The changing of the guard: the Pto/Prf receptor complex of tomato and pathogen recognition.
One important model for disease resistance is the Prf recognition complex of tomato, which responds to different bacterial effectors. Prf incorporates a protein kinase called Pto as its recognition domain that mimics effector virulence targets, and activates resistance after interaction with specific effectors. Recent findings show that this complex is oligomeric, and reveal how this impacts mechanism. Oligomerisation brings two or more kinases into proximity, where they can phosphorylate each other after effector perception. Effector attack on one kinase activates another in trans, constituting a molecular trap for the effector. Oligomerisation of plant resistance proteins may be a general concept that broadens pathogen recognition and restricts the ability of pathogens to evolve virulence.
School of Life Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom.
Vardis
V
Ntoukakis
Research School of Biology, The Australian National University, Acton 0200, Australian Capital Territory, Australia.
Isabel M L
IM
Saur
Research School of Biology, The Australian National University, Acton 0200, Australian Capital Territory, Australia.
Brendon
B
Conlan
Research School of Biology, The Australian National University, Acton 0200, Australian Capital Territory, Australia. Electronic address: john.rathjen@anu.edu.au.
John P
JP
Rathjen
D018551:Solanum lycopersicum / Q000235:genetics* / Q000276:immunology* / Q000378:metabolism; D057865:Plant Immunity; D010940:Plant Proteins / Q000235:genetics* / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000235:genetics* / Q000378:metabolism
D010940:Plant Proteins; C120613:Prf protein, Lycopersicon esculentum; C084354:Pto protein, Lycopersicon; D017346:Protein Serine-Threonine Kinases