Figure 1
From: Molecular principles of recruitment and dynamics of guest proteins in liquid droplets
At least four sets of droplet-forming disordered p53 domains are required for recruitment into liquid p53 tetramer droplets. (A) Schematic diagram of fluorescent microscopic measurements with highly inclined and laminated optical sheet (HILO) illumination for labeled guest proteins in non-labeled host protein droplets. (B) p53 mutants used in the study. NT, core, Tet, and CT represent the N-terminal, core, tetramerization, and C-terminal domains of p53, respectively. D and M represent dimer and monomer mutations in Tet domain, respectively. Green and yellow boxes represent folded regions, whereas the other colors (purple, black, and pink) represent disordered regions. (C) Fluorescent images of Alexa488-labeled p53 mutants with different oligomeric states in non-labeled p53 tetramer droplet solution. Scale bar denotes 20 μm. (D) Enrichment index (EI) of the guest p53 mutants into non-labeled p53 tetramer droplet. Dots represent the average EIs of each droplet. The errors denote the standard errors. Al488 denotes Alexa488. # of droplet-forming domains denotes the number of NT plus CT. Significant differences in average EI values between p53-Alexa488 and four p53 mutants were confirmed using Welch’s t test with α = 0.05. Significant differences were also confirmed in average EI values between Alexa488 and five p53 samples.
