Haq Fazal, Camuel Alicia, Carcagno Mélanie, Biondi Emanuele G, Pacquit Valérie, Deslandes Laurent, Giraud Eric, Mergaert Peter
Institute for Integrative Biology of the Cell (I2BC), Université Paris-Saclay, CEA, CNRS, 91198, Gif-sur-Yvette, France.
IRD, Laboratoire des Symbioses Tropicales et Méditerranéennes (LSTM), UMR IRD/Institut Agro/INRAE/Université de Montpellier/CIRAD, TA-A82/J Campus de Baillarguet, 34398, Montpellier cedex 5, France.
New Phytol. 2025 Aug;247(4):1826-1836. doi: 10.1111/nph.70334. Epub 2025 Jun 22.
Rhizobial type III effectors (T3Es) play a crucial role in the symbiotic relationship between rhizobia and legumes by manipulating host cellular processes to promote nodule formation. Previously, we identified two T3Es, ErnA and Sup3, that trigger nodulation in Aeschynomene spp. in the absence of Nod factors. Here, we further investigate the mode of action of these T3Es during root nodule symbiosis. We employed protein interaction assays, in vitro binding and enzymatic activity assays, mutational analyses, and functional nodulation tests to dissect the roles of ErnA and Sup3 and their interactions with the host Small Ubiquitin-like MOdifier (SUMO) pathway (SUMOylation). We demonstrate that ErnA contains a SUMO-interacting motif (SIM) at its C terminus, which promotes its interaction with SUMO proteins in vitro and in plant nuclei. Additionally, we show that Sup3 possesses a C-terminal SUMO protease domain, which not only interacts with SUMO proteins in vitro and in the nucleus but also exhibits SUMO protease activity. Deletion of the SIM in ErnA or mutation of the catalytic site in Sup3 abolished their ability to trigger nodulation in Aeschynomene indica. These findings suggest that type III secretion system-dependent symbiosis is regulated by posttranslational modification through SUMOylation and that ErnA and Sup3 modulate this SUMOylation pathway to trigger nodulation.
根瘤菌III型效应蛋白(T3Es)通过操纵宿主细胞过程促进根瘤形成,在根瘤菌与豆科植物的共生关系中发挥关键作用。此前,我们鉴定出两种T3Es,即ErnA和Sup3,它们在没有结瘤因子的情况下能触发合萌属植物结瘤。在此,我们进一步研究这些T3Es在根瘤共生过程中的作用方式。我们采用蛋白质相互作用分析、体外结合和酶活性分析、突变分析以及功能性结瘤测试,来剖析ErnA和Sup3的作用及其与宿主小泛素样修饰物(SUMO)途径(SUMO化)的相互作用。我们证明,ErnA在其C末端含有一个SUMO相互作用基序(SIM),该基序在体外和植物细胞核中促进其与SUMO蛋白的相互作用。此外,我们表明Sup3具有一个C末端SUMO蛋白酶结构域,该结构域不仅在体外和细胞核中与SUMO蛋白相互作用,还表现出SUMO蛋白酶活性。删除ErnA中的SIM或Sup3中催化位点的突变消除了它们在印度合萌中触发结瘤的能力。这些发现表明,III型分泌系统依赖性共生受SUMO化的翻译后修饰调控,并且ErnA和Sup3调节这种SUMO化途径以触发结瘤。