中文摘要：

在 flowering 植物，自我障碍(SI ) 作为重要 intraspecific 服务繁殖障碍支持快。在从 Solanaceae， Plantaginaceae 和 Rosaceae， S-RNase 和 SLF (S 地点 F 盒子) 蛋白质的种类被显示了分别地控制 SI 的女、男的特性。然而，很少除了它的保存 F 盒子领域对 SLF 蛋白质的结构特征被知道。这里，我们证明 SLF C 终端区域拥有结构在 SLF 蛋白质家庭之中保存了的一个新奇 ubiquitin 有约束力的领域(UBD ) 。由使用 Nicotiana benthamiana 的一个 ex vivo 系统，我们发现 UBD 调停由 ubiquitin–proteasome 小径的 SLF 蛋白质周转。而且，我们检测了 SLF 蛋白质直接涉及 S-RNase 降级。一起拿，我们的结果提供新奇卓见进 SLF 结构并且在 S-RNase-based 自我障碍加亮 SLF 蛋白质稳定性和降级的一个潜在的角色。

英文摘要：

In flowering plants, self-incompatibility （SI） serves as an important intraspecific reproductive barrier to promote outbreeding. In species from the Solanaceae, Plantaginaceae and Rosaceae, S-RNase and SLF （S-locus F-box） proteins have been shown to control the female and male specificity of SI, respectively. However, little is known about structure features of the SLF protein apart from its conserved F-box domain. Here we show that the SLF C-terminal region possesses a novel ubiquitin-binding domain （UBD） structure conserved among the SLF protein family. By using an ex vivo system of Nicotiana benthamiana, we found that the UBD mediates the SLF protein turnover by the ubiquitin-proteasome pathway. Furthermore, we detected that the SLF protein was directly involved in S-RNase degradation. Taken together, our results provide a novel insight into the SLF structure and highlight a potential role of SLF protein stability and degradation in S-RNase-based self-incompatibility.