Table 1. Properties of TRF2, TRF2ΔB, TRF2ΔM, and TRF1a.
| % of TRF2 | % change from buffer |
|||||
|---|---|---|---|---|---|---|
| protein | TRF-induced telomeric D-loop formation (AUC at 0–250 nM) | Rad51-mediated telomeric D-loop formation (AUC at 500–750 nM) | Rad51-mediated nontelomeric D-loop formation (AUC at 500–750 nM) | telomeric DNA binding, C1/2 (nM) | telomeric binding specificity | migration in agarose gels |
| buffer | N/A | 30.3 ± 0.4 | 4.7 ± 0.4 | N/A | + | – |
| 0 ± 0.7% | 0 ± 7.6% | |||||
| TRF2 | 6.0 ± 0.15 | 13.3 ± 0.8b | 4.7 ± 0.0 | 111 ± 8 | + | – |
| 100 ± 2.4% | –52 ± 5.1%b | +4 ± 2.2% | ||||
| TRF2ΔB | 2.8 | 22.1 ± 0.7b | 5.1 ± 0.7 | 257 | + | – |
| 47% | –31 ± 5.5%b | +5 ± 7.2% | ||||
| TRF2ΔM | 1.8 | 29.0 ± 1.4 | 9.6 ± 0.4b | 319 | – | +/– |
| 31% | +4 ± 4.0% | +112 ± 13.0%b | ||||
| TRF1 | 1.6 | 38.5 ± 1.9b | 5.4 ± 0.9 | 152 | + | + |
| 27% | +25 ± 1.0%b | +9 ± 5.2% | ||||
a
Buffer data are averaged. Proteins are statistically compared against matched buffer controls. TRF-induced D-loop formation calculated as the area under the curve (AUC, % complex × [TRF] in nanomolar) from Figure 1. Rad51-mediated D-loop formation calculated as AUC (% complex × [Rad51] in nanomolar) from Figures 2–5. AUC calculation examples in Figure S5 of the Supporting Information. C1/2 represents the concentration of TRF protein required to supershift 50% of the template in EMSAs. Errors shown are 95% confidence intervals from three independent experiments.
b
Significant difference (p < 0.05) from buffer via a two-tailed paired sample t test.