Fig. 4: Phase separation and disruptor-mediated dissolution behavior of the PR25 peptide at high- and low-salt concentrations. | Nature Communications

Fig. 4: Phase separation and disruptor-mediated dissolution behavior of the PR25 peptide at high- and low-salt concentrations.

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

Fig. 4

a Representative images of PR25 at 50 mM (low salt) and 2.7 M KCl (high salt) in 50 mM Tris-HCl (pH 7.2). The unlabeled peptide was mixed with a small amount of the same peptide labeled with AlexaFluor546; total peptide concentration was 72 μM. b Dissolution assay of PR25 condensates in the high-salt regime using hydrophobic (1,6-hexanediol) and electrostatic/polar disruptors (ATP and PolyU RNA). Final peptide concentration was 54 μM PR25 and final additive concentrations were 10% 1,6-hexanediol, 1.25 mg/mL PolyU RNA, 12.5 mM ATP in 2.7 M KCl, 50 mM Tris-HCl (pH 7.2). Conditions at which the disruptors dissolved the condensates are highlighted in green and those where condensates remained intact are highlighted in red. Only 1,6-hexanediol dissolves PR25 condensates at high salt. Scale bars in all images are 20 μm. In both panels, the images are representative of the observed reproducible behavior from at least three test replicates of the respective protein/salt conditions.

Back to article page