Journal
SCIENCE
Volume 301, Issue 5637, Pages 1230-1233Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1085671
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- NIDDK NIH HHS [DK18849] Funding Source: Medline
- NIGMS NIH HHS [GM46451] Funding Source: Medline
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Plant disease-resistance (R) proteins are thought to function as receptors for ligands produced directly or indirectly by pathogen avirulence (Avr) proteins. The biochemical functions of most Avr proteins are unknown, and the mechanisms by which they activate R proteins have not been determined. In Arabidopsis, resistance to Pseudomonas syringae strains expressing AvrPphB requires RPS5, a member of the class of R proteins that have a predicted nucleotide-binding site and leucine-rich repeats, and PBS1, a protein kinase. AvrPphB was found to proteolytically cleave PBS1, and this cleavage was required for RPS5-mediated resistance, which indicates that AvrPphB is detected indirectly via its enzymatic activity.
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