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    Host inhibition of a bacterial virulence effector triggers immunity to infection (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2009-05-09
    Beschreibung: Plant pathogenic bacteria secrete effector proteins that attack the host signaling machinery to suppress immunity. Effectors can be recognized by hosts leading to immunity. One such effector is AvrPtoB of Pseudomonas syringae, which degrades host protein kinases, such as tomato Fen, through an E3 ligase domain. Pto kinase, which is highly related to Fen, recognizes AvrPtoB in conjunction with the resistance protein Prf. Here we show that Pto is resistant to AvrPtoB-mediated degradation because it inactivates the E3 ligase domain. AvrPtoB ubiquitinated Fen within the catalytic cleft, leading to its breakdown and loss of the associated Prf protein. Pto avoids this by phosphorylating and inactivating the AvrPtoB E3 domain. Thus, inactivation of a pathogen virulence molecule is one mechanism by which plants resist disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ntoukakis, Vardis -- Mucyn, Tatiana S -- Gimenez-Ibanez, Selena -- Chapman, Helen C -- Gutierrez, Jose R -- Balmuth, Alexi L -- Jones, Alexandra M E -- Rathjen, John P -- BB/D00456X/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2009 May 8;324(5928):784-7. doi: 10.1126/science.1169430.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sainsbury Laboratory, Colney, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19423826" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacterial Proteins/*antagonists & inhibitors/chemistry/genetics/metabolism ; Immunity, Innate ; Lycopersicon esculentum/genetics/*metabolism/*microbiology ; Mutant Proteins/metabolism ; Phosphorylation ; Plant Diseases/immunology/*microbiology ; Plant Leaves/metabolism ; Plant Proteins/*metabolism ; Plants, Genetically Modified ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/*metabolism ; Pseudomonas syringae/genetics/growth & development/metabolism/*pathogenicity ; Signal Transduction ; Tobacco/genetics/metabolism/microbiology ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination ; Virulence Factors/antagonists & inhibitors/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
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    A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2014-03-15
    Beschreibung: Innate immunity relies on the perception of pathogen-associated molecular patterns (PAMPs) by pattern-recognition receptors (PRRs) located on the host cell's surface. Many plant PRRs are kinases. Here, we report that the Arabidopsis receptor kinase EF-TU RECEPTOR (EFR), which perceives the elf18 peptide derived from bacterial elongation factor Tu, is activated upon ligand binding by phosphorylation on its tyrosine residues. Phosphorylation of a single tyrosine residue, Y836, is required for activation of EFR and downstream immunity to the phytopathogenic bacterium Pseudomonas syringae. A tyrosine phosphatase, HopAO1, secreted by P. syringae, reduces EFR phosphorylation and prevents subsequent immune responses. Thus, host and pathogen compete to take control of PRR tyrosine phosphorylation used to initiate antibacterial immunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Macho, Alberto P -- Schwessinger, Benjamin -- Ntoukakis, Vardis -- Brutus, Alexandre -- Segonzac, Cecile -- Roy, Sonali -- Kadota, Yasuhiro -- Oh, Man-Ho -- Sklenar, Jan -- Derbyshire, Paul -- Lozano-Duran, Rosa -- Malinovsky, Frederikke Gro -- Monaghan, Jacqueline -- Menke, Frank L -- Huber, Steven C -- He, Sheng Yang -- Zipfel, Cyril -- BB/G024944/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- R01AI060761/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2014 Mar 28;343(6178):1509-12. doi: 10.1126/science.1248849. Epub 2014 Mar 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Sainsbury Laboratory, Norwich Research Park, Norwich NR4 7UH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24625928" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Arabidopsis/*immunology/*microbiology ; Arabidopsis Proteins/agonists/*metabolism ; Bacterial Proteins/*metabolism ; Peptide Elongation Factor Tu/*metabolism ; Peptides/metabolism/pharmacology ; Phosphorylation ; Protein Tyrosine Phosphatases/*metabolism ; Pseudomonas syringae/enzymology/*pathogenicity ; Receptors, Pattern Recognition/agonists/*metabolism ; Tyrosine/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
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