Skip to main content
. 2023 May 30;42(14):e113168. doi: 10.15252/embj.2022113168

Figure 5. HNRNPH1 interacts with G‐rich sequences in RBM3 poison exon in a temperature‐dependent manner. See also Fig EV5 .

Figure 5

  1. Western blot and quantification of HNRNPH1 normalised to GAPDH in WT i‐neurons at 37 and 32°C (72 h). RBM3 blots of the same samples are shown for comparison.
  2. Schematic of HNRNPH1 RNA Immunoprecipitation (RIP) in HeLa cells at 37 or 32°C. The graph on the right shows the fold change in HNRNPH1‐pulled down RBM3 mRNA after normalisation.
  3. Analysis of public HNRNPH1 iCLIP dataset in two replicates, mapped to RBM3 Exon 3–4. Crosslink counts are normalised to library size. RNA G quadruplexes (rG4) are predicted using QGRS mapper. The position of the GGGG motif deleted in the mutant RBM3 minigene is shown in pink.
  4. RT‐PCR of WT and delGGGG RBM3 minigenes in HeLa cells at 37 or 32°C (48 h) treated with SMG1 inhibitor. PSI values of RBM3 PE are shown in the graphs on the right.

Data information: N = 3 biological replicates. Mean ± SEM; n.s. (not significant), *(P < 0.05), **(P < 0.01); unpaired t‐tests in (A), (B), (F), paired t‐tests in (D).

Source data are available online for this figure.