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Correction to: Mutations in the nucleotide binding and hydrolysis domains of helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function
BMC Microbiology volume 19, Article number: 190 (2019)
Correction to: BMC Microbiol
Following publication of the original article , the authors notified us of an error in the presentation of Fig. 6G.
In the published version panels 5 and 6 of the Fig. 6G are similar, but the nuclease assays contained two different nucleotide cofactors. During assembly and handling of the images for this figure, the same image, albeit with different contrast, was used unintentionally for panels 5 and 6. This image corresponded to panel 6.
The assay addressed the effect of ADP (Fig. 6G, panel 5) and ATPγS (Fig. 6G, panel 6) on the nuclease activity of HpMutS2 on Holliday junction substrate. In absence of cofactors (Fig. 6D, and 6G panel 1), HpMutS2 degrades Holliday junction at 26.49 ± 3.95 pM min-1 (Table 3). The addition of ADP and ATPγS reduced the nuclease activity of HpMutS2 by ~ 1.5-fold, resulting in the cleavage rates of 18.85 ± 1.9 pM min-1 and 17.44 ± 0.84 pM min-1, respectively.
The quantification of the assays shown in Fig. 6D were derived from the correct gel images and therefore Fig. 6D and DNA cleavage rates presented in Table 3 remains unchanged.
Corrected Figure ^6 is presented below:
Damke et al. (2016) Mutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function (2016) 16:14 DOI: https://doi.org/10.1186/s12866-016-0629-3.
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Damke, P.P., Dhanaraju, R., Marsin, S. et al. Correction to: Mutations in the nucleotide binding and hydrolysis domains of helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function. BMC Microbiol 19, 190 (2019). https://doi.org/10.1186/s12866-019-1567-7