Journal: International Journal of Molecular Sciences
Article Title: Phospho-Switch: Regulation of the Activity of SAM-Dependent Methyltransferases Using H -Phosphinic SAM Analogue
doi: 10.3390/ijms26178590
Figure Lengend Snippet: Interaction of SAM and SAH phosphorus-containing analogues with Dnmt1 and COMT. ( a ) Inhibition of Dnmt1 methylation activity. Dnmt1 reaction mixtures contained the following: SAM (5 µM), rac-SAH-P 5 (100 µM), rac-SAM-P 5 (100 µM), rac-SAH-P H (100 µM), or (R,S)-SAM-P H (100 µM). SAH (25 µM) was used as a reference inhibitor. The D2 DNA hairpin, the product of the Dnmt1 reaction cleaved with GlaI, was used as the control. ( b ) Inhibition of COMT methylation activity. Reaction mixtures contained either SAM or (R,S)-SAM-P H (each 6 mM) as methyl group donors and SAH (3 mM) or rac-SAH-P H (3 mM) as inhibitors. The duration of the reactions was 2 h and 24 h. In both panels the results indicate means from five independent experiments. Error bars represent standard deviations. ** p ≤ 0.01 according to one-way ANOVA with Dunnett’s post hoc test (vs. “no inhibitor”).
Article Snippet: Human recombinant DNA methyltransferase Dnmt1 was purchased from ThermoFisher (Waltham, MA, USA).
Techniques: Analogues, Inhibition, Methylation, Activity Assay, Control