Document Type
Article
Publication Version
Published Version
Publication Date
1-2014
Journal or Book Title
Nucleic Acids Research
Volume
41
Issue
5
First Page
3398
Last Page
3413
DOI
10.1093/nar/gkt026
Abstract
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.
Rights
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/ by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Copyright Owner
The Author(s)
Copyright Date
2013
Language
en
File Format
application/pdf
Recommended Citation
Kraft, Jelena Jeremic; Treder, Krzysztof; Peterson, Mariko Sada; and Miller, W. Allen, "Cation-dependent folding of 30 cap-independent translation elements facilitates interaction of a 17-nucleotide conserved sequence with eIF4G" (2014). Plant Pathology and Microbiology Publications. 36.
https://lib.dr.iastate.edu/plantpath_pubs/36
Included in
Agricultural Science Commons, Biochemistry, Biophysics, and Structural Biology Commons, Plant Pathology Commons
Comments
This article is from Nucleic Acids Research 41 (2013): 3398, doi: 10.1093/nar/gkt026. Posted with permission.