PMID:1739968

Citation	Dever, TE, Feng, L, Wek, RC, Cigan, AM, Donahue, TF and Hinnebusch, AG (1992) Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68:585-96
Abstract	We show that phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2) by the protein kinase GCN2 mediates translational control of the yeast transcriptional activator GCN4. In vitro, GCN2 specifically phosphorylates the alpha subunit of rabbit or yeast eIF-2. In vivo, phosphorylation of eIF-2 alpha increases in response to amino acid starvation, which is dependent on GCN2. Substitution of Ser-51 with alanine eliminates phosphorylation of eIF-2 alpha by GCN2 in vivo and in vitro and abolishes increased expression of GCN4 and amino acid biosynthetic genes under its control in amino acid-starved cells. The Asp-51 substitution mimics the phosphorylated state and derepresses GCN4 in the absence of GCN2. Thus, an established mechanism for regulating total protein synthesis in mammalian cells mediates gene-specific translational control in yeast.
Links	PubMed
Keywords	Animals; Base Sequence; DNA Mutational Analysis; DNA-Binding Proteins; Fungal Proteins/genetics; Humans; Infant, Newborn; Models, Genetic; Molecular Sequence Data; Oligonucleotide Probes; Open Reading Frames; Peptide Initiation Factors/metabolism; Phosphorylation; Plasmids; Prokaryotic Initiation Factor-2; Protein Biosynthesis; Protein Kinases/metabolism; Protein-Serine-Threonine Kinases; Rabbits; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae Proteins; Serine; Transcription Factors/genetics
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