Cavity surface residues of PAD4 and SAG101 contribute to EDS1 dimer signaling specificity in plant immunity.

Autor: Dongus JA; Department of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829, Cologne, Germany.; Laboratory of Plant Physiology, Wageningen University, Droevendaalsesteeg 1, 6700, AA Wageningen, The Netherlands., Bhandari DD; Department of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829, Cologne, Germany.; Plant Research Laboratory, Michigan State University, 612, Wilson Road, East Lansing, Michigan, 48824, USA., Penner E; Department of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829, Cologne, Germany., Lapin D; Department of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829, Cologne, Germany.; Plant-Microbe Interactions, Utrecht University, Padualaan 8, 3584, CH Utrecht, The Netherlands., Stolze SC; Protein Mass Spectrometry, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829, Cologne, Germany., Harzen A; Protein Mass Spectrometry, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829, Cologne, Germany., Patel M; Department of Biological Sciences and BioDiscovery Institute, University of North Texas, 1511 West Sycamore, Denton, 76201, Texas, USA., Archer L; Department of Biological Sciences and BioDiscovery Institute, University of North Texas, 1511 West Sycamore, Denton, 76201, Texas, USA., Dijkgraaf L; Department of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829, Cologne, Germany.; Plant-Microbe Interactions, Utrecht University, Padualaan 8, 3584, CH Utrecht, The Netherlands., Shah J; Department of Biological Sciences and BioDiscovery Institute, University of North Texas, 1511 West Sycamore, Denton, 76201, Texas, USA., Nakagami H; Protein Mass Spectrometry, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829, Cologne, Germany., Parker JE; Department of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linné-Weg 10, 50829, Cologne, Germany.; Cologne-Düsseldorf Cluster of Excellence on Plant Sciences (CEPLAS), 40225, Düsseldorf, Germany.
Jazyk: angličtina
Zdroj: The Plant journal : for cell and molecular biology [Plant J] 2022 Jun; Vol. 110 (5), pp. 1415-1432. Date of Electronic Publication: 2022 Apr 12.
DOI: 10.1111/tpj.15747
Abstrakt: Arabidopsis pathogen effector-triggered immunity (ETI) is controlled by a family of three lipase-like proteins (EDS1, PAD4, and SAG101) and two subfamilies of HET-S/LOB-B (HeLo)-domain "helper" nucleotide-binding/leucine-rich repeats (ADR1s and NRG1s). EDS1-PAD4 dimers cooperate with ADR1s, and EDS1-SAG101 dimers with NRG1s, in two separate defense-promoting modules. EDS1-PAD4-ADR1 and EDS1-SAG101-NRG1 complexes were detected in immune-activated leaf extracts but the molecular determinants for specific complex formation and function remain unknown. EDS1 signaling is mediated by a C-terminal EP domain (EPD) surface surrounding a cavity formed by the heterodimer. Here we investigated whether the EPDs of PAD4 and SAG101 contribute to EDS1 dimer functions. Using a structure-guided approach, we undertook a comprehensive mutational analysis of Arabidopsis PAD4. We identify two conserved residues (Arg314 and Lys380) lining the PAD4 EPD cavity that are essential for EDS1-PAD4-mediated pathogen resistance, but are dispensable for the PAD4-mediated restriction of green peach aphid infestation. Positionally equivalent Met304 and Arg373 at the SAG101 EPD cavity are required for EDS1-SAG101 promotion of ETI-related cell death. In a PAD4 and SAG101 interactome analysis of ETI-activated tissues, PAD4 R314A and SAG101 M304R EPD variants maintain interaction with EDS1 but lose association, respectively, with helper nucleotide-binding/leucine-rich repeats ADR1-L1 and NRG1.1, and other immune-related proteins. Our data reveal a fundamental contribution of similar but non-identical PAD4 and SAG101 EPD surfaces to specific EDS1 dimer protein interactions and pathogen immunity.
(© 2022 The Authors. The Plant Journal published by Society for Experimental Biology and John Wiley & Sons Ltd.)
Databáze: MEDLINE
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