Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation

Andrew W. B. Craig, Ashkan Haghighat, Annie T. K. Yu and Nahum Sonenberg ()
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Andrew W. B. Craig: McGill University
Ashkan Haghighat: McGill University
Annie T. K. Yu: McGill University
Nahum Sonenberg: McGill University

Nature, 1998, vol. 392, issue 6675, 520-523

Abstract: Abstract In the initiation of translation in eukaryotes, binding of the small ribosomal subunit to the messenger RNA results from recognition of the 5′ cap structure (m7GpppX) of the mRNA by the cap-binding complex eIF4F1. eIF4F is itself a three-subunit complex comprising the cap-binding protein eIF4E2, eIF4A, an ATP-dependent RNA helicase3, and eIF4G, which interacts with both eIF4A and eIF4E and enhances cap binding by eIF4E4. The mRNA 3′ polyadenylate tail and the associated poly(A)-binding protein (PABP) also regulate translational initiation5, probably by interacting with the 5′ end of the mRNA6,7. In yeast8,9 and plants10, PABP interacts with eIF4G8,9 but no such interaction has been reported in mammalian cells. Here, we describe a new human PABP-interacting protein, PAIP-1, whose sequence is similar to the central portion of eIF4G and which interacts with eIF4A. Overexpression of PAIP-1 in COS-7 cells stimulates translation, perhaps by providing a physical link between the mRNA termini.

Date: 1998
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DOI: 10.1038/33198

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