Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus
| Autor: | Dong Xin Feng, Imre E. Somssich, Laurent Deslandes, Manirath Khounlotham, Yves Marco, Stéphane Genin, Jocelyne Olivier, Nemo Peeters, Christian Boucher |
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| Přispěvatelé: | Unité mixte de recherche interactions plantes-microorganismes, Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
0106 biological sciences
Time Factors Protein family Amino Acid Motifs Green Fluorescent Proteins Arabidopsis [SDV.BC]Life Sciences [q-bio]/Cellular Biology 01 natural sciences Models Biological 03 medical and health sciences Protein structure Bacterial Proteins Two-Hybrid System Techniques Genetic Predisposition to Disease Nuclear protein ComputingMilieux_MISCELLANEOUS 030304 developmental biology Plant Diseases Genetics Cell Nucleus 0303 health sciences Ralstonia solanacearum Multidisciplinary Microscopy Confocal biology Effector Ubiquitin food and beverages Nuclear Proteins R gene DNA RALSTONIA-SOLANACEARUM Biological Sciences biology.organism_classification WRKY protein domain Protein Structure Tertiary Luminescent Proteins Gram-Negative Aerobic Rods and Cocci Nuclear localization sequence 010606 plant biology & botany Protein Binding |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2003, 100 (13), pp.8024-8029 |
| ISSN: | 0027-8424 1091-6490 |
| Popis: | RRS1-R confers broad-spectrum resistance to several strains of the causal agent of bacterial wilt, Ralstonia solanacearum . Although genetically defined as recessive, this R gene encodes a protein whose structure combines the TIR-NBS-LRR domains found in several R proteins and a WRKY motif characteristic of some plant transcriptional factors and behaves as a dominant gene in transgenic susceptible plants. Here we show that PopP2, a R. solanacearum type III effector, which belongs to the YopJ/AvrRxv protein family, is the avirulence protein recognized by RRS1-R. Furthermore, an interaction between PopP2 and both RRS1-R and RRS1-S, present in the resistant Nd-1 and susceptible Col-5 Arabidopsis thaliana ecotypes, respectively, was detected by using the yeast split-ubiquitin two-hybrid system. This interaction, which required the full-length R protein, was not observed between the RRS1 proteins and PopP1, another member of the YopJ/AvrRxv family present in strain GMI1000 and that confers avirulence in Petunia . We further demonstrate that both the Avr protein and the RRS1 proteins colocalize in the nucleus and that the nuclear localization of the RRS1 proteins are dependent on the presence of PopP2. |
| Databáze: | OpenAIRE |
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