Cation-dependent folding of 30 cap-independent translation elements facilitates interaction of a 17-nucleotide conserved sequence with eIF4G

Simple item page
dc.contributor.author Miller, W. Allen
dc.contributor.author Treder, Krzysztof
dc.contributor.author Peterson, Mariko
dc.contributor.author Miller, W. Allen
dc.contributor.department Plant Pathology and Microbiology
dc.date 2018-02-17T04:16:56.000
dc.date.accessioned 2020-06-30T06:23:36Z
dc.date.available 2020-06-30T06:23:36Z
dc.date.copyright Tue Jan 01 00:00:00 UTC 2013
dc.date.issued 2014-01-01
dc.description.abstract <p>The 3'-untranslated regions of many plant viral RNAs contain cap-independent translation elements (CITEs) that drive translation initiation at the 5'-end of the mRNA. The barley yellow dwarf virus-like CITE (BTE) stimulates translation by binding the eIF4G subunit of translation initiation factor eIF4F with high affinity. To understand this interaction, we characterized the dynamic structural properties of the BTE, mapped the eIF4G-binding sites on the BTE and identified a region of eIF4G that is crucial for BTE binding. BTE folding involves cooperative uptake of magnesium ions and is driven primarily by charge neutralization. Footprinting experiments revealed that functional eIF4G fragments protect the highly conserved stem-loop I and a downstream bulge. The BTE forms a functional structure in the absence of protein, and the loop that base pairs the 5'-untranslated region (5'-UTR) remains solventaccessible at high eIF4G concentrations. The region in eIF4G between the eIF4E-binding site and the MIF4G region is required for BTE binding and translation. The data support the model in which the eIF4F complex binds directly to the BTE which base pairs simultaneously to the 5'-UTR, allowing eIF4F to recruit the 40S ribosomal subunit to the 5'-end.</p>
dc.description.comments <p>This article is from <em>Nucleic Acids Research</em> 41 (2013): 3398, doi: <a href="http://dx.doi.org/10.1093/nar/gkt026" target="_blank">10.1093/nar/gkt026</a>. Posted with permission.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/plantpath_pubs/36/
dc.identifier.articleid 1032
dc.identifier.contextkey 7769117
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath plantpath_pubs/36
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/57753
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/plantpath_pubs/36/2013_MillerWA_CationDependentFolding.pdf|||Fri Jan 14 23:46:38 UTC 2022
dc.source.uri 10.1093/nar/gkt026
dc.subject.disciplines Agricultural Science
dc.subject.disciplines Biochemistry, Biophysics, and Structural Biology
dc.subject.disciplines Plant Pathology
dc.subject.keywords initiation factor 4G
dc.subject.keywords magnesium ion
dc.subject.keywords RNA
dc.subject.keywords 3' untranslated region
dc.subject.keywords 5' untranslated region
dc.subject.keywords base pairing
dc.subject.keywords cation transport
dc.subject.keywords gene mapping
dc.subject.keywords genetic conservation
dc.subject.keywords Luteovirus
dc.subject.keywords molecular dynamics
dc.subject.keywords nucleotide binding site
dc.subject.keywords nucleotide sequence
dc.subject.keywords protein footprinting
dc.subject.keywords ribosome subunit
dc.subject.keywords virus neutralization
dc.subject.keywords Eukaryotic initiation factor-4G
dc.subject.keywords magnesium chloride
dc.title Cation-dependent folding of 30 cap-independent translation elements facilitates interaction of a 17-nucleotide conserved sequence with eIF4G
dc.type article
dc.type.genre article
dspace.entity.type Publication
relation.isAuthorOfPublication 4ad3ad12-430c-43b9-8f3c-3a920e00b28c
relation.isOrgUnitOfPublication a26b5928-54bb-4a0b-a973-95d649d1ad83
File
Original bundle
Now showing 1 - 1 of 1
Name:
2013_MillerWA_CationDependentFolding.pdf
Size:
4.21 MB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Publications