Gross, John D., Moerke, Nathan, von der Haar, Tobias, Lugovskoy, A.A., Sachs, A.B., McCarthy, John E. G., Wagner, Gerhard (2003) Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E. Cell, 115 . pp. 739-750. ISSN 0092-8674. E-ISSN 1097-4172. (doi:10.1016/S0092-8674(03)00975-9) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:423)
PDF
Language: English Restricted to Repository staff only |
|
|
![]() |
Official URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... |
Abstract
The eukaryotic initiation factor 4G (eIF4G) is the core of a multicomponent switch controlling gene expression at the level of translation initiation. It interacts with the small ribosomal subunit interacting protein, eIF3, and the eIF4E/cap-mRNA complex in order to load the ribosome onto mRNA during cap-dependent translation. We describe the solution structure of the complex between yeast eIF4E/cap and eIF4G (393-490). Binding triggers a coupled folding transition of eIF4G (393-490) and the eIF4E N terminus resulting in a molecular bracelet whereby eIF4G (393-490) forms a right-handed helical ring that wraps around the N terminus of eIF4E. Cofolding allosterically enhances association of eIF4E with the cap and is required for maintenance of optimal growth and polysome distributions in vivo. Our data explain how mRNA, eIF4E, and eIF4G exists as a stable mRNP that may facilitate multiple rounds of ribosomal loading during translation initiation, a key determinant in the overall rate of protein synthesis.
Item Type: | Article |
---|---|
DOI/Identification number: | 10.1016/S0092-8674(03)00975-9 |
Subjects: | Q Science |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Susan Davies |
Date Deposited: | 19 Dec 2007 18:14 UTC |
Last Modified: | 09 Mar 2023 11:29 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/423 (The current URI for this page, for reference purposes) |
- Export to:
- RefWorks
- EPrints3 XML
- BibTeX
- CSV
- Depositors only (login required):