Reference: de la Cruz J, et al. (1997) The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent translation in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 94(10):5201-6

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Abstract


The translation initiation factor eIF4E mediates the binding of the small ribosomal subunit to the cap structure at the 5' end of the mRNA. In Saccharomyces cerevisiae, the cap-binding protein eIF4E is mainly associated with eIF4G, forming the cap-binding complex eIF4F. Other proteins are detected upon purification of the complex on cap-affinity columns. Among them is p20, a protein of unknown function encoded by the CAF20 gene. Here, we show a negative regulatory role for the p20 protein in translation initiation. Deletion of CAF20 partially suppresses mutations in translation initiation factors. Overexpression of the p20 protein results in a synthetic enhancement of translation mutation phenotypes. Similar effects are observed for mutations in the DED1 gene, which we have isolated as a multicopy suppressor of a temperature-sensitive eIF4E mutation. The DED1 gene encodes a putative RNA helicase of the DEAD-box family. The analyses of its suppressor activity, of polysome profiles of ded1 mutant strains, and of synthetic lethal interactions with different translation mutants indicate that the Ded1 protein has a role in translation initiation in S. cerevisiae.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
de la Cruz J, Iost I, Kressler D, Linder P
Primary Lit For
TIF4632 | TIF4631 | DED1 | CAF20 | CDC33

Gene Ontology Annotations 1 entry for 1 gene


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Gene/ComplexQualifierGene Ontology TermAnnotation ExtensionEvidenceSourceAssigned On
CAF20involved innegative regulation of translationIMPSGD2013-08-07
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Interactor Interactor Allele Assay Annotation Action Phenotype SGA score P-value Source Reference

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No physical interaction data for de la Cruz J, et al. (1997)
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