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. Author manuscript; available in PMC: 2016 Mar 3.
Published in final edited form as: Structure. 2015 Feb 19;23(3):517–526. doi: 10.1016/j.str.2015.01.012

Figure 2. Mutational Effects on DegS Cleavage of RseA.

Figure 2

Effects of DegS mutations in an otherwise wild-type background (upper panel) or in an H198P background (lower panel) on OMP-peptide stimulated proteolytic activity, expressed as the second-order rate constant (kcat/KM) for RseA cleavage. Values are averages of two or more independent trials ± SEM. Cleavage reactions contained different sub-KM concentrations of 35S-labelled RseA, DegS or variants (1 µM trimer), and YYF OMP peptide (230 µM). Initial cleavage rates normalized by total enzyme were plotted as a function of the RseA concentration, and the second-order rate constant was determined from the slope of a linear fit.