Chin Bull Bot ›› 2019, Vol. 54 ›› Issue (3): 288-292.doi: 10.11983/CBB19035

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Open a Door of Defenses: Plant Resistosome

Xia Shitou1,*(),Li Xin2,*()   

  1. 1. Hunan Provincial Key Laboratory of Phytohormones, College of Bioscience and Biotechnology, Hunan Agricultural University, Changsha 410128, China
    2. Michael Smith Laboratories,Department of Botany, University Columbia,Vancouver, BC, V6T 1Z4,Canada
  • Received:2019-02-23 Accepted:2019-04-03 Online:2019-05-20 Published:2019-05-01
  • Contact: Xia Shitou,Li Xin E-mail:xstone0505@163.com;xinli@msl.ubc.ca

Abstract:

Nucleotide binding, leucine-rich repeat (NLR) immune receptors are a major family of plant resistance (R) proteins, which are also found in animals. NLRs turn on immune signaling by recognizing pathogen-specific effectors in plants. Although the first few plant NLR R genes were cloned more than 25 years ago, the activation mechanism remained elusive. No structure is available for the full-length plant NLRs despite attempts over the last 2 decades. Recently, studies from the Chai, Zhou and Wang labs, published in Science, solved the structure of zygote arrest 1 (ZAR1) before and after effector recognition, which fills a huge gap in NLR biology. This mini review briefly summarized these findings and related progresses, and highlighted further challenges in NLR-mediated immune signaling field.

Key words: plant immunity, NLR, ZAR1, allosteric activation, resistosome

Figure 1

PBL2UMP-induced activation and assembly of the ZAR1 resistosome Arabidopsis PBL2 is modified by uridylyl transferase AvrAC, which is an effector protein from Xanthomonas campestris. The uridylylated PBL2 (PBL2UMP) as a ligand is then recruited by the ZAR1-RKS1 complex through interaction with the pseudokinase RKS1. The activation segment of RKS1 becomes stabilized (orange surface) after interacting with the two uridylyl moieties (in sphere) of PBL2UMP, and sterically clashes with ZAR1NBD, causing the latter to rotate outward and consequently release ADP, forming an intermediate ZAR1-RKS1-PBL2UMP complex which allows it to bind dATP/ATP. Binding of dATP/ATP induces structural remodeling and fold switching of ZAR1. The very N-terminal helix (α1, red) of ZAR1 buried in the inactive ZAR1-RKS1 complex becomes solvent-exposed in the activated ZAR1-RKS1-PBL2UMP complex, forming a ZAR1 resistosome pentameric structure through polymerization (a funnel-shaped structure highlighted within the purple frame). CC, NBD, HD1, WHD and LRR are different structural domains of ZAR1."

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