Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity

The identification of two arginine residues (R206 and R210) within the region of RUNX1 that interact with the corepressor SIN3A and are methylated by PRMT1 is reported. Results provide insight into the arginine methylation sites and the loss of dynamic regulation of corepressor binding in the leukemia-associated RUNX1-ETO fusion protein, which contributes to its dominant inhibitory activity.