A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation

Macho, Alberto P, Schwessinger, Benjamin, Ntoukakis, Vardis, Brutus, Alexandre, Segonzac, Cécile, Roy, Sonali, Kadota, Yasuhiro, Oh, Man-Ho, Sklenar, Jan, Derbyshire, Paul, Lozano-Durán, Rosa, Malinovsky, Frederikke Gro, Monaghan, Jacqueline, Menke, Frank L ORCID: https://orcid.org/0000-0003-2490-4824, Huber, Steven C, He, Sheng Yang and Zipfel, Cyril (2014) A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation. Science, 343 (6178). pp. 1509-1512. ISSN 0036-8075

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Innate immunity relies on the perception of pathogen-associated molecular patterns (PAMPs) by pattern-recognition receptors (PRRs) located on the host cell's surface. Many plant PRRs are kinases. Here, we report that the Arabidopsis receptor kinase EF-TU RECEPTOR (EFR), which perceives the elf18 peptide derived from bacterial elongation factor Tu, is activated upon ligand binding by phosphorylation on its tyrosine residues. Phosphorylation of a single tyrosine residue, Y836, is required for activation of EFR and downstream immunity to the phytopathogenic bacterium Pseudomonas syringae. A tyrosine phosphatase, HopAO1, secreted by P. syringae, reduces EFR phosphorylation and prevents subsequent immune responses. Thus, host and pathogen compete to take control of PRR tyrosine phosphorylation used to initiate antibacterial immunity.

Item Type: Article
Uncontrolled Keywords: arabidopsis,arabidopsis proteins,bacterial proteins,peptide elongation factor tu,peptides,phosphorylation,protein tyrosine phosphatases,pseudomonas syringae,receptors, pattern recognition,tyrosine
Faculty \ School: Faculty of Science > School of Biological Sciences
Faculty of Science > The Sainsbury Laboratory
UEA Research Groups: Faculty of Science > Research Groups > Plant Sciences
Depositing User: Pure Connector
Date Deposited: 04 Jul 2014 12:42
Last Modified: 24 Oct 2022 06:24
URI: https://ueaeprints.uea.ac.uk/id/eprint/48856
DOI: 10.1126/science.1248849

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