Fig. 1: Identification of an acidic activation domain in NUT.
From: Structural insights into p300 regulation and acetylation-dependent genome organisation
a Domain structure of p300 and b BRD4-NUT constructs. c IUPred, prediction of intrinsic disorder; FOLD, folding prediction using the foldindex (blue), PLAAC (Prion-Like Amino Acid Composition; orange) and PAPA (Prion Aggregation Prediction Algorithm; grey) analysis, NCPR (Net Charge Per Residue) with a sliding window of ten residues of the BRD4-NUT protein. d SEC-MALLS analysis of the TAZ2 domain of p300 alone (black), NUT4 alone (blue) and the complex between TAZ2 and NUT4 (red). SDS-PAGE analysis of the peak fractions of the TAZ2-NUT4 complex is shown. The experiment was repeated twice with consistency. e Competition analysis: Cos7 cells were transfected with constructs expressing GFP-BRD4-NUT (green) alone or co-transfected with RFP-NUT-F1c and RFP-NUT4 (red). Immunofluorescence with anti-p300 antibody was used to visualize endogenous p300. Scale bars, 10 μm. The experiment was repeated three times with consistency.
