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. Author manuscript; available in PMC: 2010 Jul 21.
Published in final edited form as: Biochemistry. 2009 Jul 21;48(28):6664–6673. doi: 10.1021/bi8022653

Table 2.

GTPase Activity and Assembly Dynamics of Fluorophore-Labeled FtsZ in Seven Different Buffersa

lifetime of disassembly, τ (s)
GTPase activity (GTP min−1 FtsZ−1) 1/GTPase (s)b lifetime of subunit exchange, τ (s) GDPc dilutionc
HMK100 4.5 13.3 5.0 ± 0.5 3.6 ± 0.4 2.0 ± 0.3
HMK350 1.3 46.2 25.1 ±3 [5 and 33(1:4)]d 18.9 ± 2.1 16.3 ± 2.0
HMK500 0.6 100 32.3 ± 3 30.9 ± 4.1 27.2 ± 2.9
HMRb100 1.8 33.3 14.1 ± 2 5.0 ± 0.4 3.6 ± 0.4
HMRb500 0.6 100 54.9 ± 5 19.4 ± 2.5 17.5± 2.2
HMK100/10Mg 2.1 28.6 15.8 ± 2 [5 and 23(1:1.3)]d 8.9 ± 1.5 8.0 ± 1.4
HMK100/20Mg 0.9 66.7 20.1 ± 2 [5 and 24 (1:5)]d 20.0 ± 3.5 18.6 ± 2.5
a

All measurements were taken at 25–26 °C. τ can be converted to half-time by the formula t1/2 = τ ln 2 = 0.69τ.

b

The time of 1/GTPase can be considered the average time for nucleotide hydrolysis by polymerized FtsZ at steady state.

c

FtsZ filament disassembly was induced by addition of GDP to a 20-fold excess or by 15-fold dilution with the same buffer.

d

The data were best fit by a double-exponential decay. The two lifetimes and the ratio of the amplitudes of their contributions to the decay are given in parentheses. The ratio 1:4 means that the slow decay contributed 4 times as much as the fast decay.