Table 2.
KH3 generally contributes marginally to hnRNPK binding affinity. Table depicts average dissociation constants with standard errors for full-length hnRNPK and the KH3 and ΔKH3 constructs to several biologically derived RNAs. Fold changes are only listed between ΔKH3 and full-length hnRNPK. The P values from two-tailed t-tests determine binding constant averages that differ from each other as indicated with statistical significance (*P< 0.05; **P< 0.01). Representative binding curves can be found in Supplemental Figures S5, S7A and S9.
| RNA | Full-length hnRNPK KDApp (nM) | ΔKH3 KDApp (nM) | Fold change (ΔKH3 to full-length) | KH3KDApp (nM) |
|---|---|---|---|---|
| B motif RNA | 61 ± 6 | 140 ± 30 | **2.3 | >15000 |
| Sirloin motif | 690 ± 20 | 760 ± 40 | 1.1 | >15000 |
| Ucp2 | 44 ± 3 | 87 ± 9 | *2.0 | 11100 ± 600 |
| Rab7 | 110 ± 20 | 360 ± 80 | **3.2 | >15000 |
| CDK6 3′UTR | 450 ± 60 | 710 ± 50 | *1.6 | 12900 ± 700 |
| MYU lncRNA | 70 ± 7 | 120 ± 10 | *1.7 | >15000 |
| Env8 | 1000 ± 200 | 2300 ± 400 | **2.3 | >15000 |