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The ubiquitin conjugating enzyme E2 (UBC E2) mediates selective ubiquitination, acting with E1 and E3 enzymes to designate specific proteins for subsequent degradation. In the present study, we characterized the function of the mung bean  VrUBC1  gene (  V igna  r adiata  UBC  1 ). RNA gel-blot analysis showed that  VrUBC1  mRNA expression was induced by either dehydration, high salinity or by the exogenous abscisic acid (ABA), but not by low temperature or wounding. Biochemical studies of VrUBC1 recombinant protein and complementation of yeast  ubc4/5  by  VrUBC1  revealed that  VrUBC1  encodes a functional UBC E2. To understand the function of this gene in development and plant responses to osmotic stresses, we overexpressed  VrUBC1  in Arabidopsis ( Arabidopsis thaliana ). The  VrUBC1 -overexpressing plants displayed highly sensitive responses to ABA and osmotic stress during germination, enhanced ABA- or salt-induced stomatal closing, and increased drought stress tolerance. The expression levels of a number of key ABA signaling genes were increased in  VrUBC1 -overexpressing plants compared to the wild-type plants. Yeast two-hybrid and bimolecular fluorescence complementation demonstrated that VrUBC1 interacts with AtVBP1 (  A .  t haliana   V rUBC1  B inding  P artner  1 ), a C3HC4-type RING E3 ligase. Overall, these results demonstrate that  VrUBC1  plays a positive role in osmotic stress tolerance through transcriptional regulation of ABA-related genes and possibly through interaction with a novel RING E3 ligase.

Overexpression of VrUBC1, a Mung Bean E2 Ubiquitin-Conjugating Enzyme, Enhances Osmotic Stress Tolerance in Arabidopsis