mRNA cap-binding protein: cloning of the gene encoding protein synthesis initiation factor eIF-4E from Saccharomyces cerevisiae.

Altmann, M; Handschin, C; Trachsel, Hans

doi:10.1128/mcb.7.3.998

Cited by 136 publications

(79 citation statements)

References 12 publications

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“…The activity of elF-4E is physiologically regulated by phosphorylation at Ser-53 [2]. cDNAs or genes for elF-4E have been cloned from yeast [3], mouse [4], rabbit [5], human [6] and wheat [7,8]. The amino acid sequence as deduced from the cDNA clones predicts the presence of 8 tryptophans (9 in wheat elF-4E) that are evolutionarily remarkably conserved in number and position.…”

Section: Introductionmentioning

confidence: 99%

mRNA encoding the translation initiation factor eIF‐4E is expressed early in Xenopus embryogenesis

et al. 1995

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The translation initiation factor elF-4E plays an important role in regulating the overall rate of translation in eukaryotic cells. To investigate the expression of elF-4E itselF, we characterized the elF-4E mRNA expressed in Xenopus embryos. 5'-RACE was performed to determine the 5'-end of the mRNA and the result predicts isoforms differing at the amino-terminal end. Expression of the elF-4E mRNA in Xenopus oocytes and embryos was examined by RT-PCR. Xenopus elF-4E mRNA is produced during oogenesis and persists during the early stages of embryogenesis as a maternal mRNA.

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Section: Introductionmentioning

confidence: 99%

mRNA encoding the translation initiation factor eIF‐4E is expressed early in Xenopus embryogenesis

et al. 1995

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“…Temperature-sensitive alleles of the CDC33 gene lead to a defect in translation initiation in vivo and an arrest in the G 1 phase of the cell cycle (8)(9)(10)(11). Recently, the analysis of deletion variants of eIF4E with reduced affinity for the 5Ј cap indicated that eIF4E mediates the selectivity of yeast ribosomes for capped mRNAs (12).…”

mentioning

confidence: 99%

The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent translation in Saccharomyces cerevisiae

Cruz¹,

Iost²,

Kressler³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

198

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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.

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“…This function is critical during scanning for exposing and locating the translation start site (4 -6). In Saccharomyces cerevisiae, eIF4E was cloned as a cell division cycle gene (CDC33), essential for cell viability (7,8). CDC33 is involved in the G 1 -S transition of the cell cycle.…”

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confidence: 99%

Translational Regulation of Ribonucleotide Reductase by Eukaryotic Initiation Factor 4E Links Protein Synthesis to the Control of DNA Replication

Abid

Anthony

et al. 1999

Journal of Biological Chemistry

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Ribonucleotide reductase synthesizes dNDPs, a specific and limiting step in DNA synthesis, and can participate in neoplastic transformation when overexpressed. The small subunit (ribonucleotide reductase 2 (RNR2)) was cloned as a major product in a subtraction library from eukaryotic initiation factor 4E (eIF4E)-transformed cells (Chinese hamster ovary-4E (CHO-4E)). CHO-4E cells have 20 -40-fold elevated RNR2 protein, reflecting an increased distribution of RNR2 mRNA to the heavy polysomes. CHO-4E cells display an altered cell cycle with shortened S phase, similar to cells selected for RNR2 overexpression with hydroxyurea. The function of ribonucleotide reductase as a checkpoint component of S progression was studied in yeast in which elevated eIF4E rescued S-arrested rnr2-68 ts cells, by increasing recruitment of its mRNA to polysomes. Crosses between rnr2-68 ts and mutant eIF4E (cdc33-1 ts ) engendered conditional synthetic lethality, with extreme sensitivity to hydroxyurea and the microtubule depolymerizing agent, benomyl. The double mutant (cdc33-1 rnr2-68) also identified a unique terminal phenotype, arrested with small bud and a randomly distributed single nucleus, which is distinct from those of both parental single mutants. This phenotype defines eIF4E and RNR2 as determinants in an important cell cycle checkpoint, in early/mid-S phase. These results also provide a link between protein and DNA synthesis and provide an explanation for cell cycle alterations induced by elevated eIF4E.

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mRNA cap-binding protein: cloning of the gene encoding protein synthesis initiation factor eIF-4E from Saccharomyces cerevisiae.

Cited by 136 publications

References 12 publications

mRNA encoding the translation initiation factor eIF‐4E is expressed early in Xenopus embryogenesis

mRNA encoding the translation initiation factor eIF‐4E is expressed early in Xenopus embryogenesis

The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent translation in Saccharomyces cerevisiae

Translational Regulation of Ribonucleotide Reductase by Eukaryotic Initiation Factor 4E Links Protein Synthesis to the Control of DNA Replication

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