Vorinostat-induced RUNX3 acetylation increases enhancer activity of NK-92 cells. (A) Transcription factor motif identification from ATAC-seq peaks in differential H3K27ac peaks. (B) Expression of RUNX1, RUNX2, and RUNX3 genes determined by RNA-seq. (C) Snapshot of signal tracks for RUNX3 ChIP-seq, H3K27ac ChIP-seq, and ATAC-seq in the representative genomic region. (D) Box plot presenting the distribution of RUNX3 peaks among different gene features. (E) Scatterplot of ChIP-Seq signals called for RUNX3. (F) Heatmaps of ChIP-Seq signals called for RUNX3 (left) and H3K27ac (right). (G) Box plot of H3K27ac enrichment at RUNX3 binding sites (n = 1,807). (H) Scatter plot of relative enrichment in RUNX3 and H3K27ac ChIP-Seq signals at RUNX3 binding sites (n = 1,807). (I) acetylation of RUNX3 by Vorinostat treatment. The cell lysates were analyzed by immunoprecipitation using an antibody against acetylated lysine, followed by Western blotting using an anti-RUNX3 antibody (upper panel). To examine the level of RUNX3 expression, the same lysates were analyzed by Western blotting using anti-RUNX3 and anti-α-Tubulin antibodies (middle and lower panels).
