Table 1.
Summary of FtsZ mutations
| Mutation | aa no. | Location | Comple | GTPase | Asmb. | Asmb. | Asmb. | Asmb. | Asmb. | |||
| aa.no. | MjFtsZ | on FtsZ | ment? | %WT | GTP | GTP | GTP, | GTP, | GDP, | Ref | ||
| EcFtsZ | (1) | 42° (2) | Mg | Ca | 0.06 Dd | 0.6 Dd | 0.6 Dd | s | ||||
| Wild type | + | 100 | PF (3) | + | S (3) | T (3) | T (3) | (4) | ||||
| Benign mutations | ||||||||||||
| A70T(Z1) | A97 | Top-G | + (c) | 14 (a); | PF | S | T | T | a/c/ | |||
| <10 (d) | d | |||||||||||
| A81V/F268C | A108 | Top | + | 15 (d) | ||||||||
| (Z100) | (Buried) | |||||||||||
| D158A | D185 | Front | + | 120 | PF | S(-) | T(-) | T(-) | a | |||
| D158A | + | 155 (b) | b | |||||||||
| D158N | + | b | ||||||||||
| D187A | D212 | Back-G | + | PF | S | T | T | a | ||||
| F268C(Z114) | E293 | BtmRtBk | + (c) | 70 (d) | c/d | |||||||
| D269A | D294 | BtmRtBk | + | 10 | PF | S | T | T | a | |||
| D299A | D324 | Back | +/? | 200 | PF | S | T | T | a | |||
| GTP contact mutations | ||||||||||||
| N43D | N70 | Buried-Gγ | - | 31 (b) | b | |||||||
| D45A | D72 | Top-Gγ | - | 5 | NONE | + | T | T | T | a | ||
| D45N | - | 5 (b) | b | |||||||||
| G105S(Z84) | G132 | Top-G | +TS(f) | ~ 10 (g) | S | S | T | f/g/ | ||||
| a | ||||||||||||
| T108A(Z3) | T135 | Buried-G | - | ~ 0 (c) | NONE | c/e | ||||||
| N165D/Y | E192 | Buried-G | - | 17 (b) | b | |||||||
| N207D | N233 | Btm-Gsyn | - | 5 (b) | b | |||||||
| D209A | D235 | Btm-Gsyn | - | 7 | PF | + | T | T | T | a | ||
| D209N | - | b | ||||||||||
| D212G(Z2) | D238 | Btm-Gsyn | +TS2(c) | 0.5 (h) | T | c/e/h | ||||||
| D212A | - | 7 | NONE | + | S+T | T | T | a | ||||
| D212N | 35 | S (i) | i | |||||||||
| D212C | 17 | S (i) | i | |||||||||
| D212E | 17 | i | ||||||||||
| Lateral mutations | ||||||||||||
| D86K | E113 | Left | - | 49 | twPF+T | + | S+T | S+T | T | a | ||
| D96A | D123 | Left | - | PF | + | S | NONE | a | ||||
| D166K/F268V | E193/E293 | Right | - | 15 | PF | + | S (-) | S (-) | NONE | a | ||
| E238A | E264 | Right | - | 145 | PF | + | S | T | T | a | ||
| S245F | N271 | Right | - | 75 | PF+T | + | S | T | T | a | ||
| E250A | D276 | Right | - | 67 | PF | + | S (-) | S (-) | T (-) | a | ||
| E250K/D253K | D276/D278 | Right | - | 23 | PF | + | S (-) | S (-) | NONE | a | ||
1. Mutated amino acids are all surface residues, and their locations on the atomic structure are shown in Fig. 1. Top = the top surface, forming the interface in the protofilament; most "Top" amino acids tested also contact the GTP, as indicated by Top-G; N43 and D45 probably contact the gamma phosphate, indicated by -Gγ. Btm = the bottom surface, the other interface in the protofilament. N207, D209 and D212 form the "synergy" loop and probably contact the GTP of the subunit below; these are indicated Btm-Gsyn. Front = the front surface (corresponding to the outside of the microtubule). Back = the back surface (inside of the microtubule). Right = the right lateral surface. Left = the left lateral surface. N165 is largely buried, and makes contact with the GDP (buried-G). 2. Complementation tests in the present study (ref. a) were done with ftsZ84 (Ts) mutant cells. The mutant FtsZ was on the pBS58 plasmid. + indicates that the mutant plasmid supported cell growth and division in liquid culture overnight at 42°C. - indicates that the mutant gave only filamentous cells with limited growth. Complementations in ref. b were done with both ftsZ84 and a genomic FtsZ null, with identical results. A blank indicates that this was not tested; TS = temperature sensitive. 3. Assembly was in MEMK 6.5, with 1 mg/ml FtsZ and 2 mM GTP or GDP, and monitored by electron microscopy. A blank in any assembly condition means this was not tested, and NONE means no polymers were found by electron microscopy. Assembly in GTP (without Ca or DEAE dextran) produced single protofilaments (PF) in wild type and most mutants. D86K produced twined protofilaments (twPF). Assembly in 20 mM Ca produced protofilament bundles when indicated by a +. Assembly in DEAE dextran normally produced sheets of protofilaments (S) at 0.06 mg/ml, and tubes (T, protofilaments in the curved conformation) at 0.6 mg/ml. 4. References: a, the present work; b, Table 2 of Wang et al., [13]; c, Bi and Lutkenhaus, [24, 38]; d, Fig.5B of Dai et al.[25]; e, Mukherjee et al, [1]; f, Phoenix and Drapeau [20] and Powell and Court [21]; g, RayChaudhuri and Park, [19]; and de Boer et al., [17]; h, Trusca et al., [23]; i, Scheffers et al., [39].