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We began analyzing https://www.tandfonline.com/doi/full/10.1128/MCB.17.12.6876, but it redirected us to https://www.tandfonline.com/doi/full/10.1128/MCB.17.12.6876. The analysis below is for the second page.

Title[redir]:
Binding of Eukaryotic Translation Initiation Factor 4E (eIF4E) to eIF4G Represses Translation of Uncapped mRNA: Molecular and Cellular Biology: Vol 17, No 12
Description:
mRNA translation in crude extracts from the yeast Saccharomyces cerevisiae is stimulated by the cap structure and the poly(A) tail through the binding of the cap-binding protein eukaryotic translat...

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Keywords {🔍}

translation, eife, eifg, binding, mrna, taylor, francis, group, page, journals, article, extracts, yeast, search, eukaryotic, research, initiation, factor, uncapped, protein, uncappedmrna, vivo, vitro, open, register, molecular, cellular, biology, volume, issue, journal, citations, date, reprints, read, polya, pabp, proteins, mutations, tifp, stimulation, information, access, solutions, skip, main, content, publish, login, add,

Topics {✒️}

tail-binding protein pab1p twitter page taylor francis group eukaryotic translation initia receive personalised research efficiently stimulate translation pab1p binding sites eif4g represses translation uncapped-mrna translation tarun jr &alan yeast saccharomyces cerevisiae general translational apparatus temperature-sensitive growth journals books uncapped mrna salvador exogenous uncapped mrna yeast extracts due eif4e binding site eif4g protein cap structure article https date register yeast extracts deficient mrna free eif4g register add cart home sachs pages 6876-6886 published online crude extracts translated poorly tif4632p lead data support translationally regulated contact newsroom email sign taylor england & wales sw1p 1wg journal binding search excess eif4e vitro reverses uncapped mrna tail proteins eif4g extracts

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      name:Binding of Eukaryotic Translation Initiation Factor 4E (eIF4E) to eIF4G Represses Translation of Uncapped mRNA
      headline:Binding of Eukaryotic Translation Initiation Factor 4E (eIF4E) to eIF4G Represses Translation of Uncapped mRNA
      abstract:mRNA translation in crude extracts from the yeast Saccharomyces cerevisiae is stimulated by the cap structure and the poly(A) tail through the binding of the cap-binding protein eukaryotic translation initiation factor 4E (eIF4E) and the poly(A) tail-binding protein Pab1p. These proteins also bind to the translation initiation factor eIF4G and thereby link the mRNA to the general translational apparatus. In contrast, uncapped, poly(A)-deficient mRNA is translated poorly in yeast extracts, in part because of the absence of eIF4E and Pab1p binding sites on the mRNA. Here, we report that uncapped-mRNA translation is also repressed in yeast extracts due to the binding of eIF4E to eIF4G. Specifically, we find that mutations which weaken the eIF4E binding site on the yeast eIF4G proteins Tif4631p and Tif4632p lead to temperature-sensitive growth in vivo and the stimulation of uncapped-mRNA translation in vitro. A mutation in eIF4E which disturbs its ability to interact with eIF4G also leads to a stimulation of uncapped-mRNA translation in vitro. Finally, overexpression of eIF4E in vivo or the addition of excess eIF4E in vitro reverses these effects of the mutations. These data support the hypothesis that the eIF4G protein can efficiently stimulate translation of exogenous uncapped mRNA in extracts but is prevented from doing so as a result of its association with eIF4E. They also suggest that some mRNAs may be translationally regulated in vivo in response to the amount of free eIF4G in the cell.
      description:mRNA translation in crude extracts from the yeast Saccharomyces cerevisiae is stimulated by the cap structure and the poly(A) tail through the binding of the cap-binding protein eukaryotic translation initiation factor 4E (eIF4E) and the poly(A) tail-binding protein Pab1p. These proteins also bind to the translation initiation factor eIF4G and thereby link the mRNA to the general translational apparatus. In contrast, uncapped, poly(A)-deficient mRNA is translated poorly in yeast extracts, in part because of the absence of eIF4E and Pab1p binding sites on the mRNA. Here, we report that uncapped-mRNA translation is also repressed in yeast extracts due to the binding of eIF4E to eIF4G. Specifically, we find that mutations which weaken the eIF4E binding site on the yeast eIF4G proteins Tif4631p and Tif4632p lead to temperature-sensitive growth in vivo and the stimulation of uncapped-mRNA translation in vitro. A mutation in eIF4E which disturbs its ability to interact with eIF4G also leads to a stimulation of uncapped-mRNA translation in vitro. Finally, overexpression of eIF4E in vivo or the addition of excess eIF4E in vitro reverses these effects of the mutations. These data support the hypothesis that the eIF4G protein can efficiently stimulate translation of exogenous uncapped mRNA in extracts but is prevented from doing so as a result of its association with eIF4E. They also suggest that some mRNAs may be translationally regulated in vivo in response to the amount of free eIF4G in the cell.
      author:
            type:Person
            name:Salvador Z. Tarun
            type:Person
            name:Alan B. Sachs
      pageStart:6876
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      datePublished:2023-03-29
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