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46
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Translational initiation factor elF-G mediates in vitro poly(A) tail-dependent translation
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of outstanding interest. The authors provide evidence that yeast translation factor elF-4G features a binding site for poly(A)-binding protein Pab 1p. This leads to an interaction between elF-4G, a subunit of cap-associated initiation factor elF-4F at the 5′ end of the mRNA and poly(A)-Pab1p at the 3′ ends of the mRNA.
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Tarun SZ, Wells SE, Deardoff JA, Sachs AB. Translational initiation factor elF-G mediates in vitro poly(A) tail-dependent translation. of outstanding interest Proc Natl Acad Sci USA. 94:1997;9046-9051 The authors provide evidence that yeast translation factor elF-4G features a binding site for poly(A)-binding protein Pab 1p. This leads to an interaction between elF-4G, a subunit of cap-associated initiation factor elF-4F at the 5′ end of the mRNA and poly(A)-Pab1p at the 3′ ends of the mRNA.
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Tarun, S.Z.1
Wells, S.E.2
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Sachs, A.B.4
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47
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0030952218
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Translation initiation factors elF-iso4G and elF-4B interact with the poly(A)-binding protein and increase its RNA binding activity
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of outstanding interest. This report demonstrates the interaction between cap-associated initiation factor elF-iso4F and elF-4B with the poly(A)-binding protein (PABP) in plants. elF-iso4G, the subunit of elF-iso4F, was found to be involved in the binding of PABP. A similar mechanism in yeast and plants seems to participate in 3′-UTR regulation of mRNA initiation and turnover.
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Le H, Tanguay RL, Balasta ML, Wei CC, Browning KS, Metz AM, Goss DJ, Gallie DR. Translation initiation factors elF-iso4G and elF-4B interact with the poly(A)-binding protein and increase its RNA binding activity. of outstanding interest J Biol Chem. 272:1997;16247-16255 This report demonstrates the interaction between cap-associated initiation factor elF-iso4F and elF-4B with the poly(A)-binding protein (PABP) in plants. elF-iso4G, the subunit of elF-iso4F, was found to be involved in the binding of PABP. A similar mechanism in yeast and plants seems to participate in 3′-UTR regulation of mRNA initiation and turnover.
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J Biol Chem
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Le, H.1
Tanguay, R.L.2
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48
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Interaction of polyadenylate-binding protein with the eF4G homologue PAIP enhances translation
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Roberts RW, Szostak JW. RNA-peptide fusions for the in vitro selection of peptides and proteins. of outstanding interest Proc Natl Acad Sci USA. 94:1997;12297-12302 The authors demonstrate in a model system that the puromycin-based in vitro selection technique is able to enrich binding ligands out of a doped peptide library.
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