TABLE 1.
Interaction between LexA DNA-binding domain fusions and the carboxyl terminus of Ku70 in the yeast two-hybrid assay
| LexADBD fusiona | β-Galactosidase activity (U/mg of protein)
|
Fold inductionb | |
|---|---|---|---|
| GAL4AD | KuC-GAL4AD | ||
| rho | 10 ± 6 | 17 ± 1 | ∼2 |
| hGCN5.BrD | 9 ± 1 | 489 ± 58 | 54 |
| hGCN5.BrD.HT | 7 ± 4 | 91 ± 21 | 13 |
| hGCN5.BrD.Pro | 6 ± 2 | 19 ± 10 | ∼3 |
| CBP.BrD | 7 ± 1 | 120 ± 21 | 17 |
| TAF250.BrD | 8 ± 4 | 147 ± 38 | 18 |
a
Shown are LexA DNA-binding domain (LexADBD) fusion proteins derived from rho, the hGCN5 BrD, the helix-turn-helix motif from the hBrD (BrD.HT; aa 364 to 421), the proline-rich region from the hBrD (BrD.Pro; aa 339 to 363), the CBP BrD, and the TAF250 BrDs. The LexA fusions were cotransformed into yeast with either the GAL4AD or the carboxyl terminus of Ku70 (aa 279 to 610) fused to the GAL4AD.
b
Ratio of each LexA fusion interaction with GAL4AD-KuC to interaction with the GAL4AD alone.