Zhang Xue, Ménard Rozenn, Li Ying, Coruzzi Gloria M, Heitz Thierry, Shen Wen-Hui, Berr Alexandre
Institut de Biologie Moléculaire des Plantes du CNRS, Université de Strasbourg, Strasbourg, France.
Department of Horticulture and Landscape Architecture, Purdue University, West Lafayette, IN, United States.
Front Plant Sci. 2020 Mar 11;11:277. doi: 10.3389/fpls.2020.00277. eCollection 2020.
Post-translational covalent modifications of histones play important roles in modulating chromatin structure and are involved in the control of multiple developmental processes in plants. Here we provide insight into the contribution of the histone lysine methyltransferase SET DOMAIN GROUP 8 (SDG8), implicated in histone H3 lysine 36 trimethylation (H3K36me3), in connection with RNA polymerase II (RNAPII) to enhance immunity. We showed that even if the loss-of-function mutant, defective in H3K36 methylation, displayed a higher sensitivity to different strains of the bacterial pathogen , effector-triggered immunity (ETI) still operated, but less efficiently than in the wild-type (WT) plants. In , the level of the plant defense hormone salicylic acid (SA) was abnormally high under resting conditions and was accumulated similarly to WT at the early stage of pathogen infection but quickly dropped down at later stages. Concomitantly, the transcription of several defense-related genes along the SA signaling pathway was inefficiently induced in the mutant. Remarkably, albeit the defense genes () and have retained responsiveness to exogenous SA, their inductions fade more rapidly in than in WT. At chromatin, while global levels of histone methylations were found to be stable, local increases of H3K4 and H3K36 methylations as well as RNAPII loading were observed at some defense genes following SA-treatments in WT. In , the H3K36me3 increase was largely attenuated and also the increases of H3K4me3 and RNAPII were frequently compromised. Lastly, we demonstrated that SDG8 could physically interact with the RNAPII C-terminal Domain, providing a possible link between RNAPII loading and H3K36me3 deposition. Collectively, our results indicate that SDG8, through its histone methyltransferase activity and its physical coupling with RNAPII, participates in the strong transcriptional induction of some defense-related genes, in particular and , to potentiate sustainable immunity during plant defense response to bacterial pathogen.
组蛋白的翻译后共价修饰在调节染色质结构中发挥重要作用,并参与植物多个发育过程的调控。在此,我们深入探讨了组蛋白赖氨酸甲基转移酶SET结构域蛋白8(SDG8)在组蛋白H3赖氨酸36三甲基化(H3K36me3)方面的作用,以及其与RNA聚合酶II(RNAPII)协同作用增强植物免疫的机制。我们发现,尽管H3K36甲基化功能缺失的突变体对不同菌株的细菌病原体表现出更高的敏感性,但效应子触发免疫(ETI)仍能发挥作用,不过其效率低于野生型(WT)植物。在突变体中,植物防御激素水杨酸(SA)在静息条件下水平异常高,在病原体感染早期与WT植物中SA的积累情况相似,但在后期迅速下降。与此同时,突变体中沿SA信号通路的几个防御相关基因的转录诱导效率低下。值得注意的是,尽管防御基因()和对外源SA仍有反应,但其诱导在突变体中比在WT植物中更快消失。在染色质水平上,虽然发现组蛋白甲基化的整体水平是稳定的,但在WT植物中,经SA处理后,一些防御基因处观察到H3K4和H3K36甲基化以及RNAPII负载的局部增加。在突变体中,H3K36me3的增加在很大程度上减弱,H3K4me3和RNAPII的增加也经常受到影响。最后,我们证明SDG8可以与RNAPII的C末端结构域发生物理相互作用,这为RNAPII负载与H3K36me3沉积之间提供了一种可能的联系。总的来说,我们的结果表明,SDG8通过其组蛋白甲基转移酶活性以及与RNAPII的物理结合,参与了一些防御相关基因(特别是和)的强烈转录诱导,从而在植物对细菌病原体的防御反应中增强可持续免疫。