Table 2. Characterization of DamX SPOR domain mutants (fused to GFP).
Map of GFP-DamX constructsa | ΔdamX backgroundb | ΔdamXdedD backgrounde | |||
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Septal Localization (%)c | DC resistanced | Rescue divisionf | Inhibit divisionf | ||
GFP-DamX(WT) | 71 ±4 | +++ | +++ | +++ | |
GFP | 0 | - | - | - | |
GFP-DamX(Q351K) | 8±1 | - | - | - | |
GFP-DamX(S354K) | 26 ±6 | +/- | - | - | |
GFP-DamX(W416L) | 40 ±7 | + | - | - | |
GFP-DamX(A350-428) | 2±1 | - | - | - | |
GFP-DamX(A346-428) | 2±1 | - | - | - |
For clarity, domains not drawn to scale. Cyto, cytoplasmic domain; TM, transmembrane helix; Linker, putative unstructured linker region; SPOR, SPOR domain.
The following derivatives of EC1910 were used: EC2882, EC2884, EC2886, EC2888, EC2965, EC2966, and EC2967.
The percentage of cells in the population judged to have a fluorescent band at the division site. Values are the average ± S.D. of 2-6 separate assays, with at least 100 cells scored each time.
Growth in the presence of 0.1 % deoxycholate. See supplemental figure S7 for the original data.
The following derivatives of EC1926 were used: EC2312, EC2313, EC2314, EC2315, EC2316, EC2785, and EC2786.
Cell length during growth in the presence of various concentrations of IPTG. See supplemental figure S8 for the data.