Fig. 3: Loss of BCL7A/B does not affect BRM-SWI/SNF complexes stability and genomic targeting.

a Immunoblot analysis showing the relative protein levels of BRM-GFP in WT and bcl7a bcl7b background. The numbers at the bottom represent amounts normalized to the loading control, histone H3. WT is used as a GFP-free control. b Mass spectrometry analysis showing numbers of peptides corresponding to SWI/SNF complex subunits recovered by immunoprecipitation of BRM-GFP in the WT and bcl7a bcl7b background. Error bars are presented as mean ± s.d. from two biological replicates. c Immunoblot showing the levels of SWI3C-3×FLAG and BRM-GFP from co-IP experiments with anti-FLAG antibody in the genetic backgrounds indicated above lanes. For each plot, the antibody used is indicated on the left, and the sizes of the protein markers are indicated on the right. Data in (a, c) represent at least 3 biological experiments. d Fold change (log₂) in BRM occupancy between WT and bcl7a bcl7b background. Differentially occupied sites with a false discovery rate (FDR) < 0.05 are highlighted in purple (decreased sites) and green (increased sites). Two biological replicates were performed. Metagene plot (e), heatmap (f) and box plots (g) representation of the mean density BRM occupancy at all BRM binding sites in the WT and bcl7a bcl7b background. n = 7465. In box plots, center line and bounds of box represent median value and the interquartile range (IQR), respectively. Whiskers extend within 1.5 times the IQR. P values were calculated with the two-tailed Student’s t test. h IGV screenshots showing BRM occupancy on selected loci in the WT and bcl7a bcl7b background. i Validation of ChIP-seq signals by ChIP-qPCR. TA3 serves as a negative control. Error bars are presented as mean ± s.d. from three biological replicates. P values were calculated with the two-tailed Student’s t test. Source data are provided as a Source Data file.