Fig. 1: LapB is an adaptor specific for FtsH-mediated LpxC degradation.
From: Regulatory mechanisms of lipopolysaccharide synthesis in Escherichia coli
a Kinetic analysis of LpxC degradation with proteoliposomes (PL). The initial rates of LpxC degraded by FtsH or FtsH/LapB proteoliposomes were fitted to the Michaelis-Menten equation, and KM and Vmax were estimated. b Effect of replacing LapB’s TM helix. His-tagged wild-type or chimeric LapB proteins were expressed and affinity-purified from bacteria, and co-elution of FtsH was examined. The normalized ratio of SDS-PAGE intensities of co-eluted FtsH and LapB bands are listed below the lane of elution. Sup., supernatant of detergent-solubilized membrane after ultracentrifugation; F.T., flow-through. c LapBcyto concentration-dependent inhibition of LpxC degradation by the FtsH/LapB proteoliposomes. The degradation rate without LapBcyto was set to 100% and used to normalize rates of LpxC degradation with different LapBcyto concentrations. For the kinetic analysis and inhibition assay, each experiment was repeated three times and all data were presented as mean values with error bars representing standard deviations (SDs) of triplicates. Source data for (a) and (c) are provided as a Source Data file.
