数字农科院2.0

Plant U-box E3 ligase PpPUB59 regulates anthocyanin accumulation by ubiquitinating PpBBX24 in 'Zaosu' pear and its red bud mutation

文献类型： 外文期刊

作者： Li, Shuran;Ou, Chunqing;Liu, Xiaofeng;Wang, Fei;Zhang, Yanjie;Qi, Liyong;Jiang, Shuling;Li, He

作者机构：

关键词： PpPUB59;Ubiquitination;Anthocyanin;Pear

期刊名称： PLANT PHYSIOLOGY AND BIOCHEMISTRY

ISSN： 0981-9428

年卷期： 2025 年 219 卷

页码：

收录情况： SCIE（2025版）

摘要： Ubiquitination is the specific modification of target proteins in cells by ubiquitin molecules, which is under the action of a series of special enzymes such as ubiquitin-activating enzymes, binding, and ligase enzymes. Ubiquitination plays an essential role in anthocyanin accumulation in plants. There are few studies on the coloring of pear peel by ubiquitin ligase E3. In this study, an E3 ubiquitin ligase protein PpPUB59 with seven WD40 repeats was cloned. And the function of PpPUB59 on the ubiquitination and protein stability of PpBBX24 and Ppbbx24del, and the possible action mechanism in the anthocyanin accumulation of 'Red Zaosu' was studied. Our results showed that the WD40 repeats were verified to be the key domain interacting with the VP domain of BBX protein. PpPUB59 could degrade PpBBX24 in vitro by interacting with the VP domain but could not degrade the mutant PpBBX24-del without the VP domain. Dual luciferase assay showed that Ppbbx24-del could activate the PpCHS promoter, while PpPUB59 did not interfere with this activation; PpBBX24 could not activate the promotor of PpCHS but could suppress the activation of PpHY5; when the PpPUB59 was co-expressed with PpBBX24 and PpHY5, the activation roles of PpHY5 in the promotor of PpCHS was not recovered. BiFC and yeast two-hybrid experiments showed that PpPUB59 could also interact with PpHY5, which may make it ubiquitinated and degraded by 26S proteasome. In conclusion, PpPUB59 played an essential role in pear anthocyanin accumulation by ubiquitinating the associated transcription factors. These findings clarified the mutant mechanism of the 'Red Zaosu' pear at the post-translational modification level and enriched the regulation theory of the pear anthocyanin accumulation.

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