Fig. 4: Kinetics of EspPΔ5’ assembly into native OMs purified from MC4100 and mutant strains. | Nature Communications

Fig. 4: Kinetics of EspPΔ5’ assembly into native OMs purified from MC4100 and mutant strains.

From: Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes

Fig. 4: Kinetics of EspPΔ5’ assembly into native OMs purified from MC4100 and mutant strains.The alt text for this image may have been generated using AI.

A The assembly of de novo synthesized EspPΔ5’ in the presence of 8 µM SurA and either the absence (left) or presence (right) of OMs purified from MC4100 after BAM expression was induced (containing 1 µM BAM) was monitored over a 30 min time course using the experimental scheme illustrated in Fig. 2b. A representative experiment is shown. B The experiment shown in a was repeated except the native OMs were derived from the indicated strain. A representative experiment is shown. The experiments shown in (A, left) was repeated three times and (A, right) and (B) were repeated four times with similar results. C The percent of EspPΔ5’ that was folded in the presence of SurA and OMs purified from the indicated strain over a 30 min time course is shown. The average values of four independent experiments are indicated in the plot. The error bars represent the standard error. The rate constant (k) and the t1/2 were calculated from a single-exponential fit, and the values for each strain were compared to those of MC4100 via one-way ANOVA followed by a Dunnett test. p < 0.05 was considered statistically significant.

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