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. 1998 Feb;18(2):859–871. doi: 10.1128/mcb.18.2.859

FIG. 7.

FIG. 7

P52rIPK and P58IPK regulate PKR-mediated eIF-2α phosphorylation. Protein extracts (16 μg) from yeast strains cultured in galactose-containing selective liquid medium for 9 h (A) or 5 h (B), were subjected to vertical gel isoelectric focusing and anti-eIF-2α immunoblot analysis. For each panel, the lower arrow indicates the position of hypophosphorylated eIF-2α. The upper arrow denotes the position of hyperphosphorylated eIF-2α, which is phosphorylated on serine 51 by PKR (22). The percentage of hypophosphorylated eIF-2α is presented beneath each lane. (A) Analysis of RY1-1 strains shown in Fig. 5, harboring pEMBLYex4 (vector; lane 1), pYex-P58IPK (lane 2), or pYex-PKR Δ295–300 (lane 3). (B) Analysis of the isogenic control strain J110 harboring pEMBLYex4 (lane 1) and the RY1-1 strains shown in Fig. 6, which harbor the plasmid combinations of pEMBLYex4-pYX233 (v/v; lane 2), pEMBLYex4–pYX-P52 (v/P52rIPK; lane 3), pYex-P58IPK–pYX233 (P58IPK/v; lane 4), and pYex-P58IPK–pYX-P52 (P58/P52; lane 5).