Table 2.
Interactions of Psp and ArcB proteins in vivo.
| T25 fusions |
||||
|---|---|---|---|---|
| T18 fusions | T25–ArcBWT | T25–ArcB* | T25–ArcBLeuZm | T25–PspC |
| T18C–ArcBWT | +/− | ND | ND | +/− |
| T18C–ArcB* | ND | + | ND | +/− |
| PspB–T18 | ++ | ++ | + | ++ |
| PspBLeuZm–T18 | − | − | − | ++ |
| T18C–PspA | +/− | +/− | +/− | + |
| T18C–PspC | +/− | +/− | +/− | − |
| T18C–ArcBLeuZm | ND | ND | +/− | +/− |
| T18C–PspF | − | − | − | − |
The BACTH system was used to detect the protein–protein interactions between the Psp and ArcB proteins. Negative control: BTH101/pKT25+pUT18C vectors alone (74 ± 4 MU); positive control: BTH101/pKT25-zip+pUT18C-zip (1017 ± 34 MU); interaction estimates including SD were as follows: (+/−) weak interaction (235–350 MU); (+) interaction (350–500 MU); (++) strong interaction (>700 MU); (−) no interaction (≤ 234 MU); ND, not determined. For construction of fusion proteins, growth conditions and mean values with SD, see Experimental procedures.