biostudies-literatureMonge-Waleryszak LInvestissement d'Avenir Infrastructures Nationales en Biologie et SantéAgence Nationale de la RechercheFonds Européens de DEveloppement Régional, FEDERFrench Ministry of National Education and ResearchFBI, France BioImagingÉcole Universitaire de Recherche (EUR)Erasmus Universiteit RotterdamFrench Laboratory of Excellence project "TULIP"Graduate School of University Grenoble Alpese70205https://www.ebi.ac.uk/biostudies/studies/S-EPMC12071340biostudies-literatureUnknown122(3)Like many gram-negative phytopathogenic bacteria, Ralstonia solanacearum uses a type III secretion system to deliver into host cells a cocktail of effector proteins that can interfere with plant defenses and promote infection. One of these effectors, the nuclear-targeted PopP2 acetyltransferase, was reported to inhibit many defensive WRKY transcription factors through acetylation. To gain a better understanding of the mechanisms by which PopP2 might exert its virulence functions, we searched for other PopP2-interacting partners. Here we report the identification of the Arabidopsis thaliana AT-Rich Interaction Domain protein 3 (ARID3) and its close homologs, ARID2 and ARID4, as additional targets of PopP2. These ARID proteins are core components of the chromatin remodeling PEAT complexes thThe Plant journal : for cell and molecular biologyThree ARID proteins involved in chromatin remodeling PEAT complexes are targeted by the Ralstonia solanacearum effector PopP2 and contribute to bacterial wilt disease.PMC12071340ANR-18-CE20-0015ANR-10-INBS-08ANR‐18‐CE20‐0015ANR15‐CE20‐0016‐01ANR-10-LABX-41ANR-11-IDEX-0002-02ANR-17-EURE-0003ANR-10-INBS-0004ANR15-CE20-0016-01ANR‐18‐EURE‐0019ANR-18-EURE-0019Martinez YCoute YVicedo CVerin CPacquit VGirard MMonge-Waleryszak LCarcagno MCulerrier RDeslandes LfalseThree ARID proteins involved in chromatin remodeling PEAT complexes are targeted by the Ralstonia solanacearum effector PopP2 and contribute to bacterial wilt disease.Like many gram-negative phytopathogenic bacteria, Ralstonia solanacearum uses a type III secretion system to deliver into host cells a cocktail of effector proteins that can interfere with plant defenses and promote infection. One of these effectors, the nuclear-targeted PopP2 acetyltransferase, was reported to inhibit many defensive WRKY transcription factors through acetylation. To gain a better understanding of the mechanisms by which PopP2 might exert its virulence functions, we searched for other PopP2-interacting partners. Here we report the identification of the Arabidopsis thaliana AT-Rich Interaction Domain protein 3 (ARID3) and its close homologs, ARID2 and ARID4, as additional targets of PopP2. These ARID proteins are core components of the chromatin remodeling PEAT complexes th2025-01-01T00:00:00Z2025 May2026-06-01T14:58:58.887Z2026-04-08T13:30:43.449ZS-EPMC120713404035847310.1111/tpj.70205