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

Table 2 DNA binding affinities (nM) determined for HpMutS2 and mutants

	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

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

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