title: The Pseudomonas syringae type III effector AvrRpt2 promotes pathogen virulence via stimulating Arabidopsis auxin/indole acetic acid protein turnover.
abstract: To accomplish successful infection, pathogens deploy complex strategies to interfere with host defense systems and subvert host physiology to favor pathogen survival and multiplication. Modulation of plant auxin physiology and signaling is emerging as a common virulence strategy for phytobacteria to cause diseases. However, the underlying mechanisms remain largely elusive. We have previously shown that the Pseudomonas syringae type III effector AvrRpt2 alters Arabidopsis (Arabidopsis thaliana) auxin physiology. Here, we report that AvrRpt2 promotes auxin response by stimulating the turnover of auxin/indole acetic acid (Aux/IAA) proteins, the key negative regulators in auxin signaling. AvrRpt2 acts additively with auxin to stimulate Aux/IAA turnover, suggesting distinct, yet proteasome-dependent, mechanisms operated by AvrRpt2 and auxin to control Aux/IAA stability. Cysteine protease activity is required for AvrRpt2-stimulated auxin signaling and Aux/IAA degradation. Importantly, transgenic plants expressing the dominant axr2-1 mutation recalcitrant to AvrRpt2-mediated degradation ameliorated the virulence functions of AvrRpt2 but did not alter the avirulent function mediated by the corresponding RPS2 resistance protein. Thus, promoting auxin response via modulating the stability of the key transcription repressors Aux/IAA is a mechanism used by the bacterial type III effector AvrRpt2 to promote pathogenicity.
authors: Department of Plant Pathology, China Agricultural University, Beijing 100193, China.
authors: Fuhao
authors: F
authors: Cui
authors: Shujing
authors: S
authors: Wu
authors: Wenxian
authors: W
authors: Sun
authors: Gitta
authors: G
authors: Coaker
authors: Barbara
authors: B
authors: Kunkel
authors: Ping
authors: P
authors: He
authors: Libo
authors: L
authors: Shan
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism* / Q000382:microbiology*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D057056:Cysteine Proteases / Q000378:metabolism; D054884:Host-Pathogen Interactions / Q000502:physiology; D007210:Indoleacetic Acids / Q000378:metabolism*; D009154:Mutation; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D010935:Plant Diseases / Q000382:microbiology; D030821:Plants, Genetically Modified; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D055550:Protein Stability; D044224:Pseudomonas syringae / Q000378:metabolism / Q000472:pathogenicity*; D014157:Transcription Factors
chemical_list: C110728:AXR3 protein, Arabidopsis; D029681:Arabidopsis Proteins; D001426:Bacterial Proteins; D007210:Indoleacetic Acids; D009687:Nuclear Proteins; D014157:Transcription Factors; C030737:indoleacetic acid; D057056:Cysteine Proteases; D046988:Proteasome Endopeptidase Complex
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