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Phosphorylation-Regulated Activation of the Arabidopsis RRS1-R/RPS4 Immune Receptor Complex Reveals Two Distinct Effector Recognition Mechanisms.
Cell Host & Microbe ( IF 30.3 ) Pub Date : 2020-03-31 , DOI: 10.1016/j.chom.2020.03.008
Hailong Guo 1 , Hee-Kyung Ahn 1 , Jan Sklenar 1 , Jianhua Huang 1 , Yan Ma 1 , Pingtao Ding 1 , Frank L H Menke 1 , Jonathan D G Jones 1
Affiliation  

The Arabidopsis immune receptors RPS4 and RRS1 interact to co-confer responsiveness to bacterial effectors. The RRS1-R allele, with RPS4, responds to AvrRps4 and PopP2, whereas RRS1-S responds only to AvrRps4. Here, we show that the C terminus of RRS1-R but not RRS1-S is phosphorylated. Phosphorylation at Thr1214 in the WRKY domain maintains RRS1-R in its inactive state and also inhibits acetylation of RRS1-R by PopP2. PopP2 in turn catalyzes O-acetylation at the same site, thereby preventing its phosphorylation. Phosphorylation at other sites is required for PopP2 but not AvrRps4 responsiveness and facilitates the interaction of RRS1's C terminus with its TIR domain. Derepression of RRS1-R or RRS1-S involves effector-triggered proximity between their TIR domain and C termini. This effector-promoted interaction between these domains relieves inhibition of TIRRPS4 by TIRRRS1. Our data reveal effector-triggered and phosphorylation-regulated conformational changes within RRS1 that results in distinct modes of derepression of the complex by PopP2 and AvrRps4.

中文翻译:

拟南芥 RRS1-R/RPS4 免疫受体复合物的磷酸化调节激活揭示了两种不同的效应子识别机制。

拟南芥免疫受体 RPS4 和 RRS1 相互作用共同赋予对细菌效应物的反应性。带有 RPS4 的 RRS1-R 等位基因对 AvrRps4 和 PopP2 有反应,而 RRS1-S 仅对 AvrRps4 有反应。在这里,我们显示 RRS1-R 而不是 RRS1-S 的 C 末端被磷酸化。WRKY 结构域中 Thr1214 的磷酸化使 RRS1-R 保持在其非活性状态,并且还抑制 PopP2 对 RRS1-R 的乙酰化。PopP2 反过来在同一位点催化 O-乙酰化,从而防止其磷酸化。PopP2 需要其他位点的磷酸化,而不是 AvrRps4 响应性,并促进 RRS1 的 C 末端与其 TIR 结构域的相互作用。RRS1-R 或 RRS1-S 的去抑制涉及其 TIR 域和 C 末端之间的效应器触发接近。这些结构域之间的这种效应子促进的相互作用减轻了 TIRRRS1 对 TIRRPS4 的抑制。我们的数据揭示了 RRS1 内由效应器触发和磷酸化调节的构象变化,导致 PopP2 和 AvrRps4 对复合物的不同抑制模式。
更新日期:2020-03-31
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