Fig. 2: Salt-mediated reentrant phase separation of FUS, FUS G156E, TDP-43, Brd4, Sox2, and A11. | Nature Communications

Fig. 2: Salt-mediated reentrant phase separation of FUS, FUS G156E, TDP-43, Brd4, Sox2, and A11.

From: Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions

Fig. 2

Representative images of FUS, FUS G156E, TDP-43 at 50 mM (low salt), 500 mM (intermediate salt), and 2.7 M KCl (high salt) in 50 mM Tris-HCl (pH 7.2); Brd4 and Sox2 at 50 mM (low salt), 500 mM (intermediate salt), and 2.15 M KCl (high salt); Brd4 buffer: 5 mM Tris (pH 7.5), 0.2 mM EDTA, 0.5% glycerol; Sox2 buffer: 5 mM Bis-Tris-Propane (pH 7.5), 0.5% glycerol; and A11 at 22.5 mM (low salt), 225 mM (intermediate salt), and 500 mM NaCl (high salt) in 20 mM HEPES (pH 7.0). For fluorescence imaging, both FUS variants and TDP-43 were tagged with EGFP and studied at a protein concentration of 6 μM; Brd4 and Sox2 were tagged with monoGFP and studied at protein concentrations of 6 µM and 12.4 µM, respectively; A11 was labeled with AlexaFluor647 and studied at a protein concentration of 15 μM. Scale bars are 20 µm in all images. Each data image (center panel) is representative of the observed behavior from at least three test replicates of the respective protein/salt conditions.

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