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Plants are constantly threatened by biotic stresses and, in order to overcome these stresses, they have developed an innate immune system. There is growing evidence that ubiquitination, a post-translational modification, plays a role in regulating the plant defense responses. The ubiquitination reaction involves three enzymes, an ubiquitin-activating enzyme, an ubiquitin-conjugating enzyme, and an ubiquitin ligase. The ubiquitination of a target protein leads to its degradation by a proteasome. The majority of studies have indicated the involvement of the ubiquitin ligase in plant defense regulation, but very little information is available regarding the role of ubiquitin-conjugating enzymes. The Lycopersicon esculentum (tomato) ubiquitin-conjugating enzymes, £eUBCl and 57UBC3, have been previously linked to stress responses. Here, we show through bioinformatics data that these two ubiquitin-conjugating enzymes have significant homology to ubiquitin-conjugating enzymes from other organisms and may perform similar function. Here, we report that the transcript level o f leU BCl and S7UBC3 did not change in tomato leaves treated with fumonisin B l, a fungal toxin, and a proteasome inhibitor, Z-Leu-Leu-NVa-CHO. It has been reported that upon stress, particularly biotic stress, there is an accumulation of defense-related proteins such as glucanases, and a down regulation of metabolism-related enzymes such as glutamine synthetases. In my study, the activity of both (31,3-glucanases and glutamine synthetase was significantly increased after 48 hours of treatment with H2 O, FBI, MG-115, and FB1+MG-115. Finally, TeUBCl and 5/11603 expression was successfully induced in Escherichia coli cells, paving the way for future purification and protein interaction analysis on these proteins.

The role of Lycopersicon esculentum ubiquitin-conjugating enzymes LeUBC1 and S/UBC3 in the response to stress induced by fungal toxin fumonisin B1