This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 20/8/2252    most recent tpc.108.058685v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Google Scholar Articles by Bernoux, M. Articles by Deslandes, L. PubMed PubMed Citation Articles by Bernoux, M. Articles by Deslandes, L. Agricola Articles by Bernoux, M. Articles by Deslandes, L.

RD19, an Arabidopsis Cysteine Protease Required for RRS1-R–Mediated Resistance, Is Relocalized to the Nucleus by the Ralstonia solanacearum PopP2 Effector^[W]

^a Laboratoire des Interactions Plantes Microorganismes, Unité Mixte de Recherche, Centre National de la Recherche Scientifique–Institut National de la Recherche Agronomique 2594/441, F-31320 Castanet-Tolosan, France
^b Institut Fédératif de Recherche 40, Centre National de la Recherche Scientifique, Plateforme Imagerie, Pôle de Biotechnologie Végétale, F-31320 Castanet-Tolosan, France
^c Unité Mixte de Recherche, Centre National de la Recherche Scientifique, Université Paul Sabatier, F-31320 Castanet-Tolosan, France
^d Laboratory of Phytopathology, Wageningen University, 6709 PD Wageningen, The Netherlands
^e Centre for Biosystems Genomics, Wageningen University, 6709 PD Wageningen, The Netherlands

² Address correspondence to laurent.deslandes{at}toulouse.inra.fr.

Bacterial wilt, a disease impacting cultivated crops worldwide, is caused by the pathogenic bacterium Ralstonia solanacearum. PopP2 (for Pseudomonas outer protein P2) is an R. solanacearum type III effector that belongs to the YopJ/AvrRxv protein family and interacts with the Arabidopsis thaliana RESISTANT TO RALSTONIA SOLANACEARUM 1-R (RRS1-R) resistance protein. RRS1-R contains the Toll/Interleukin1 receptor–nucleotide binding site–Leu-rich repeat domains found in several cytoplasmic R proteins and a C-terminal WRKY DNA binding domain. In this study, we identified the Arabidopsis Cys protease RESPONSIVE TO DEHYDRATION19 (RD19) as being a PopP2-interacting protein whose expression is induced during infection by R. solanacearum. An Arabidopsis rd19 mutant in an RRS1-R genetic background is compromised in resistance to the bacterium, indicating that RD19 is required for RRS1-R–mediated resistance. RD19 normally localizes in mobile vacuole-associated compartments and, upon coexpression with PopP2, is specifically relocalized to the plant nucleus, where the two proteins physically interact. No direct physical interaction between RRS1-R and RD19 in the presence of PopP2 was detected in the nucleus as determined by Förster resonance energy transfer. We propose that RD19 associates with PopP2 to form a nuclear complex that is required for activation of the RRS1-R–mediated resistance response.