TABLE 2.
Deletion of the multimerization domain(s) of Rev in the nine-arginine-substituted Rev–MS-C proteins has differential effects on RRE and MS2 targets
| Rev and Rev–MS-C protein | Oligomers in EMSAa
|
Subcellular locationb |
trans-Activationc (SD)
|
||
|---|---|---|---|---|---|
| RRE | MS2 | RRE | RREZ-MS2 | ||
| Rev | Yes | Yes | Nuc>>>Cyt | 100 | 1.3 (0.7) |
| Rev–MS-C | Yes | Yes | Nuc>>>Cyt | 148 (9.7) | 114 (14.8) |
| Δ35/50Rev-i-9R/MS-C | Yes | Yes | Nuc>>>Cyt | 97 (14.5) | 122 (16.7) |
| Δ35/60Rev-i-9R/MS-C | +/− | +/− | Nuc>>>Cyt | 3.7 (14.5) | 83 (17.1) |
| Δ24/50Rev-i-9R/MS-C | No | No | Nuc>>>Cyt | 3.3 (1.9) | 111 (18.3) |
| Δ24/60Rev-i-9R/MS-C | No | No | Nuc>>>Cyt | 3.7 (0.8) | 97 (12.1) |
| Δ24/60Rev-i-9R & ter 87/MS-C | ND | ND | Nuc>>>Cyt | 2.4 (1.4) | 3.3 (2.4) |
a
Oligomer formation was evaluated in EMSA using fixed amounts of 32P-labeled PPE or MS2 RNAs. +/−, occasional occurrence of dimer species; ND, not determined.
b
Subcellular localization data are from indirect immunofluorescence microscopy analyses. Nuc, nuclear; Cyt, cytoplasmic.
c
Mean GAG expression values from six experiments, normalized for transfection efficiency, are tabulated with the respective standard deviations. The positive values are denoted by boldface.