Genetic evidence for functional specificity of the yeast GCN2 kinase.
In yeast the GCN2 kinase mediates translational control of GCN4 by phosphorylating the alpha subunit of eIF-2 in response to extracellular amino acid limitation. Although phosphorylation of eIF-2 alpha has been shown to inhibit global protein synthesis, amino acid starvation results in a specific activation effect on GCN4 mRNA translation. Under the same conditions, translation of other mRNAs appears only slightly affected. The mechanism responsible for the observed selectivity of the GCN2 kinase is not clear. Here, we present genetic evidence that suggests that locally restricted action of the GCN2 kinase facilitates GCN4-specific translational regulation.
Tavernarakis
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N
Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology, Heraklion, Crete, Greece.
Thireos
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G
D004268:DNA-Binding Proteins; D005656:Fungal Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal / Q000235:genetics; D014176:Protein Biosynthesis / Q000235:genetics*; D011494:Protein Kinases / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism*; D012331:RNA, Fungal / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity; D015003:Yeasts / Q000201:enzymology / Q000235:genetics* / Q000254:growth & development
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D012331:RNA, Fungal; D012333:RNA, Messenger; D029701:Saccharomyces cerevisiae Proteins; D011494:Protein Kinases