A Bacterial Tyrosine Phosphatase Inhibits Plant Pattern Recognition Receptor Activation

作者：Macho Alberto P; Schwessinger Benjamin; Ntoukakis Vardis; Brutus Alexandre; Segonzac Cecile; Roy Sonali; Kadota Yasuhiro; Oh Man Ho; Sklenar Jan; Derbyshire Paul; Lozano Duran Rosa; Malinovsky Frederikke Gro; Monaghan Jacqueline; Menke Frank L; Huber Steven C; He Sheng Yang; Zipfel Cyril^*

来源：Science, 2014, 343(6178): 1509-1512.

DOI：10.1126/science.1248849

Innate immunity relies on the perception of pathogen-associated molecular patterns (PAMPs) by pattern-recognition receptors (PRRs) located on the host cell%26apos;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.

• 出版日期2014-3-28