Table 1.
RecA3 binding to G4 oligonucleotides
| Without Poly[d(I-C)] | With Poly[d(I-C)] | ||||||
|---|---|---|---|---|---|---|---|
| Av | RecA3 KD (nM) | ± SE (nM) | R2 curve | RecA3 KD (nM) | ± SE (nM) | R2 curve | |
| Parental T:TT:T | Av | 14.1 | 0.3 | 0.99 | 22.0 | 1.1 | 0.99 |
| T:TT:AT | Avi | 16.6 | 0.5 | 0.98 | 25.5 | 1 | 0.99 |
| A:AA:A | Avi | 119 | 24 | 0.96 | 84.2 | 15.6 | 0.98 |
| AT:ATT:AT | Avd | 77.5 | 3.9 | 0.99 | 101 | 8 | 0.99 |
| TTT:GC:ATC | Avd | 47.8 | 1.6 | 0.99 | 62.2 | 4.3 | 0.99 |
| G4 Mutant | Avd | 123 | 15 | 0.97 | 140 | 34 | 0.93 |
The pilin Av phenotype is shown for comparison (Figure 2 and Figure 4). At least twenty-four different concentrations of purified RecA3 (a generous gift from Phoebe Rice) were added to 10 nM of each G4 oligo. Binding curves for each G4 structure were determined using Prism’s Specific Binding with Hill Slope by fitting points to the curve (Figure S2 and S3), each point was repeated in triplicate. The KD and standard error of the KD is presented as calculated by the program. The KDs were also calculated in the presence of 100 ug/ml Poly[d(I-C)] to reduce any non-specific binding by RecA3 to each G4 structure. The R2 represents how well the data fit to the standard Hill slope binding curve. KD = disassociation constant SE= standard error.