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Cleavage of Arabidopsis PBS1 by a Bacterial Type III Effector
Feng Shao,1*
Catherine Golstein,2*
Jules Ade,2*
Mark Stoutemyer,2
Jack E. Dixon,1
Roger W. Innes2
Abstract:
Plant disease-resistance (R) proteins are thought to functionas receptors for ligands produced directly or indirectly bypathogen avirulence (Avr) proteins. The biochemical functionsof most Avr proteins are unknown, and the mechanisms by whichthey activate R proteins have not been determined. In Arabidopsis,resistance to Pseudomonas syringae strains expressing AvrPphBrequires RPS5, a member of the class of R proteins that havea predicted nucleotide-binding site and leucine-rich repeats,and PBS1, a protein kinase. AvrPphB was found to proteolyticallycleave PBS1, and this cleavage was required for RPS5-mediatedresistance, which indicates that AvrPphB is detected indirectlyvia its enzymatic activity.
1 Department of Biological Chemistry, Medical School and Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA. 2 Department of Biology, Indiana University, Bloomington, IN 47405, USA.
Present address: Departments of Pharmacology, Cellular and MolecularMedicine, School of Medicine, and Department of Chemistry andBiochemistry, University of California, San Diego, La Jolla,CA 92093, USA.
To whom correspondence should be addressed. E-mail: rinnes{at}indiana.edu
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