria harboring either empty vector (pUCP; solid) or pFlhF(R251G) (open) were assayed for swimming motility. Each symbol is a biological replicate; line indicates mean. Only disruption of fimV suppresses the dominant-negative phenotype associated with FlhF(R251G) overexpression (***, p < 0.001; 2 way ANOVA with Bonferroni posttest).