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P6 protein of Cauliflower mosaic virus, a translation reinitiator, interacts with ribosomal protein L13 from Arabidopsis thaliana

Véronique Leh

Muriel Haas

Institut de Biologie Moléculaire des Plantes, UPR CNRS 2357, Université Louis Pasteur, 12 rue du Général Zimmer, 67084 Strasbourg Cedex, France

Correspondence
Mario Keller
mario.keller{at}ibmp-ulp.u-strasbg.fr

The P6 protein of Cauliflower mosaic virus (CaMV) transactivates translation of the CaMV 35S polycistronic pregenomic RNA and its spliced versions, and thus allows synthesis of a complete set of viral proteins. Previous studies have shown that P6 interacts with plant L18 and L24 ribosomal proteins and initiation factor eIF3, and it has been proposed that these interactions are involved in the reinitiation of translation of polycistronic viral RNAs. This study characterizes a novel cellular partner of P6, the ribosomal protein L13 from Arabidopsis thaliana. Far-Western assays performed with several P6 deletion mutants have shown that L13 interacts with the miniTAV of P6, which represents the minimal domain for transactivation, suggesting that the P6–L13 interaction might also be involved in this process. L13 and L18 were found to bind to the same region within the miniTAV. Competition assays between L18 and L13 for binding to miniTAV suggest that interactions between P6 and these ribosomal proteins involve separate P6 molecules, and/or occur at different stages of translation or in the context of another function also mediated by P6.

Present address: Laboratoire de Dynamique, Evolution et Expression des Génomes de Microorganismes, FRE CNRS 2326, Université Louis Pasteur, 28 rue Goethe, 67084 Strasbourg Cedex, France.

Present address: UPR CNRS 9050, Département Récepteurs et Protéines Membranaires, ESBS, boulevard Sébastient Brant, 67412 Illkirch Cedex, France.

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