Figure 5
From: Extragenic suppressor mutations in ΔripA disrupt stability and function of LpxA
RipA is necessary for stability of LpxA. (A) Relative protein concentrations were determined from mid log phase cultures treated with 1.75 mg ml−1 chloramphenicol for an hour to stop protein translation. The relative abundance of LpxA protein was quantified using Image J with IglB as a loading control for equal protein from three independent experiments. Statistical significance was determined by comparing LpxA-HA adjusted relative protein values for wild type to each of the respective mutants. *, P < 0.05; **, P < 0.005. (B) Representative Western blot probed for LpxA-HA and IglB protein loaded with equal protein. (C) Transcript levels of lpxA in wild type F. tularensis and the ∆ripA strain measured by qRT-PCR. Data represent the relative transcript of lpxA normalized to gyrA from three independent experiments done in triplicate and the relative transcripts were not statistically different.