Structural determinants of an internal ribosome entry site that direct translational reading frame selection.

Abstract:

:The dicistrovirus intergenic internal ribosome entry site (IGR IRES) directly recruits the ribosome and initiates translation using a non-AUG codon. A subset of IGR IRESs initiates translation in either of two overlapping open reading frames (ORFs), resulting in expression of the 0 frame viral structural polyprotein and an overlapping +1 frame ORFx. A U-G base pair adjacent to the anticodon-like pseudoknot of the IRES directs +1 frame translation. Here, we show that the U-G base pair is not absolutely required for +1 frame translation. Extensive mutagenesis demonstrates that 0 and +1 frame translation can be uncoupled. Ribonucleic acid (RNA) structural probing analyses reveal that the mutant IRESs adopt distinct conformations. Toeprinting analysis suggests that the reading frame is selected at a step downstream of ribosome assembly. We propose a model whereby the IRES adopts conformations to occlude the 0 frame aminoacyl-tRNA thereby allowing delivery of the +1 frame aminoacyl-tRNA to the A site to initiate translation of ORFx. This study provides a new paradigm for programmed recoding mechanisms that increase the coding capacity of a viral genome.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Ren Q,Au HH,Wang QS,Lee S,Jan E

doi

10.1093/nar/gku622

subject

Has Abstract

pub_date

2014-08-01 00:00:00

pages

9366-82

issue

14

eissn

0305-1048

issn

1362-4962

pii

gku622

journal_volume

42

pub_type

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