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Table 1 Summary of FtsZmutations

From: Site-specific mutations of FtsZ - effects on GTPase and in vitro assembly

Mutation EcFtsZ aa no. MjFtsZ Location on FtsZ Comple ment? 42° (2) GTPase %WT Asmb. GTP Mg Asmb. GTP Ca Asmb. GTP, 0.06 Dd Asmb. GTP, 0.6 Dd Asmb. GDP, 0.6 Dd Refs
Wild type    + 100 PF (3) + S (3) T (3) T (3) (4)
Benign mutations
A70T(Z1) A97 Top-G + (c) 14 (a); <10 (d) PF   S T T a/c/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. 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 theinterface in the protofilament; most "Top" amino acids tested alsocontact the GTP, as indicated by Top-G; N43 and D45 probably contactthe gamma phosphate, indicated by -Gγ. Btm = the bottom surface,the other interface in the protofilament. N207, D209 and D212 formthe "synergy" loop and probably contact the GTP of the subunit below;these are indicated Btm-Gsyn. Front = the front surface (correspondingto the outside of the microtubule). Back = the back surface (insideof the microtubule). Right = the right lateral surface. Left = theleft lateral surface. N165 is largely buried, and makes contactwith the GDP (buried-G). 2. Complementation tests in the presentstudy (ref. a) were done with ftsZ84 (Ts) mutant cells.The mutant FtsZ was on the pBS58 plasmid. + indicates that the mutantplasmid supported cell growth and division in liquid culture overnightat 42°C. - indicates that the mutant gave only filamentous cellswith limited growth. Complementations in ref. b were done with both ftsZ84 anda genomic FtsZ null, with identical results. A blank indicates thatthis was not tested; TS = temperature sensitive. 3. Assembly wasin MEMK 6.5, with 1 mg/ml FtsZ and 2 mM GTP or GDP, and monitored byelectron microscopy. A blank in any assembly condition means thiswas not tested, and NONE means no polymers were found by electronmicroscopy. Assembly in GTP (without Ca or DEAE dextran) producedsingle protofilaments (PF) in wild type and most mutants. D86K producedtwined protofilaments (twPF). Assembly in 20 mM Ca produced protofilamentbundles when indicated by a +. Assembly in DEAE dextran normallyproduced 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., [];c, Bi and Lutkenhaus, [,];d, Fig.5B of Dai et al.[]; e, Mukherjeeet al, []; f, Phoenix and Drapeau [] and Powell and Court [];g, RayChaudhuri and Park, []; and de Boeret al., []; h, Trusca et al., []; i, Scheffers et al., [].