The 5'-leader of tobacco mosaic virus promotes translation through enhanced recruitment of eIF4F.

The 5'-leader sequence (called Omega) of tobacco mosaic virus (TMV) functions as a translational enhancer in plants. A poly(CAA) region within Omega is responsible for the translation enhancement and serves as a binding site for the heat shock protein, HSP101, which is required for the translational enhancement. Genetic analysis of the HSP101-mediated enhancement of translation from Omega-containing mRNA suggested that two eukaryotic initiation factors (eIFs), i.e. eIF4G and eIF3, were necessary. In this study, the functional interaction between Omega and other RNA elements known to participate in the recruitment of eIF4G, i.e. the 5'-cap and the poly(A) tail, was examined. Omega exhibited functional overlap with the 5'-cap and the poly(A) tail but not with the native TMV 3'-UTR which contains an independent translational enhancer. Consistent with the role of HSP101 in mediating the translational function of Omega, the enhancement afforded by Omega increased following a heat shock, which elevates expression of HSP101. The use of a fractionated translation lysate revealed that of the two eIF4F proteins present in plants, eIF4F was specifically required for the activity of Omega. The data suggest that Omega is functionally similar to a 5'-cap and a poly(A) tail in that it serves to recruit eIF4F in order to enhance translation from an mRNA.