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. 2006 Aug 21;26(21):7871–7879. doi: 10.1128/MCB.00573-06

FIG. 6.

FIG. 6.

The toxicity of YNG1 overexpression correlates with the level of Yng1p-triMeH3K4 binding. (A) Schematic representation of Yng1p (open bar), the Yng1 PHD finger (black bar), the coordinating cysteines and histidine residues of the PHD finger (underlined), and the residues subjected to mutation (highlighted). (B) Histone peptide binding assays were performed with the indicated biotinylated peptides and purified wild-type and mutant versions of GST-Yng1PHD. Shown are Western blots of peptide-bound GST-Yng1PHD proteins with GST antibodies. Input lanes represent 10% of the GST protein used in the pull-down assays. (C) Tenfold serial dilutions of yeast strain YLH101 containing the indicated plasmids were plated on synthetic complete medium lacking uracil containing either dextrose or galactose as a carbon source and incubated at 30°C for 3 days. (D) Normalized amounts of whole-cell extract from a wild-type yeast strain (YLH101) carrying plasmids expressing the indicated HA-tagged versions of Yng1p from a GAL1 promoter and grown on galactose were subjected to Western blotting for HA.