title: Cleavage of Arabidopsis PBS1 by a bacterial type III effector.
abstract: 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.
authors.affiliation: Department of Biological Chemistry, Medical School and Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.
authors.forename: Feng
authors.initials: F
authors.lastname: Shao
authors.forename: Catherine
authors.initials: C
authors.lastname: Golstein
authors.forename: Jules
authors.initials: J
authors.lastname: Ade
authors.forename: Mark
authors.initials: M
authors.lastname: Stoutemyer
authors.forename: Jack E
authors.initials: JE
authors.lastname: Dixon
authors.forename: Roger W
authors.initials: RW
authors.lastname: Innes
mesh_terms: D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D002460:Cell Line; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D017343:Genes, Plant; D005816:Genetic Complementation Test; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D008954:Models, Biological; D008969:Molecular Sequence Data; D009154:Mutation; D010766:Phosphorylation; D010935:Plant Diseases / Q000382:microbiology*; D010936:Plant Extracts / Q000378:metabolism; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism; D030821:Plants, Genetically Modified; D011233:Precipitin Tests; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011549:Pseudomonas / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D014026:Nicotiana / Q000235:genetics / Q000378:metabolism; D014170:Transformation, Genetic
chemical_list: D029681:Arabidopsis Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D047908:Intracellular Signaling Peptides and Proteins; C499581:PBS2 protein, Arabidopsis; D010936:Plant Extracts; D010940:Plant Proteins; C465630:RPS5 protein, Arabidopsis; D011994:Recombinant Proteins; C477340:PBS1 protein, Arabidopsis; D017346:Protein Serine-Threonine Kinases; D003546:Cysteine Endopeptidases