Fig. 1: CsgF undergoes phase separation.
From: Cell surface-localized CsgF condensate is a gatekeeper in bacterial curli subunit secretion
a Schematic representation and amino acid sequence of mature CsgF (CsgF without signal peptide). The N-terminal region (amino acids 20–54) is colored in blue, the middle domain (amino acids 55–127) is shown in gray, and the C-terminal region (amino acids 128–138) is indicated in pink. Phenylalanine residues in the N-terminus are indicated in black. b An overlay of 16 conformations of WT-CsgF NMR structure (PDB ID: 5M1U) generated using PyMOL. c Prion-like amino acid (PLAAC) analysis on WT-CsgF. d Concentration-dependent density change of WT-CsgF in 25 mM potassium phosphate pH 7.5 buffer. e Concentration-dependent turbidity change of WT-CsgF, 25 mM potassium phosphate pH 7.5 measured at 350 nm. The data represent mean ± SD, n = 4. f Fluorescence images of WT-CsgF at 1 µM, 5 µM, and 20 µM in 25 mM potassium phosphate pH 7.5. The unlabeled to labeled WT-CsgF ratio was 50:1. The imaging was carried out three times with similar observations. g Time-dependent FRAP measurements on WT-CsgF and quantification of FRAP recovery as a function of time. The scale bar is 1 µm. The data represent mean ± SD, n = 3.
