Figure 2: Tudor interaction with the nucleosome is dependent on methylation at H3K36.
From: Binding of PHF1 Tudor to H3K36me3 enhances nucleosome accessibility
(a) Western analysis of pulldowns of wild-type (wt) GST-Tudor with H3KC36me3-NCP (top) of Y47A GST-Tudor with H3KC36me3-NCP (middle) or wild-type GST-Tudor with the unmodified wild-type NCP (bottom). (b) The representative binding curves shown for each combination of the Tudor domain and NCP. Densitometry analysis of the bound H3KC36me3-NCP reveals an apparent affinity of 1.3±0.5 μM (SD based on three experiments) of wild-type GST-Tudor (squares), and significantly weaker association of the Y47A mutant GST-Tudor with H3KC36me3-NCP (circles) or wild-type Tudor with wild-type nucleosomes (triangles). All experiments were performed in triplicate. (c) Western blot analysis of GST pulldown with H3KC36me3-NCP showing that GST does not bind to H3KC36me3-NCP.
