AI Article Synopsis

  • Plants use innate immunity to fight off diseases caused by pathogens, specifically through NLR proteins like AtZAR1 that recognize certain bacterial effector proteins (T3SEs), such as HopZ1a.
  • The T3SE HopZ1a interacts with the plant protein AtZED1, triggering a defense response mediated by AtZAR1, although the exact molecular processes behind this immunity are not fully understood.
  • Researchers developed a transient expression system to explore the interactions between HopZ1a, AtZED1, and AtZAR1, revealing critical domains and residues in these proteins that contribute to immune responses, highlighting the role of the coiled-coil domain in activating immunity.

Article Abstract

Plants depend on innate immunity to prevent disease. Plant pathogenic bacteria, like and , use the type III secretion system as a molecular syringe to inject type III secreted effector (T3SE) proteins in plants. The primary function of most T3SEs is to suppress immunity; however, the plant can evolve nucleotide-binding domain-leucine-rich repeat domain-containing proteins to recognize specific T3SEs. The AtZAR1 NLR induces strong defense responses against and The T3SE HopZ1a is an acetyltransferase that acetylates the pseudokinase AtZED1 and triggers recognition by AtZAR1. However, little is known about the molecular mechanisms that lead to AtZAR1-induced immunity in response to HopZ1a. We established a transient expression system in to study detailed interactions among HopZ1a, AtZED1, and AtZAR1. We show that the AtZAR1 immune pathway is conserved in and identify AtZAR1 domains, and residues in AtZAR1 and AtZED1, that are important for immunity and protein-protein interactions in planta and in yeast (). We show that the coiled-coil domain of AtZAR1 oligomerizes, and this domain acts as a signal to induce immunity. This detailed analysis of the AtZAR1-AtZED1 protein complex provides a better understanding of the immune signaling hub controlled by AtZAR1.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5543953PMC
http://dx.doi.org/10.1104/pp.17.00441DOI Listing

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