A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation.
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.
Duke Scholars
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- Tyrosine
- Receptors, Pattern Recognition
- Pseudomonas syringae
- Protein Tyrosine Phosphatases
- Phosphorylation
- Peptides
- Peptide Elongation Factor Tu
- General Science & Technology
- Bacterial Proteins
- Arabidopsis Proteins
Citation
Published In
DOI
EISSN
ISSN
Publication Date
Volume
Issue
Start / End Page
Related Subject Headings
- Tyrosine
- Receptors, Pattern Recognition
- Pseudomonas syringae
- Protein Tyrosine Phosphatases
- Phosphorylation
- Peptides
- Peptide Elongation Factor Tu
- General Science & Technology
- Bacterial Proteins
- Arabidopsis Proteins