Recruitment of the 40S ribosome subunit to the 3'-untranslated region (UTR) of a viral mRNA, via the eIF4 complex, facilitates cap-independent translation.

The Journal of Biological Chemistry
Sohani Das SharmaDixie J Goss

Abstract

Barley yellow dwarf virus mRNA, which lacks both cap and poly(A) tail, has a translation element (3'-BTE) in its 3'-UTR essential for efficient translation initiation at the 5'-proximal AUG. This mechanism requires eukaryotic initiation factor 4G (eIF4G), subunit of heterodimer eIF4F (plant eIF4F lacks eIF4A), and 3'-BTE-5'-UTR interaction. Using fluorescence anisotropy, SHAPE (selective 2'-hydroxyl acylation analyzed by primer extension) analysis, and toeprinting, we found that (i) 40S subunits bind to BTE (Kd = 350 ± 30 nm), (ii) the helicase complex eIF4F-eIF4A-eIF4B-ATP increases 40S subunit binding (Kd = 120 ± 10 nm) to the conserved stem-loop I of the 3'-BTE by exposing more unpaired bases, and (iii) long distance base pairing transfers this complex to the 5'-end of the mRNA, where translation initiates. Although 3'-5' interactions have been recognized as important in mRNA translation, barley yellow dwarf virus employs a novel mechanism utilizing the 3'-UTR as the primary site of ribosome recruitment.

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Citations

Sep 15, 2015·Virus Research·Phillida A Charley, Jeffrey Wilusz
Jul 22, 2016·RNA Biology·Shira Weingarten-Gabbay, Eran Segal
Dec 15, 2017·Frontiers in Plant Science·Verónica TrunigerMiguel A Aranda
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Sep 25, 2015·Virology·Tamari ChkuaseliK Andrew White
Feb 19, 2021·Journal of Virology·Muhammad IlyasAnne E Simon

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