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. 2022 Jan 5;11:e72867. doi: 10.7554/eLife.72867

Figure 4. PRMT inhibition promotes aberrant binding of RNA processing factors to chromatin-associated poly(A) RNA.

(a) Overview of chromatin-associated poly(A)-RNA LC-MS/MS experiment. (b, c) Dot plot of proteins bound to chromatin (b) or chromatin-associated poly(A) RNA (c) relative to DMSO. Circle size is proportional to −log2(p). Colored values denote factors with ontology pertaining to RNA splicing, transport, or degradation. The names of the top 15 significant proteins are labeled. Significance determined using a heteroscedastic t-test. (d, e) Venn diagram comparing proteins containing methylarginine (Maron et al., 2021) and those that were differentially enriched in the chromatin (d) or chromatin-associated poly(A) (e) fractions following PRMT inhibition. (f) Western blot of chromatin following 2-day treatment with DMSO, GSK591, or MS023. See Figure 4—source data 1. (g) Immunoprecipitation and analysis of CHTOP and SNRPB methylarginine following treatment with DMSO, GSK591, or MS023 for 2 days. See Figure 4—source data 2.

Figure 4—source data 1. Western blot data for Figure 4f.
Figure 4—source data 2. Western blot data for Figure 4g.

Figure 4.

Figure 4—figure supplement 1. PRMT inhibition alters association of RNA splicing, localization, and processing factors to chromatin and chromatin-associated poly(A) RNA.

Figure 4—figure supplement 1.

(a, b) Enriched biological processes found in the proteome of input chromatin (a) and chromatin-associated poly(A) RNA (b) in A549 cells treated with GSK591 or MS023 relative to DMSO.