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Stress responses

Translational control perks up

Nature volume 397, pages 209–211 (1999)Cite this article

The ability to respond to a variety of threats — from nutrient deprivation and viruses to chemical insults — is an essential property of cells. But how did primitive organisms survive these challenges, enabling them to evolve into complex animals? Stress responses are often linked to protein synthesis and folding which, in the budding yeast Saccharomyces cerevisiae, are controlled by two different kinds of gene, GCN2 and Ire1. On page 271 of this issue, Harding et al.1 describe a newly discovered mammalian gene with features from both of these yeast genes.

In yeast, amino-acid starvation is sensed by the GCN2 protein, which phosphorylates a conserved serine residue on the α-subunit of the eukaryotic initiation factor-2 (eIF2α)2. Phosphorylation of eIF2α suppresses translation from short upstream open reading frames within the messenger RNA for GCN4. The result is increased translation of GCN4, which activates transcription of the enzymes that synthesize amino acids.

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Figure 1: Relationship of yeast and mammalian stress-response proteins.

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Authors and Affiliations

  1. The Department of Cancer Biology of the Lerner Research Institute, The Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, 44195, Ohio, USA

    Robert H. Silverman & Bryan R. G. Williams

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  1. Robert H. Silverman
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  2. Bryan R. G. Williams
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Silverman, R., Williams, B. Translational control perks up. Nature 397, 209–211 (1999). https://doi.org/10.1038/16586

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