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A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation

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Macho, A. P., Schwessinger, B., Ntoukakis, Vardis, Brutus, A., Segonzac, C., Roy, S., Kadota, Y., Oh, M. -H., Sklenar, J., Derbyshire, P., Lozano-Duran, R., Malinovsky, F. G., Monaghan, J., Menke, F. L., Huber, S. C., He, S. Y. and Zipfel, C. (2014) A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation. Science, Volume 343 (Number 6178). pp. 1509-1512. doi:10.1126/science.1248849 ISSN 0036-8075.

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Official URL: http://dx.doi.org/10.1126/science.1248849

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Abstract

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: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Journal or Publication Title: Science
Publisher: American Association for the Advancement of Science
ISSN: 0036-8075
Official Date: 28 March 2014
Dates:
DateEvent
28 March 2014Published
13 March 2014Available
28 February 2014Accepted
22 November 2013Submitted
Volume: Volume 343
Number: Number 6178
Page Range: pp. 1509-1512
DOI: 10.1126/science.1248849
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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