Structural studies of the eIF4E-VPg complex reveal a direct competition for capped RNA: Implications for translation.

ABSTRACT: Viruses have transformed our understanding of mammalian RNA processing, including facilitating the discovery of the methyl-7-guanosine (m⁷G) cap on the 5' end of RNAs. The m⁷G cap is required for RNAs to bind the eukaryotic translation initiation factor eIF4E and associate with the translation machinery across plant and animal kingdoms. The potyvirus-derived viral genome-linked protein (VPg) is covalently bound to the 5' end of viral genomic RNA (gRNA) and associates with host eIF4E for successful infection. Divergent models to explain these observations proposed either an unknown mode of eIF4E engagement or a competition of VPg for the m⁷G cap-binding site. To dissect these possibilities, we resolved the structure of VPg, revealing a previously unknown 3-d

SUBMITTER: Coutinho de Oliveira L 

PROVIDER: S-EPMC6883836 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature