Skip to main content
. 2021 Jul 2;12:4090. doi: 10.1038/s41467-021-24373-5

Fig. 5. SS18 interacts with BAF through its N-terminal 70 residues.

Fig. 5

a Representative images for EGFP fusions expressed in mESCs as indicated. Note the similar condensates formed by SS18, FUS and TAF IDRs as compared to those for MED1 and BRD4. Poly Y is an artificial 24 tyrosine residue polypeptide. FL full length. Scale bars, 5 μm. laser intensity 2.5%, detector gain 500 V, background subtraction treatment. Three biological replicates. b Rescue of Ss18KO by constructs in (a) to show that IDRs from TAF and FUS or even polyY can substitute that of SS18. Data are mean ± s.d., two-sided, unpaired t test; n = 3 independent experiments, ***p < 0.001, ****p < 0.0001. c Volcano plots of IP-MS results from flag tagged Ss18-FL, SS18(IDR), N terminal 70aa of Ss18 alone or fused with IDRs from FUS or Brd4 and polyY expressed in Ss18KO mESCs by Flag antibody with label-free quantification. Every point represents a single protein. SS18 and BAF components are marked in blue and red, respectively. IP-MS experiments were performed in triplicates and a two-sample t test was applied. P = 0.01 and fold change = 2 were used as threshold. d Summary table for various constructs for their abilities to condensate, interact with BAF and mediate PST. e A proposed structure and function relationship for SS18: N-terminal BAF interacting domain or BID and C-terminal condensate forming IDR domain (CFD).