Figure 4 | Scientific Reports

Figure 4

From: Dual regulation of activity and intracellular localization of the PASTA kinase PrkC during Bacillus subtilis growth

Figure 4

PrkC binds PG. Oligomerization of PrkC, PrkC(R500A) and PrkCc in the presence of increasing concentrations of PG fragments. (A) Correlograms displaying raw data of time dependent diffusion of 3 µM PrkC proteins analyzed with increasing concentrations of PG fragments from 0 to 1.6 µg/ml. The insets represent the size distribution by size of PrkC, PrkC(R500A) or PrkCc delta PG mean size. For PrkC and PrkC(R500A), the values of 8.23 and 8.6 hydrodynamic diameters respectively suggests elongated monomers and for PrkCc the value of 4.96 hydrodynamic diameter suggests a globular monomer. Broken blue lines indicate the start of the exponential decay without PG fragments. (B) Histogram of PrkC (light grey), PrkCc (medium grey) and PrkC(R500A) (white) Z-average values (mean intensity size) in the presence of increasing concentrations of PG fragments from 0 to 1.6 µg/ml. Z-average gradually increases suggesting an oligomerization effect of PG fragments on PrkC but a lower effect on oligomerization of PrkC(R500A) and infers a non-specific aggregation of PrkCc with PG. Z-average displayed on a logarithmic scale.

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