Fig. 5: TRIP4 and ALKBH3 may conscribe ASCC core subunits for distinct cellular functions.

a SDS-PAGE analyses of analytical SEC elution fractions monitoring the competitive binding of TRIP4 and AlkBH3 to ASCC3^HR. Throughout all panels, equivalent elution fractions are vertically aligned. Input samples are identified on top of each run. Molecular mass markers in kDa are shown on the left; protein bands are identified on the right. Stable complexes eluting from some analytical SEC runs are identified below the respective gels. For some analytical SEC runs, separate regions of the same gel were spliced together for display purposes (see Source Data file for uncropped gels). Dashed lines, splice lines. TRIP4 and AlkBH3 do not stably interact (run 4). AlkBH3 and TRIP4 form stable binary complexes with ASCC3^HR (runs 5 and 6). AlkBH3 is excluded from a pre-formed ASCC3^HR-TRIP4 complex (run 7). Experiments were repeated independently at least three times with similar results. b Western blots documenting CRISPR/Cas9-mediated KO of TRIP4. GAPDH was used as a loading control. c Assay comparing the relative degree of viability of TRIP4 wt and KO PC-3 cells in the presence of increasing concentrations of MMS. TRIP4 wt cells, black; TRIP4 KO cells, red. Values represent means ± SD; n = 5 technical replicates. Error bars are hidden by data points. Source data are provided as a Source Data file.