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. 1998 Apr 14;95(8):4164–4169. doi: 10.1073/pnas.95.8.4164

Figure 1.

Figure 1

Reduced eIF2α phosphorylation in insect cells infected with wild-type but not pk2-deleted baculovirus. (A) Comparison of the PK2, PKR, and GCN2 proteins. Kinase subdomains (1, 2) are indicated, and the ATP-binding site is indicated as a box. The regulatory domains of PKR [dsRNA-binding domain (dsRNA-BD)] and GCN2 [histidyl-tRNA synthetase-like domain (HisRS)] are indicated as lightly shaded boxes. GCN2-TK, a truncated version of GCN2, corresponds in size to PK2 and contains only kinase subdomains V–XI (amino acids 779–996) of GCN2; the corresponding region of PKR extends from amino acid residue 357 to 551. (B) Analysis of eIF2α phosphorylation in insect cells. Twenty (lanes 1–3) or 50 (lanes 4–6) μg of crude protein extracts from SF-9 cells infected with wild-type (L1) or pk2-deleted (vKINdel) baculovirus or mock-infected (uninfected) were analyzed by IEF gel electrophoresis followed by immunoblotting with eIF2α monoclonal antibodies. The migration positions of phosphorylated and unphosphorylated eIF2α are indicated, and the percentage of eIF2α that is phosphorylated was determined by quantitative densitometry and is indicated below lanes 1–3.