Fig. 3
From: Characterization of protein arginine methyltransferase of TgPRMT5 in Toxoplasma gondii
In vitro methylation of histones by purified HA-tagged endogenous TgPRMT5. a The HA-tagged endogenous TgPRMT5 were purified with an anti-HA antibody and checked in SDS/PAGE. b Immunoprecipitations using an anti-HA antibody were performed on parasite lysates made from TgPRMT5-HA and the parental Pru∆ku80 line. The immunoprecipitated products were used in vitro methylation assays with T. gondii recombinant histones H3/H4 (rTgH3 and rTgH4) and calf core histones as substrates or without substrates (blank), and the reactions were separated by SDS/PAGE (15% gel). Immunoblots were performed using rabbit polyclonal antibodies as follows: anti-monomethyl H3R26, anti-symmetric dimethyl H3R26, anti-monomethyl H4R3 and anti-symmetric dimethyl H4R3