{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kong L"],"funding":["NSF","Cancer Research UK","National Institutes of Health","Wellcome Trust","NIGMS NIH HHS","Biotechnology and Biological Sciences Research Council","National Science Foundation"],"pagination":["4591-4604.e8"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8684601"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["81(22)"],"pubmed_abstract":["Protein ADP-ribosylation is a reversible post-translational modification that transfers ADP-ribose from NAD<sup>+</sup> onto acceptor proteins. Poly(ADP-ribosyl)ation (PARylation), catalyzed by poly(ADP-ribose) polymerases (PARPs) and poly(ADP-ribose) glycohydrolases (PARGs), which remove the modification, regulates diverse cellular processes. However, the chemistry and physiological functions of mono(ADP-ribosyl)ation (MARylation) remain elusive. Here, we report that Arabidopsis zinc finger proteins SZF1 and SZF2, key regulators of immune gene expression, are MARylated by the noncanonical ADP-ribosyltransferase SRO2. Immune elicitation promotes MARylation of SZF1/SZF2 via dissociation from PARG1, which has an unconventional activity in hydrolyzing both poly(ADP-ribose) and mono(ADP-ribose"],"journal":["Molecular cell"],"pubmed_title":["Noncanonical mono(ADP-ribosyl)ation of zinc finger SZF proteins counteracts ubiquitination for protein homeostasis in plant immunity."],"pmcid":["PMC8684601"],"funding_grant_id":["MCB-1906060","R01GM092893","22284","R01 GM092893","R01 GM097247","101794","R01GM097247","IOS-1951094","210634/Z/18/Z","210634","C35050/A22284","BB/R007195/1"],"pubmed_authors":["Xu L","Kong L","Ahel I","Rack JGM","Shan L","Jang JC","Kim JH","Feng B","Yan Y","Zhang C","Wang Y","He P"],"additional_accession":[]},"is_claimable":false,"name":"Noncanonical mono(ADP-ribosyl)ation of zinc finger SZF proteins counteracts ubiquitination for protein homeostasis in plant immunity.","description":"Protein ADP-ribosylation is a reversible post-translational modification that transfers ADP-ribose from NAD<sup>+</sup> onto acceptor proteins. Poly(ADP-ribosyl)ation (PARylation), catalyzed by poly(ADP-ribose) polymerases (PARPs) and poly(ADP-ribose) glycohydrolases (PARGs), which remove the modification, regulates diverse cellular processes. However, the chemistry and physiological functions of mono(ADP-ribosyl)ation (MARylation) remain elusive. Here, we report that Arabidopsis zinc finger proteins SZF1 and SZF2, key regulators of immune gene expression, are MARylated by the noncanonical ADP-ribosyltransferase SRO2. Immune elicitation promotes MARylation of SZF1/SZF2 via dissociation from PARG1, which has an unconventional activity in hydrolyzing both poly(ADP-ribose) and mono(ADP-ribose","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Nov","modification":"2026-06-01T02:12:25.585Z","creation":"2025-02-19T01:28:35.007Z"},"accession":"S-EPMC8684601","cross_references":{"pubmed":["34592134"],"doi":["10.1016/j.molcel.2021.09.006"]}}