TABLE 1:
Comparison of properties of SpPRF, WT ScPFY, and ScPFY(9-Mut).
| Profilin | Protein stabilitya (D1/2, M urea) | Poly-l-proline bindingb (Kd, μM) | Cdc12(FH1) bindingc (Kd, μM) | Muscle G-actin bindingd (Kd, μM) | Fission yeast G-actin bindinge (actin band intensity at 5 μM profilin, a.u.) | Nucleotide exchangef (time to one-half exchange at 0.5 μM profilin, s) | PtdIns(4,5)P2 bindingg (percentage unbound profilin in flowthrough, 100 μM PtdIns(4,5)P2) |
|---|---|---|---|---|---|---|---|
| SpPRF | 4.5 | 59 | 6.4 | 0.8 | 6.4 | 59.3 ± 6.7 | 34.1 ± 1.6 |
| ScPFY | 3.3 | 224 | 24.7 | 0.7 | 10.1 | 29.0 ± 3.9 | 57.4 ± 2.8 |
| ScPFY (9-Mut) | 2.6 | 195 | 22.7 | 0.4 | 9.4 | 16.3 ± 3.9 | 18.0 ± 2.9 |
aSupplemental Figure S3A.
bSupplemental Figure S4A.
cSupplemental Figure S4B.
dSupplemental Figure S3, B and C.
eSupplemental Figure S3, D and E.
fSupplemental Figure S3, F and G.
gSupplemental Figure S4C.