Structural highlights
FunctionPublication Abstract from PubMedNucleotide-binding, leucine-rich repeat receptors (NLRs) perceive pathogen effectors to trigger plant immunity. The direct recognition mechanism of pathogen effectors by coiled-coil NLRs (CNLs) remains unclear. We demonstrate that the Triticum monococcum CNL Sr35 directly recognizes the pathogen effector AvrSr35 from Puccinia graminis f. sp. tritici and report a cryo-electron microscopy structure of Sr35 resistosome and a crystal structure of AvrSr35. We show that AvrSr35 forms homodimers that are disassociated into monomers upon direct recognition by the leucine-rich repeat domain of Sr35, which induces Sr35 resistosome assembly and the subsequent immune response. The first 20 amino-terminal residues of Sr35 are indispensable for immune signaling but not for plasma membrane association. Our findings reveal the direct recognition and activation mechanism of a plant CNL and provide insights into biochemical function of Sr35 resistosome. Pathogen effector AvrSr35 triggers Sr35 resistosome assembly via a direct recognition mechanism.,Zhao YB, Liu MX, Chen TT, Ma X, Li ZK, Zheng Z, Zheng SR, Chen L, Li YZ, Tang LR, Chen Q, Wang P, Ouyang S Sci Adv. 2022 Sep 9;8(36):eabq5108. doi: 10.1126/sciadv.abq5108. Epub 2022 Sep 9. PMID:36083908[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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