Table 2.
RNA dissociation rate constants for WT and mutant RIG-I
| Protein | Nucleotide | k1 (× 10−3 s−1) | Amplitude | k2 (× 10−3 s−1) | Amplitude |
|---|---|---|---|---|---|
| WT RIG-I | None | 28 ± 13 | 25% | 4 ± 0.2 | 75% |
| ATPγS | 187 ± 3 | 45% | 26 ± 0.4 | 55% | |
| ADP | 187 ± 3 | 40% | 25 ± 0.3 | 60% | |
| K270A | None | 108 ± 1 | 80% | 5.3 ± 0.1 | 20% |
| ATP | 327 ± 2 | 79% | 25 ± 0.3 | 21% | |
| ATPγS | 390 ± 3 | 75% | 35 ± 0.4 | 25% | |
| K270R | None | 92.9 ± 1 | 53% | 16 ± 0.1 | 47% |
| ATP | 227 ± 2 | 70% | 14 ± 0.1 | 30% | |
| ATPγS | 224 ± 1 | 81% | 16 ± 0.2 | 19% | |
| ΔCARDs | None | 30.5 ± 0.5 | 34% | 2.1 ± 0.02 | 66% |
| ATPγS | 24.0 ± 0.3 | 27% | 2.2 ± 0.01 | 73% | |
| ADP | 35.3 ± 0.5 | 23% | 1.7 ± 0.01 | 77% |
Rate constants for the dissociation of RIG-I proteins measured using stopped-flow fluorescence spectroscopy as described in ‘Materials and methods’. Dissociation was measured from a 5′ppp10L hairpin RNA in all cases. The data were fit to a biphasic exponential decay equation and. Values represent mean ± SD (n = 3).