在豆类结节过程中,通过RING型E3酶的酸化介导功能开关来动态调节结节因子受体水平
Hao Li1, Yajuan Ou1, Jidan Zhang1
1National Key Lab of Agricultural Microbiology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan 430070, China.
Molecular plant
|June 1, 2024
概括
一种新的E3连接酶,NIRE1,调节了日本莲花的结节因子受体 (NFR) 水平. 酸化开关 NIRE1 的 NIRE1 的
科学领域:
- 植物分子生物学 植物分子生物学
- 共生相互作用的共生相互作用.
- E3 无处不在合酶的功能
背景情况:
- 精确控制细胞信号受体水平对于生物反应至关重要.
- 在共生过程中调节结结因子 (NF) 受体 (NFR) 水平的机制尚未完全理解.
- 豆类中的树生物共生是由NF感知介导的,需要调节NFR活动.
研究的目的:
- 为了研究NIRE1在调节NFR1/NFR5在日本莲花的恒温中的作用.
- 阐明NIRE1在根茎菌感染期间控制NFR蛋白水平的机制.
- 了解NIRE1的酸化状态对共生发展的影响.
主要方法:
- 酵母两杂交测定以确认蛋白质与蛋白质的相互作用.
- 活化试验 (体外和植物内) 用于确定多活化类型.
- 突变性研究 (死和模仿突变) 评估功能意义.
- 转基因莲花japonicus线的表型分析.
主要成果:
- 在接种之前,NIRE1与NFR1和NFR5相互作用,通过K48链接的多基化介导它们的降解.
- 在Tyr-109中NIRE1的NFR1-介导酸化将其功能切换为通过K63链接的多基化后注射稳定NFR1/NFR5.
- 死亡的NIRE1 (Y109F) 突变导致结节发育延迟,而模仿的NIRE1 (Y109E) 诱导自发结节.
结论:
- 在根茎生物共生过程中,NIRE1充当了NFR蛋白稳定性的关键调节者.
- 在NIRE1中,一个依赖酸化的功能开关动态控制NFR水平,优化共生信号传输.
- 这种机制突显出一种复杂的宿主-微生物相互作用,涉及到精确的E3酶调节.
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