Fig. 5: Selectivity in IDR interactions with condensates formed by prion-like domains. | Nature Communications

Fig. 5: Selectivity in IDR interactions with condensates formed by prion-like domains.

From: Heterotypic interactions can drive selective co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex

Fig. 5

a The PONDR (Predictor of Natural Disordered Regions) score showing regions of disorder (>0.5) for the FOXG1 protein. The region shaded in red shows the N-terminus IDR for FOXG1 used in the study. b Amino acid composition of FOXG1N-IDR. The color codes for amino acids are provided in Table S6. c Partitioning of AlexaFluor488 labeled FOXG1N-IDR within condensates of FUSPLD (250 µM) and SS18PLD (50 µM), respectively. d Enrichment is calculated as partition coefficient and displayed as a box-and-whisker plot for both FOXG1N-IDR and BRG1PLD (data reported in Fig. 3b, c) within these condensates (FUSPLD condensates: FOXG1N-IDR n = 37, BRG1PLD n = 153 condensates; SS18PLD condensates; FOXG1N-IDR n = 99, BRG1PLD n = 326 condensates). e HEK293T cells co-expressing SS18PLD and mCherry-tagged FOXG1N-IDR or GFP-tagged FOXG1N-IDR and OptoFUSPLD constructs. The degree of colocalization is displayed as intensity profiles for condensates shown in the inset images. Green represents the intensity profile of GFP-tagged protein and red represents the intensity profile for mCherry-tagged protein.

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