Figure 3: Disrupting the function of the PHD1 abrogates the catalytic activity of KDM5A.
From: Histone demethylase KDM5A is regulated by its reader domain through a positive-feedback mechanism
(a) Binding of WT KDM5A1–797 and W335A KDM5A1–797 to H3K4me0 tail peptides. (b) Stimulation of H3K4me3 demethylation by WT and W335A KDM5A1–797 with increasing concentration of H3K4me0 effector tail peptides. (c) Demethylation activity of WT KDM5A1–797 and W335A KDM5A1–797 towards H3K4me3 histone tails. Errors (n≥3) represent s.e.m.
