Journal
MOLECULAR PLANT-MICROBE INTERACTIONS
Volume 23, Issue 12, Pages 1635-1642Publisher
AMER PHYTOPATHOLOGICAL SOC
DOI: 10.1094/MPMI-06-10-0136
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Funding
- National Research Initiative of the United States Department of Agriculture Co operative State Research Education and Extension Service [2007 35301 18205]
- National Institute of Food and Agriculture [2010 65108 20568]
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Stem rust threatens cereal production worldwide Understanding the mechanism by which durable resistance genes, such as Rpg1, function is critical We show that the RPG1 protein is phosphorylated within 5 nun by exposure to spores from avirulent but not virulent races of stem rust Transgenic mutants encoding an RPG1 protein with an in vitro inactive kinase domain fail to phosphorylate RPG1 in vivo and are susceptible to stem rust, demonstrating that phosphorylation is a prerequisite for disease resistance Protein kinase inhibitors prevent RPG1 phosphorylation and result in susceptibility to stem rust, providing further evidence for the importance of phosphorylation in disease resistance We conclude that phosphorylation of the RPG1 protein by the kinase activity of the pK2 domain Induced by the interaction with an unknown pathogen spore product is required for resistance to the avirulent stem rust races The pseudokinase pK1 domain is required for disease resistance but not phosphorylation The very rapid phosphorylation of RPG1 suggests that an effector is already present in or on the stem rust urediniospores when they are placed on the leaf surface However, spores must be alive, as determined by their ability to germinate, in order to elicit RPG1 phosphorylation
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