Fig. 6: ILE significantly impedes the proteolytic function of both the ClpC1P1P2 proteases and the ClpXP1P2 proteases. | Communications Biology

Fig. 6: ILE significantly impedes the proteolytic function of both the ClpC1P1P2 proteases and the ClpXP1P2 proteases.

From: Mutations in ClpC1 or ClpX subunit of caseinolytic protease confer resistance to ilamycins in mycobacteria

Fig. 6

Degradation of FITC-casein by a ClpC1wtP1P2, b ClpC1F80IP1P2, c ClpC1F80LP1P2, d ClpC1F80VP1P2, and e ClpC1F80CP1P2 proteases in the presence or absence of ILE. Data are presented as mean ± SD from three technical replicates (n = 3). f Degradation of GFP-DAS+4 by ClpXwtP1P2 proteases in the presence or absence of ILE. Panel (f) shows data from a representative experiment without error bars. Numbers following the drug names indicate the working concentrations (µg mL−1). DMSO was added as control. The D-value of fluorescence intensity represents the change in fluorescence intensity by subtracting the initial fluorescence intensity from the fluorescence intensity of subsequent detections. Statistical significance was determined using one-way ANOVA. *P < 0.05; ***P < 0.0001; ****P < 0.00001; ns no significant difference, where P ≥ 0.05.

Back to article page