Abstract
The unconventional, lysine-63-linked ubiquitination has been shown to play a central role in regulating human and animal innate and adaptive immunity. By contrast, the role and mechanism of K63-linked ubiquitination in plant biology remain largely unexplored. The tomato (Solanum lycopersicum) Fni3 ubiquitin-conjugating enzyme and its co-factor, Suv ubiquitin E2 variant (Uev) were shown recently to catalyze K63-linked ubiquitination and are essential for protein Fen and other resistance protein-mediated plant immunity. In this study we detected the subcellular localization of Fen, Fni3 and Suv and confirmed the interaction of Fni3 with Suv in tomato protoplasts. Additionally, we identified 2 tomato Uev1 homologs, SlUev1C and SlUev1D, respectively and showed they are not required for Fen-mediated programmed cell death in Nicotiana benthamiana, suggesting Uev homologs play differential role in the cell.
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