Fig. 5: Methylation activity of PRDM9 on H3K4 and H3K36 peptides observed in experiments and MD simulations.
From: Investigation and design of the dual specificity of the PRDM9 protein lysine methyltransferase
a Exemplary autoradiographic image of soluble H3K4 (1−19) and H3K36 (26–44) peptides methylated by PRDM9 (195–415) and separated by Tricine-SDS-PAGE. b Kinetics of H3K4 and H3K36 methylation by PRDM9 (195–415). Data were fitted to an exponential reaction progress curve yielding a ratio of 5.2 for the initial methylation rates of H3K4/H3K36. Data points show results of three independent experiments with each substrate, lines show the combined fit of the data. Exemplary gel images are shown in Supplementary Fig. 4a. c Representation of the characteristic distances and angles between the Nε-atom of the target lysine, the C-atom of the AdoMet methyl group, and the S-atom of AdoMet for a PKMT TS-like conformation. d Distribution of the number of TS-like conformations observed in each of the 21 individual MD simulations with the H3K4 and H3K36 substrates. The p-value was determined by Fisher’s exact test.
