Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus

By L. Deslandes, Jocelyne Olivier, N. Peeters, D. Feng, Manirath Khounlotham, C. Boucher, I. Somssich, S. Genin, Yves Marco. Proceedings of the National Academy of Sciences of the United States of America, 2003

750 citations recorded by the source corpus.

Subfields: Plant Science

View Paper: https://www.semanticscholar.org/paper/b7d656bcb8cd308f455e129c3f6d4c26ee05abc7

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In Plant Science

1. David Mackey
2. A. Bent
3. I. Somssich
4. Jeffery L. Dangl
5. B. Staskawicz
6. T. Eulgem
7. Shree P. Pandey
8. P. Dodds

Citations in the corpus

• Type III secretion system effector proteins: double agents in bacterial disease and plant defense. (2004, background): “The AvrBs3 and YopJ/P/AvrBsT families have members that localize to the nucleus (49, 73, 161, 172).”
• A Novel Role for the TIR Domain in Association with Pathogen-Derived Elicitors (2007, background): “Further, nuclear-localized Arabidopsis RRS1 possesses a WRKY DNA-binding domain as a C-terminal extension to its TIR-NB-LRR core structure [11,44].”
• Plant NBS-LRR proteins in pathogen sensing and host defense (2006, methodology): “The direct detection model was further supported by the observation that the Arabidopsis thaliana RRS1 protein interacts with the bacterial wilt pathogen protein PopP2 in a 'split-ubiquitin' yeast two-hybrid experimen”
• Tomato stress-responsive factor TSRF1 interacts with ethylene responsive element GCC box and regulates pathogen resistance to Ralstonia solanacearum (2004, background): “R. solanacearum has been investigated both biochemically and genetically and recognized as a model system for the analysis of pathogenicity (Deslandes et al., 2002, 2003).”
• Recognition and response in the plant immune system. (2003, background): “RRS1-R protein is an NBS-LRR with the addition of a WRKY transcription factor domain as part of its open reading frame (26, 27).”
• WRKY transcription factors: from DNA binding towards biological function. (2004, background): “RRS1/AtWRKY52 physically interacts with the corresponding bacterial avirulence gene product, PopP2, and both colocalise to the plant cell nucleus [40 ].”
• Plant NBS-LRR proteins: adaptable guards (2006, background): “The simplest model for NBS-LRR R protein function is as receptors that bind effector molecules secreted by pathogens, but direct interactions between NBS-LRR R proteins and effector proteins have been detected only rarely [47,48].”
• Host-microbe interactions: shaping the evolution of the plant immune response. (2006, background): “For instance, RRS1-R that recognizes Ralstonia solanacearum is a TIR-NB-LRR protein that also contains an carboxy-terminal nuclear localization signal and WRKY transcriptional activation domain (Deslandes et al., 2003).”
• Elicitors, effectors, and R genes: the new paradigm and a lifetime supply of questions. (2007, background): “These include the function of a fused NB-LRR-WRKY protein, the nuclear presence of the tobacco N protein, and the nuclear activity of AvrBs3-family pathogen effector proteins (25, 43, 66).”
• Networks of WRKY transcription factors in defense signaling. (2007, background): “Thus, it is tempting to speculate that the interaction with PopP2 excludes AtWRKY52/RRS1 from its proper DNA target sites and activates defenses by de-repression.”
• Plant immunity: towards an integrated view of plant–pathogen interactions (2010, background): “thaliana RRS1-R interacts with the Ralstonia solanacearum effector PopP2 in the nucleu”