FIGURE 2.

Concentration-dependent DNMT3A activation. A, the activity of DNMT3A shows a sigmoidal relationship with protein concentration. DNMT3A is more active at higher enzyme concentrations suggesting that DNMT3A oligomerization is concentration-dependent. The DNA is below the K_m at 500 nm bp. B, DNMT3A with DNMT3L is more active at higher DNMT3A concentrations (DNMT3L is kept constant at saturating concentrations), suggesting that the concentration-dependent oligomerization takes place at the dimer interface (the interface that does not bind DNMT3L). The DNA is below the K_m at 500 nm bp. C, the activity of DNMT3A shows a linear relationship when DNA is at over above the K_m, data shown are when DNA is at 2 μm bp. Reactions took place on poly-dIdC, a multiple site substrate.