edoc

A new plant protein interacts with eIF3 and 60S to enhance virus-activated translation re-initiation

Thiebeauld, O. and Schepetilnikov, M. and Park, H. S. and Geldreich, A. and Kobayashi, K. and Keller, M. and Hohn, T. and Ryabova, L. A.. (2009) A new plant protein interacts with eIF3 and 60S to enhance virus-activated translation re-initiation. The EMBO journal, Vol. 28, H. 20. pp. 3171-3184.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A5261900

Downloads: Statistics Overview

Abstract

The plant viral re-initiation factor transactivator viroplasmin (TAV) activates translation of polycistronic mRNA by a re-initiation mechanism involving translation initiation factor 3 (eIF3) and the 60S ribosomal subunit (60S). QJ; Here, we report a new plant factor-re-initiation supporting protein (RISP)-that enhances TAV function in re-initiation. RISP interacts physically with TAV in vitro and in vivo. Mutants defective in interaction are less active, or inactive, in transactivation and viral amplification. RISP alone can serve as a scaffold protein, which is able to interact with eIF3 subunits a/c and 60S, apparently through the C-terminus of ribosomal protein L24. RISP pre-bound to eIF3 binds 40S, suggesting that RISP enters the translational machinery at the 43S formation step. RISP, TAV and 60S co-localize in epidermal cells of infected plants, and eIF3-TAV-RISP-L24 complex formation can be shown in vitro. These results suggest that RISP and TAV bridge interactions between eIF3-bound 40S and L24 of 60S after translation termination to ensure 60S recruitment during repetitive initiation events on polycistronic mRNA; RISP can thus be considered as a new component of the cell translation machinery.
Faculties and Departments:05 Faculty of Science > Departement Umweltwissenschaften > Ehemalige Einheiten Umweltwissenschaften > Molekulare Pflanzenvirologie (Hohn)
UniBasel Contributors:Hohn, Thomas
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Nature Publishing Group
ISSN:0261-4189
Note:Publication type according to Uni Basel Research Database: Journal article
Related URLs:
Identification Number:
Last Modified:22 Mar 2012 14:25
Deposited On:22 Mar 2012 13:46

Repository Staff Only: item control page