Fig. 3: Dbr1 interacts with spliceosomal proteins and other splicing factors.
From: The debranching enzyme Dbr1 regulates lariat turnover and intron splicing
A Dbr1-FLAG and binding partners were isolated through co-immunoprecipitation with anti-FLAG magnetic beads. The eluate shows a clear band for Dbr1 on a Coomassie-stained gel (n = 3 independent replicates for both non-transfected control cells and Dbr1-FLAG transfected cells). B Significant interactions between Dbr1 and spliceosome factors Prp8, Prp19, and Cwc2 (red) were detected, and these factors are adjacent to the lariat (green) in cryo-EM structures of the C and intron lariat spliceosome (ILS) complexes. After transition to the ILS complex, the lariat becomes accessible to Dbr1. C The count of human introns with an eCLIP binding site from ENCODE for Dbr1 co-IP partners that are RNA-binding proteins. D Immunofluorescence using anti-AQR and anti-HA antibodies in U2OS cells shows Dbr1 and AQR co-localize to nuclear speckles (n = 3 independent replicates for each treatment). Source data are provided as a Source Data file.
