Evidence that Yih1 resides in a complex with ribosomes

@article{Waller2012EvidenceTY,
  title={Evidence that Yih1 resides in a complex with ribosomes},
  author={Tracey Waller and Su Jung Lee and E. Sattlegger},
  journal={The FEBS Journal},
  year={2012},
  volume={279}
}
Adjusting protein synthesis by phosphorylating eukaryotic translation initiation factor 2 (eIF2α) is a major mechanism by which eukaryotes adapt to and overcome stress. The eIF2α kinase Gcn2 is essential for overcoming amino acid starvation in all eukaryotes. We have shown that to sense starvation, the Gcn2 RWD domain must directly contact its effector protein, Gcn1, and both must bind to the ribosome, suggesting that starvation is sensed within a Gcn1–Gcn2–ribosome complex. The mammalian… Expand
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TLDR
This work has proposed a model for sensing starvation, in which Gcn1 and Gcn2 are tethered to the ribosome, and EEF1A is directly involved in delivering uncharged tRNAs from the A-site to GCN2 for its subsequent activation. Expand
Saccharomyces cerevisiae Rbg1 Protein and Its Binding Partner Gir2 Interact on Polyribosomes with Gcn1
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It is shown here that Rbg1 specifically associates with translating ribosomes, and its interacting partner Gir2 associate with ribosites, and their possible biological roles are discussed. Expand
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TLDR
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TLDR
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YIH1, when overexpressed, dampens the GAAC response (Gcn– phenotype) by suppressing eIF2α phosphorylation by GCN2, and it is discovered that YIH 1 normally resides in a complex with monomeric actin, rather than GCN1, and that a genetic reduction in actin levels decreases theGAAC response. Expand
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