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Assay for Pathogen-Associated Molecular Pattern PAMP-Triggered Immunity PTI in Plants
Published on: September 9, 2009
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Ligand-triggered allosteric ADP release primes a plant NLR complex
Jizong Wang1,2, Jia Wang2, Meijuan Hu1
1State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Academy of Seed Design, Chinese Academy of Sciences, 100101 Beijing, China.
Science (New York, N.Y.)
|April 6, 2019
Summary
Plant NLR immune receptors like ZAR1 are activated by pathogen effectors. Structural studies reveal how PBL2UMP binding to RKS1 stabilizes ZAR1, blocking ADP binding and initiating plant defense.
Area of Science:
- Plant immunity
- Molecular mechanisms of plant defense
- Structural biology
Background:
- Nucleotide-binding (NB), leucine-rich repeat (LRR) receptors (NLRs) are crucial for plant immune responses.
- The Xanthomonas campestris effector AvrAC modifies the Arabidopsis PBL2 kinase to PBL2UMP, which activates the ZAR1 NLR receptor.
Purpose of the Study:
- To determine the cryo-electron microscopy structures of ZAR1-RKS1 and ZAR1-RKS1-PBL2UMP.
- To elucidate the structural basis of ZAR1 activation by PBL2UMP.
Main Methods:
- Cryo-electron microscopy (cryo-EM)
- Structural analysis of protein complexes
Main Results:
- Determined structures of ZAR1-RKS1 (inactive) and ZAR1-RKS1-PBL2UMP (intermediate state).
- The ZAR1 LRR domain adopts a unique conformation in plants, sequestering ZAR1 in an inactive state.
- RKS1 mediates PBL2UMP recognition, stabilizing the RKS1 activation segment and blocking ZAR1 ADP binding.
- PBL2UMP binding induces flexibility in the ZAR1 NB domain.
Conclusions:
- The ZAR1-RKS1-PBL2UMP structure provides a template for understanding plant NLR activation.
- Structural insights into ZAR1 function advance our knowledge of plant immune signaling pathways.
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