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Table 1 Summary of FtsZ mutations and their effects on cell viability, GTPase activity and polymer morphology

From: Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coliviability

Location of the mutation Viabilityb, % GTPase activityc, % Polymer morphologyd Ref.
Lateral sidea aa, nº ZipA  
  WT 100 100 B This study
Left E83Q 10 40 B This study
Left R85Q 0.5 5 S This study
Left D86K N 49 Nd [11]
Right E250A N 67 Nd [11]
  1. aThe mutations are positioned on the surface and their location on the structure are shown in Figure 1. Left: the left lateral surface; Right: the right lateral surface.
  2. aa, nº = amino acid number.
  3. bThe % viability was determined from data of Figure 2. N = no growth of ftsZ84 at the restrictive temperature.
  4. cGTPase activity was measured with 12 μM of protein in all cases.
  5. dB, bundles; S, short filaments; Nd, not determined. The shape of the polymers was determined by electron microscopy (Figure 5).