Skip to main content

Table 3 DNA cleavage rates (pM min−1) determined for HpMutS2 and mutants

From: Mutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function

 

No nucleotide

+ ATP

+ ADP

+ ATPγS

Single-stranded DNA

 HpMutS2

24.82 ± 1.15

32.08 ± 5.32

28.11 ± 5.15

28.5 ± 3.68

 HpMutS2-G338R

40.19 ± 8.73

40.45 ± 9.52

38.87 ± 8.79

ND

 HpMutS2-E413A

6.50 ± 0.55

7.23 ± 0.65

6.90 ± 1.4

ND

 HpMutS2ΔSmr-D30A

2.12 ± 1.67

ND

ND

ND

Holliday junction

 HpMutS2

26.49 ± 3.95

37.77 ± 8.59

18.85 ± 1.9

17.44 ± 0.84

 HpMutS2-G338R

41.59 ± 9.53

43.7 ± 11.42

41.6 ± 10.27

ND

 HpMutS2-E413A

4.92 ± 1.25

1.27 ± 1.01

6.77 ± 3.53

ND

 HpMutS2ΔSmr-D30A

3.34 ± 1.67

ND

ND

ND

  1. Reaction rates were estimated by dividing the total product formed by corresponding incubation time obtained from the linear range of enzymatic activity (Figs. 6a-f). The error values represent standard deviation from two or more different time points. ND, not determined