PUB25和PUB26通过在Arabidopsis的寒冷应激过程中通过差异性泛化动态调节ICE1的稳定性
Xi Wang1, Xiaoyan Zhang1, Chun-Peng Song2
1State Key Laboratory of Plant Environmental Resilience, Frontiers Science Center for Molecular Design Breeding, College of Biological Sciences, China Agricultural University, Beijing 100193, China.
The Plant cell
|June 6, 2023
概括
植物E3连接酶PUB25和PUB26通过将不同的乌比基链连接到ICE1和MYB15上,动态调节植物的冷应激反应,调节它们的稳定性和活性.
科学领域:
- 植物分子生物学 植物分子生物学
- 植物应激生理学 植物应激生理学
- 乌比基的信号传递方式
背景情况:
- 乌比奎化,即乌比奎 (Ub) 部分的附着,调节了蛋白质的稳定性和活性.
- 氨酸48 (K48) 连接的聚比奎丁链通常针对蛋白质进行蛋白质体降解,而其他链接,如K63,则起着调节作用.
- 植物的冷应激反应涉及复杂的调节网络,控制基因表达和蛋白质功能.
研究的目的:
- 调查植物U-BOX E3链酶 (PUB25和PUB26) 在冷应力期间调节关键转录调节者的稳定性和活性方面的作用.
- 阐明在ICE1和MYB15.5上由PUB25和PUB26介导的特定类型的无处不在 (K48和K63链接).
- 了解PUB25和PUB26对ICE1和MYB15的差异性无处不在如何影响下游冷反应基因表达.
主要方法:
- 在寒冷压力条件下,对 Arabidopsis thaliana 中的 ICE1 和 MYB15 无处不在模式的分析.
- 生物化学测试以确定ICE1和MYB15之间的相互作用及其DNA结合活动.
- 对PUB25和PUB26表达的基因操纵,以评估它们对寒冷耐受性的影响.
主要成果:
- 在冷应激的不同阶段,PUB25和PUB26促进了ICE1和MYB15的K48和K63结合的无处不在.
- ICE1和MYB15的PUB25和PUB26的无处不在模式是不同的,导致它们的蛋白质稳定性和丰度的差异调制.
- ICE1直接与MYB15的DNA结合活性相互作用并抑制它,这对于调节CBF表达至关重要.
结论:
- PUB25和PUB26通过差异性无处不在作用来动态控制ICE1和MYB15的稳定性和功能,作为植物冷应激反应的关键调节者.
- 由PUB25和PUB26介导的独特的无处不在事件微调了植物对寒冷应激反应的时间和程度.
- 这项研究揭示了一种涉及E3链酶和植物寒冷适应过程中的差异性泛化的一种新机制.
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