Table 2 Summary of the properties of the Kif2C-(sN+M) mutants studied

From: Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin

Kif2C protein

Microtubule-stimulated ATPasea

Microtubule depolymerase activityb

 

k cat (s−1)

K mMT (μM)

 

Kif2C-(sN + M)

3.5 ± 0.1

1.1 ± 0.1

100%

Kif2C-(nsN + M)

2.9 ± 0.1

2.8 ± 0.3

11 ± 4%(6)

Kif2C-(sN + M-Δα)

3.1 ± 0.1

1.0 ± 0.1

17 ± 3% (3)

A233P

n.d.

n.d.

53 ± 5% (2)

R240P

3.6 ± 0.2

1.9 ± 0.4

46 ± 10% (7)

A233P-R240P

2.9 ± 0.2

1.2 ± 0.3

25 ± 7% (2)

M235Q-I236E

2.5 ± 0.2

8.0 ± 1.6

6 ± 2% (3)

L304R

1.6 ± 0.1

2.2 ± 0.4

12 ± 6% (6)

R420S

0.33 ± 0.03

3.3 ± 0.8

5.7 ± 2% (5)

G499A

5.8 ± 0.5

6.0 ± 1.2

90 ± 8% (3)

G499del

1.4 ± 0.1

0.8 ± 0.1

8 ± 8% (4)

A500del

0.97 ± 0.1

0.4 ± 0.1

10 ± 5% (5)

SS-to-G

1.9 ± 0.5

1.1 ± 0.4

26 ± 6% (2)

D506A

1.8 ± 0.2

1.0 ± 0.3

50 ± 10% (4)

R510A

1.5 ± 0.3

17 ± 6

38 ± 12% (5)

R540A

n.d.c

n.d.c

5.5 ± 3.5% (6)

  1. n.d.: not determined
  2. aKinetic parameters are given as value ± s.e. (calculated from the fit)
  3. bbased on the turbidity signal variation during the first 50 s of the kinetics and compared to wild-type Kif2C (mean ± s.d. evaluated from n = 2–7 replicates, as indicated). Examples of turbidity traces are provided for all mutants in Figs. 3c, 4a,b, 5c,d,f, and in Supplementary Figs. 5, 7 and 8
  4. cfor this mutant, because of a very weak enhancement of the ATPase rate by microtubules, accurate values could not be determined
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