Fig. 4: The presence of the SurA core and P2 domains are required for maximal rate enhancement of tOmpA folding on BAM. | Communications Biology

Fig. 4: The presence of the SurA core and P2 domains are required for maximal rate enhancement of tOmpA folding on BAM.

From: Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding

Fig. 4

a Fraction folded of tOmpA in the presence or absence of BAM and SurA variants at different time points as measured by cold SDS–PAGE. Points are the mean of two independent replicates and error bars represent the range of values covered by the replicates. For BAM-containing samples fits to a single exponential equation are shown. In the absence of BAM no folding is observed. b Observed rate constants (kobs) from kinetic experiments in (a). Error bars represent the error on the fit to a single exponential. Example SDS–PAGE gels of the folding reactions are shown in Fig. S11. Samples contained 1 μM BAM (where included) in proteoliposomes containing E. coli polar lipid extract (see the “Methods” section), 2 μM tOmpA, 10 μM SurA variant (where included) in 20 mM Tris–HCl, 150 mM NaCl, pH 8.0, at 25 °C. Source data are provided as a Source Data file (Supplementary Data 10).

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