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

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

Location of the mutation		Viability^b, %	GTPase activity^c, %	Polymer morphology^d	Ref.
Lateral side^a	aa, nº	Viability^b, %	GTPase activity^c, %	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]

^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.
aa, nº = amino acid number.
^bThe % viability was determined from data of Figure 2. N = no growth of ftsZ84 at the restrictive temperature.
^cGTPase activity was measured with 12 μM of protein in all cases.
^dB, bundles; S, short filaments; Nd, not determined. The shape of the polymers was determined by electron microscopy (Figure 5).

ISSN: 1471-2180