Raw data and analysis of the data corresponding to the manuscript A mutation in the RNA-binding protein Cth2 limits the adaptation of a subset of wild Saccharomyces cerevisiae yeast strains to iron deficiency [DATASET]

Figure 1. S. cerevisiae strains adapted to human feces are tolerant to high iron concentrations. Figure 2. Sensibility of S. cerevisiae yeast strains to iron scarcity. Figure 3. Glycine 195 is a conserved residue in tandem-zinc finger proteins similar to Cth2. Figure 4. The CTH2-G195R allele leads to a growth defect in iron-deficient conditions. Figure 5. The CTH2-G195R allele limits the downregulation of ARE-containing mRNAs. Figure 6. Glycine 195 is essential for the in vivo interaction between Cth2 protein with its target mRNAs. Figure 7. Cth2-G195R protein accumulates in the nucleus. Figure 8. Wild yeast strains expressing CTH2-G195R are defective in Cth2-mediated mRNA downregulation. Figure 9. The replacement of CTH2-R195 by CTH2-G195 allele improves the growth of a set of wild yeast strains in iron-deficient conditions. Figure S1. S. cerevisiae strains adapted to human feces are tolerant to high iron concentrations. Figure S2. Sensibility of S. cerevisiae yeast strains to iron scarcity. Figure S3. The CTH2-G195R allele leads to a growth defect in iron-deficient conditions. Figure S4. The CTH2-G195R allele limits the downregulation of ARE-containing mRNAs. Figure S5. Wild yeast strains expressing CTH2-G195R are defective in Cth2-mediated mRNA downregulation. Figure S6. Sensibility of S. cerevisiae yeast strains to iron scarcity.