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An accurately preorganized IRES RNA structure enables eIF4G capture for initiation of viral translation.

Abstract：

:Many viruses bypass canonical cap-dependent translation in host cells by using internal ribosomal entry sites (IRESs) in their transcripts; IRESs hijack initiation factors for the assembly of initiation complexes. However, it is currently unknown how IRES RNAs recognize initiation factors that have no endogenous RNA binding partners; in a prominent example, the IRES of encephalomyocarditis virus (EMCV) interacts with the HEAT-1 domain of eukaryotic initiation factor 4G (eIF4G). Here we report the solution structure of the J-K region of this IRES and show that its stems are precisely organized to position protein-recognition bulges. This multisite interaction mechanism operates on an all-or-nothing principle in which all domains are required. This preorganization is accomplished by an 'adjuster module': a pentaloop motif that acts as a dual-sided docking station for base-pair receptors. Because subtle changes in the orientation abrogate protein capture, our study highlights how a viral RNA acquires affinity for a target protein.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Imai S,Kumar P,Hellen CU,D'Souza VM,Wagner G

doi

10.1038/nsmb.3280

subject

Has Abstract

pub_date

2016-09-01 00:00:00

pages

859-64

issue

9

eissn

1545-9993

issn

1545-9985

pii

nsmb.3280

journal_volume

23

pub_type

杂志文章

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