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

Thiébeauld, Odon and Schepetilnikov, Mikhail and Park, Hyun-Sook and Geldreich, Angèle and Kobayashi, Kappei and Keller, Mario and Hohn, Thomas and Ryabova, Lyubov A (2009) A new plant protein interacts with eIF3 and 60S to enhance virus-activated translation re-initiation. The EMBO Journal, 28 (20). pp. 3171-3184. ISSN 0261-4189

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.

Item Type: Article
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Additional Information: Author can archive post-print (ie final draft post-refereeing); Publisher's version/PDF cannot be used
Keywords: Cauliflower mosaic virus (CaMV); eIF3; large ribosomal subunit (60S); re-initiation supporting protein (RISP); transactivator viroplasmin (TAV)
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Date Deposited: 22 Feb 2010 11:49
Last Modified: 05 Sep 2018 00:45
URI: https://oak.novartis.com/id/eprint/2227

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