Structural and Functional Characterization of a Complex between the Acidic Transactivation Domain of EBNA2 and the Tfb1/p62 Subunit of TFIIH
Figure 6
The hydrophobic residues of the ΦXXΦΦ motif from EBNA2 are important for transactivation.
LexA-EBNA2431–487 and mutant (W458T, I461 and F462S) fusion proteins were co-transformed in yeast with the reporter LexA operator-Lac-Z fusion plasmid pSH18–34. Results are presented as the percentage of the β-galactosidase units of the tested fusion proteins relative to that of the LexA-GAL474–881 positive control (100%). Error bars represent standard error about the mean of a minimum of three independent experiments.