Table 3.
Bacterial two-hybrid analysis of C-terminal DivIVA truncation mutants regarding their ability to interact with full-length DivIVA, MinJ, and RacA
| DivIVA | C-terminal protein sequencea | Reactivityb |
||
|---|---|---|---|---|
| DivIVA | MinJ | RacA | ||
| wt | LKKQSKVFRTRFQMLIEAQLDLLKNDDWDHLLEYEVDAVFEEKE-164 | + | + | ± |
| Δ11 | LKKQSKVFRTRFQMLIEAQLDLLKNDDWDHLLE-153 | + | + | − |
| Δ20 | LKKQSKVFRTRFQMLIEAQLDLLK-144 | + | + | − |
| Δ21 | LKKQSKVFRTRFQMLIEAQLDLL-143 | + | + | − |
| Δ26 | LKKQSKVFRTRFQMLIEA-138 | ± | ± | − |
| Δ34 | LKKQSKVFRT-130 | ± | ± | − |
a
Starting from position 121. The shadowed sequence stretch corresponds to the DivIVA tetramerization domain. The position of the last amino acid in the truncated DivIVA proteins is given at the end of the sequence.
b
Symbols coincide with the colors in Fig. S1 in the supplemental material: +, dark blue; ±, light blue; −, white.