Nucleotide-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.
Nucleotide-binding, Leucine-rich Repeat Receptors Pathogen Effector Direct Recognition Leucine-rich Repeat Receptors Leucine-rich Repeat Recognition Mechanism Subsequent Response Direct Activation Cryo Electron Microscopy Structure Plasma Membrane Association
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Round-ups are the summaries of handpicked papers around trending topics published every week. These would enable you to scan through a collection of papers and decide if the paper is relevant to you before actually investing time into reading it.
Climate change Research Articles published between Nov 21, 2022 to Nov 27, 2022
Nov 28, 2022
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No potential conflict of interest was reported by the authors. The conception and design of the study, acquisition of data, analysis and interpretatio...Read More
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