, an E3 Ubiquitin Ligase, Enhances the Thermotolerance in .

E3 ubiquitin ligase plays a vital role in the ubiquitin-mediated heat-related protein degradation pathway. Herein, we report that the expression of , a C3HC4 zinc-finger ubiquitin E3 ligase gene, was induced by heat stress, and the β-glucuronidase () gene driven by the promoter has shown increased activity after basal and acquired thermotolerance. To further explore the function of in heat stress response (HSR), we used the mutant and -overexpressing lines (OE2 and OE10) to expose in heat shock. In this study, the mutant had a lower germination and survival rate than those of Col-0 when suffered from the heat stress, whereas OEs enhanced basal and acquired thermotolerance in seedlings. When compared to Col-0 and OEs, loss-of-function in resulted in lower chlorophyll retention and higher content of reactive oxygen species (ROS) after heat treatment. Moreover, the transcript levels of and several heat-related genes ( and ) were upregulated to greater extents in OEs and lower extents in compared to Col-0 after heat treated. Hence, we suggest that may act as a positive role in regulating the high temperature by mediating the degradation of unknown target proteins.