
Structural studies of the eIF4E–VPg complex reveal a direct ... - PNAS
2019年11月12日 · We demonstrated that VPg binds the cap-binding site of eIF4E and forms trimeric complexes with eIF4E and eIF4G; furthermore, we demonstrated that VPg–RNA conjugates directly bind eIF4E and were templates for translation consistent with the requirement of potyviruses for VPg–eIF4E interactions for their lifecycle.
Norovirus Translation Requires an Interaction between
2014年8月1日 · Mutational analyses indicated that the C-terminal region of VPg is important for the VPg-eIF4G interaction; viruses with mutations that alter or disrupt this interaction are debilitated or non-viable. Our results shed new light on the unusual mechanisms of protein-directed translation initiation.
Norovirus translation requires an interaction between the C ... - PubMed
2014年8月1日 · Mutational analyses indicated that the C-terminal region of VPg is important for the VPg-eIF4G interaction; viruses with mutations that alter or disrupt this interaction are debilitated or non-viable. Our results shed new light on the unusual mechanisms of protein-directed translation initiation.
A Conserved Interaction between a C-Terminal Motif in Norovirus VPg …
2016年1月6日 · Fine mutagenic mapping suggests that the MNV VPg C terminus may interact with eIF4G in a helical conformation. NMR spectroscopy was used to define the VPg binding site on eIF4G HEAT-1, which was confirmed by mutagenesis and binding assays.
A Conserved Interaction between a C-Terminal Motif in Norovirus VPg …
The functional significance of the VPg-eIF4G interaction was shown by the ability of fusion proteins containing the C-terminal peptide of MNV VPg to inhibit in vitro translation of norovirus RNA but not cap- or IRES-dependent translation. These observations define important structural details of a functional interaction between norovirus VPg ...
Structural studies of the eIF4E-VPg complex reveal a direct ... - PubMed
2019年11月26日 · 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 m 7 G cap-binding site.
To dissect these possibilities, we resolved the structure of VPg, revealing a previously unknown 3-dimensional (3D) fold, and characterized the VPg–eIF4E complex using NMR and biophysical techniques. VPg directly bound the cap-binding site of eIF4E and competed for …
Norovirus Translation Requires an Interaction between the C …
This approach revealed that VPg binds directly to the eIF4F complex, with a high affinity interaction occurring between VPg and eIF4G. Mutational analyses indicated that the C-terminal region of VPg is important for the VPg-eIF4G interaction; viruses with mutations that alter or disrupt this interaction are debilitated or non-viable.
Potyvirus Genome-linked Protein, VPg, Directly Affects Wheat …
2008年1月18日 · Potyvirus genome linked protein, VPg, interacts with translation initiation factors eIF4E and eIFiso4E, but its role in protein synthesis has not been elucidated. We show that addition of VPg to wheat germ extract leads to enhancement of uncapped viral mRNA translation and inhibition of capped viral mRNA translation.
Structural studies of the eIF4E–VPg complex reveal a direct …
We demonstrated that VPg binds the cap-binding site of eIF4E and forms trimeric complexes with eIF4E and eIF4G; furthermore, we demonstrated that VPg–RNA conjugates directly bind eIF4E and were templates for translation consistent with the requirement of potyviruses for VPg–eIF4E interactions for their lifecycle.