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A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation.

Publication ,  Journal Article
Macho, AP; Schwessinger, B; Ntoukakis, V; Brutus, A; Segonzac, C; Roy, S; Kadota, Y; Oh, M-H; Sklenar, J; Derbyshire, P; Lozano-Durán, R ...
Published in: Science (New York, N.Y.)
March 2014

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.

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Published In

Science (New York, N.Y.)

DOI

EISSN

1095-9203

ISSN

0036-8075

Publication Date

March 2014

Volume

343

Issue

6178

Start / End Page

1509 / 1512

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
 

Citation

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Macho, A. P., Schwessinger, B., Ntoukakis, V., Brutus, A., Segonzac, C., Roy, S., … Zipfel, C. (2014). A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation. Science (New York, N.Y.), 343(6178), 1509–1512. https://doi.org/10.1126/science.1248849
Macho, Alberto P., Benjamin Schwessinger, Vardis Ntoukakis, Alexandre Brutus, Cécile Segonzac, Sonali Roy, Yasuhiro Kadota, et al. “A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation.Science (New York, N.Y.) 343, no. 6178 (March 2014): 1509–12. https://doi.org/10.1126/science.1248849.
Macho AP, Schwessinger B, Ntoukakis V, Brutus A, Segonzac C, Roy S, et al. A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation. Science (New York, NY). 2014 Mar;343(6178):1509–12.
Macho, Alberto P., et al. “A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation.Science (New York, N.Y.), vol. 343, no. 6178, Mar. 2014, pp. 1509–12. Epmc, doi:10.1126/science.1248849.
Macho AP, Schwessinger B, Ntoukakis V, Brutus A, Segonzac C, Roy S, Kadota Y, Oh M-H, Sklenar J, Derbyshire P, Lozano-Durán R, Malinovsky FG, Monaghan J, Menke FL, Huber SC, He SY, Zipfel C. A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation. Science (New York, NY). 2014 Mar;343(6178):1509–1512.
Journal cover image

Published In

Science (New York, N.Y.)

DOI

EISSN

1095-9203

ISSN

0036-8075

Publication Date

March 2014

Volume

343

Issue

6178

Start / End Page

1509 / 1512

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