TABLE 3.
3′UTR length and SKI7 effects on mRNA translation and stabilitya
| Strain | C+ A− RNAb | Initial rate | Ft1/2 | Maximum activity |
|---|---|---|---|---|
| Wild type | UTR 4b | 0.9 ± 0.1 | 3.7 ± 0.1 | 0.15 ± 0.01 |
| UTR 24b | 2.9 ± 0.1 | 3.2 ± 0.2 | 0.2 ± 0.01 | |
| UTR 64b | 10.3 ± 2.4 | 7.1 ± 0.1 | 1.9 ± 0.6 | |
| UTR 104b | 10.8 ± 0.6 | 8.4 ± 0.4 | 1.7 ± 0.3 | |
| ski7::HIS3 | UTR 4b | 3.9 ± 0.5 | 13.7 ± 0.3 | 1.4 ± 0.1 |
| UTR 24b | 16.3 ± 3.1 | 17.2 ± 2.5 | 4.4 ± 0.1 | |
| UTR 64b | 18.0 ± 3.3 | 31.6 ± 0.3 | 8.6 ± 0.2 | |
| UTR 104b | 21.2 ± 4.8 | 34.4 ± 3.5 | 13.7 ± 0.5 |
a
Wild-type (B959) and isogenic mutant (B117) strains were electroporated with the indicated C+ A− luciferase mRNAs. From the time course of luciferase synthesis, we determined the initial rate of luciferase accumulation (initial rate) (in light units [×100] per minute per microgram of protein) and functional stability (Ft1/2) (in minutes required to reach one-half maximum luciferase activity). Maximum activity is reported in light units per microgram of protein. The control had 0.005 light unit/μg of protein. Errors indicate the variation of results within one experiment with identical preparations of RNA and cells.
b
4b, 24b, etc., indicate the number of bases in the 3′UTR.