Supplemental Data

Files in this Data Supplement:

• Supplemental Figure 1 - Supplemental Figure 1. Alignment of Arabidopsis PHF1 with presumed functional PHF1 homologues and with SEC12 proteins using the program T-COFFEE (Notredame et al., 2000). Coloured in green are amino acid residues conserved in all PHF1 and SEC12 proteins from plants or animals, blue, amino acid residues conserved in all PHF1 proteins; pink, amino acid residues conserved in all plant and animal SEC12 proteins. At PHF1 (A. thaliana PHF1); Le PHF1 (L. esculentum); Os PHF1 (O. sativa); At STL2P (A. thaliana SEC12 ortholog);Os SEC12 (O. sativa); Ce SEC12 (C. elegans); Dm SEC12 (D. melanogaster); Hs PREB (H. sapiens); Sc SEC12 (S. cerevisiae); Sp STL1 (S. pombe).
• Supplemental Figure 2 - Supplemental Figure 2. Complementation of phf1 with constructs expressing a functional PHF1:GFP fusion protein. Histochemical analysis of IPS1:GUS activity in plants grown in Pi-rich medium (upper panel), and phenotype of plants grown in the presence of 10 ppm arsenate (lower panel). Genetic constitution of plants were: wild type (wt); phf1-1 (phf1); and phf1-1 transformed with a fusion between the promoter plus the coding region of PHF1 and the GFP coding region at the 3’ end (phf1; gPHF1:GFP); or with the PHF1:GFP coding region under the control of the 35S promoter (phf1; oPHF1:GFP).
• Supplemental Figure 3 - Supplemental Figure 3. Subcellular localisation of PHT1;1:GFP in wild type plants grown under a Pi-rich regimen. Micrograph of leaf epidermal cells from transgenic wild type plants harbouring the 35S:PHT1;1:GFP construct. Fluorescence highlights the plasma membrane. Cell junctions are less evident than in Pi starved plants (only one in the center of the micrograph is observed). Scale bars, 10 μµm.
• Supplemental Table 1