{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Monge-Waleryszak L"],"funding":["Investissement d'Avenir Infrastructures Nationales en Biologie et Santé","Agence Nationale de la Recherche","Fonds Européens de DEveloppement Régional, FEDER","French Ministry of National Education and Research","FBI, France BioImaging","École Universitaire de Recherche (EUR)","Erasmus Universiteit Rotterdam","French Laboratory of Excellence project \"TULIP\"","Graduate School of University Grenoble Alpes"],"pagination":["e70205"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12071340"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["122(3)"],"pubmed_abstract":["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 th"],"journal":["The Plant journal : for cell and molecular biology"],"pubmed_title":["Three ARID proteins involved in chromatin remodeling PEAT complexes are targeted by the Ralstonia solanacearum effector PopP2 and contribute to bacterial wilt disease."],"pmcid":["PMC12071340"],"funding_grant_id":["ANR-18-CE20-0015","ANR-10-INBS-08","ANR‐18‐CE20‐0015","ANR15‐CE20‐0016‐01","ANR-10-LABX-41","ANR-11-IDEX-0002-02","ANR-17-EURE-0003","ANR-10-INBS-0004","ANR15-CE20-0016-01","ANR‐18‐EURE‐0019","ANR-18-EURE-0019"],"pubmed_authors":["Martinez Y","Coute Y","Vicedo C","Verin C","Pacquit V","Girard M","Monge-Waleryszak L","Carcagno M","Culerrier R","Deslandes L"],"additional_accession":[]},"is_claimable":false,"name":"Three ARID proteins involved in chromatin remodeling PEAT complexes are targeted by the Ralstonia solanacearum effector PopP2 and contribute to bacterial wilt disease.","description":"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 th","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-01T14:58:58.887Z","creation":"2026-04-08T13:30:43.449Z"},"accession":"S-EPMC12071340","cross_references":{"pubmed":["40358473"],"doi":["10.1111/tpj.70205"]}}