Fig. 1: C9ORF78 stably interacts with BRR2. | Nature Communications

Fig. 1: C9ORF78 stably interacts with BRR2.

From: A multi-factor trafficking site on the spliceosome remodeling enzyme BRR2 recruits C9ORF78 to regulate alternative splicing

Fig. 1

a SDS–PAGE gels showing elution fractions from analytical SEC, monitoring interaction of GST-C9ORF78 with BRR2FL. Elution direction is indicated by an arrow. The same elution fractions from runs under identical conditions are shown. Protein bands are identified on the right. M, molecular mass marker. In the third and fifth panel, upper and lower regions of the same gels were spliced together. Dotted lines, splice positions. Independent experiments were conducted at least twice with similar results. b C9ORF78 interacts with BRR2 in HEK293T cells. Flag-IP with HEK293T nuclear extract followed by Western blot and antibody staining against BRR2 (top) or Flag-tag (middle and bottom). Flag-CLK1 protein was taken as negative control (Flag-control). Protein bands are identified on the right. M, molecular mass marker. Independent experiments were conducted twice with similar results. Source data for a and b are provided as a Source Data file. c CryoEM map of a BRR2HR-PRPF8Jab1-C9ORF78 complex at 2.76 Å resolution, contoured at 6 root-mean-square-deviation (RMSD). Color coding in this and the following figures: BRR2 NC, gray; BRR2 CC), slate blue; PRPF8Jab1, gold; C9ORF78, orange. d CryoEM map of a BRR2HR-FBP21200-376 complex at 3.3 Å resolution, contoured at 6 RMSD. Color coding in this and the following figures: FBP21200-376, yellow.

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