Nucleic Acids Research, 2019: https://doi.org/10.1093/nar/gkz524
The Authors wish to make the following corrections to their article.
In Figure 1, panel B1 (Apo MtsR) was inadvertently repeated in B5 (MtsR:Mn – non-specific probe). A new Figure 1 is provided below. The Figure has also been replaced in the published article.
Figure 1.
Transcription regulation of mtsA by MtsR is Mn dependent. (A) Genetic organization of the mtsR and mtsA gene region in GAS genome. The mtsR and mtsA genes are divergently transcribed. Numbers below the line indicate the nucleotide positions relative to the first nucleotide of the mtsA start codon. The putative –10 and –35 hexamers of the mtsA promoter and an inferred ribosomal-binding site (RBS) located upstream of mtsAlabeled are marked and labeled above the line. The predicted MtsR-binding site in the mtsA promoter is marked by a shaded box and the pseudoinverted repeat within the MtsR-binding site is marked by arrows. The nucleotide sequence of the MtsR-binding site used in the electrophoretic mobility shift (EMSA) and fluorescent polarization (FP) analyses is shown. (B) The interactions between MtsR and the operator sequences in mtsA promoter as assessed by EMSA. Increasing concentrations (0, 100, 200 and 300 nM MtsR) of non-metallated (apo MtsR) or MtsR bound with different metals were incubated with oligoduplex containing the mtsA promoter sequences. The reaction mixtures were resolved on a 10% native-PAGE and the PAGE running buffer does not contain EDTA. Each indicated metal was added at a final concentration of 300 μM. The positions of free (F) and MtsR-bound (B) probes are labeled and indicated by arrows. E; indicates addition of metal chelator EDTA to the reaction mixture. (C) MtsR-mts motif binding constants assessed in the absence or presence of the indicated metals as assessed by fluorescent polarization (FP) assay. The apparent binding constants with standard deviations are shown. Each indicated metal was added at a final concentration of 10 μM and Mg was added at a final concentration of 1 mM. (D) Wild-type (WT) GAS was grown in THY medium to mid-exponential phase of growth (A600 1.0) and incubated with 100 μM of the indicated metals for 30 min. Transcript level of mtsA was measured by qRT-PCR. Three biological replicates were performed and analyzed in triplicate. Data graphed are means ± standard deviation. Average values for unsupplemented samples were used as a reference and fold changes in transcript levels of the indicated samples relative to reference are shown. Statistical significance was determined by t test. **** indicates statistical significance with P < 0.0001 for the indicated samples compared to reference growth.