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. Author manuscript; available in PMC: 2012 Nov 18.
Published in final edited form as: J Mol Biol. 2011 Oct 1;414(1):106–122. doi: 10.1016/j.jmb.2011.09.040

Figure 5. Methyltransferase activities of different AtPRMT10 constructs in vitro.

Figure 5

(A) Indicated AtPRMT10 proteins (5 μg) were used for in vitro methylation activity assay. The reaction mixture was separated on a 15% SDS-PAGE and the autoradiograph of the gel is recorded. The experiments were performed in triplicate and a typical result is shown here. (B) Quantification of the results from Figure 5A. The relative activities presented here were calculated by considering the activity of wild-type AtPRMT10 over H2A as one. The activities of AtPRMT10 mutants over H2A are significantly higher than that of wild-type enzyme (n=3; error bars represent SEM; Student t test *p < 0.03, **p < 0.002). (C) Methyltransferase activities of different AtPRMT10 constructs on H4, GST-H4 and H4N1-20.