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In vitro methyltransferase assay showing a direct role of OXR1 in regulating the enzymatic activity of PRMT5. N-terminal H4 peptides (1-21aa) and the mutant ones H4-R3K (1-21aa) were used as substrates. Different molar ratio of PRMT5/MEP50 protein complex (calculated as tetramer) to the full length OXR1A or truncated ones, such as 4:1 ( +), 1:1(+ +), and 1:4(+ + +), was applied in each reaction. The enzymatic activity of PRMT5 was shown by the CPM (Count per minute) value of 3 H-Methyl incorporation. All Data are shown as mean ± SD, * p < 0.05, *** p < 0.001, Student’s t test
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