Fig. 1: FimT is critical for the transformation of L. pneumophila and binds to DNA.
From: The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation
a Natural transformation efficiencies of the parental L. pneumophila Lp02 strain and Lp02 strains harbouring deletions of genes known to play a role in transformation compared to the fimU and fimT deletion strains. The ΔfimT strain was complemented by ectopic expression of wild-type FimT, under the control of an IPTG-inducible promoter. The mean transformation efficiencies of three independent biological replicates is shown (error bars represent standard deviation [SD]). < d.l., below detection limit (d.l.) (average d.l. = 2.0 × 10−8 ± 8.2 × 10−9). Statistical significances of transformation differences were determined on log-transformed83 data using an unpaired two-sided t-test with Welch’s correction. All strains were compared to the parental strain. n.s., not statistically significant, p > 0.05 (pΔfimU = 0.39; pΔfimT Ptac-fimT = 0.89). b In vitro DNA binding of purified L. pneumophila PilA1, PilA2, FimU and FimT assessed by an EMSA. A 30 bp dsDNA fragment (1 µM) was incubated with increasing concentrations of purified pilins (0–100 µM) and resolved by agarose gel electrophoresis. This experiment was independently performed three times with reproducible results. c ITC binding studies of wild-type FimT binding to 12meric dsDNA (left) and ssDNA (right). In both cases, DNA (syringe) was injected into FimT (cell). Data were fitted using the “one set” of sites model, assuming that both binding sites on the dsDNA are of equal affinity. Source data are provided as a Source Data file.
