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Table 2 DNA binding affinities (nM) 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 21.48 ± 2.28 a 17.27 ± 2.89 11.44 ± 0.19
 HpMutS2-G338R 32.37 ± 3.32 30.70 ± 3.43 23.89 ± 2.91 ND
 HpMutS2-E413A 73.77 ± 75.74 a a ND
Holliday junction
 HpMutS2 14.38 ± 0.82 20.77 ± 2.95 22.63 ± 1.391 22.46 ± 1.23
 HpMutS2-G338R 21.41 ± 0.93 32.04 ± 4.34 34.02 ± 5.31 ND
 HpMutS2-E413A 30.80 ± 1.97 31.72 ± 3.34 46.38 ± 5.60 ND
  1. Dissociation constants were estimated from analysis of Figs. 5b-g. The error values represent standard deviation from at least two different experiments. ND not determined; a, could not be determined