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. 2018 Apr 10;114(7):1636–1645. doi: 10.1016/j.bpj.2018.02.020

Figure 3.

Figure 3

Coacervates and poly-L-lysine enhance actin assembly via different mechanisms. (A) Cartoon depicts the time course for spontaneous actin assembly monitored by changes in pyrene-actin fluorescence. (B) Spontaneous assembly is shown of 1.5 μM Mg-ATP-actin (12% pyrene-labeled) alone (black), with 3 μM pLK (cyan), or with 3 μM pLK and 3 μM pRE (red). (C) The assembly rate (1/t1/2) is shown for 1.5 μM actin samples with pLK alone (cyan) or equal concentrations of pLK and pRE (red) as a function of the concentration of pLK. Dashed lines denote the assembly rate of 1.5 μM actin alone measured in parallel with pLK-containing (cyan dashed) or pLK- and pRE-containing (red dashed) samples. (D) Timecourse of pyrene excimer fluorescence during spontaneous assembly is given of 1.5 μM Mg-ATP-actin (12% pyrene-labeled) alone (black), with 3 μM pLK alone (cyan), or with 3 μM pLK and 3 μM pRE together (red). In all experiments with polypeptides, Mg-ATP-actin is incubated with variable pLK in low salt before addition of pRE (red) or a buffer blank (cyan) in 50 mM KCl, 1 mM MgCl2, 1 mM EGTA, 10 mM imidazole (pH 7.0), and 72–150 μM ATP (all concentrations final). To see this figure in color, go online.