<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kong L</submitter><funding>NSF</funding><funding>Cancer Research UK</funding><funding>National Institutes of Health</funding><funding>Wellcome Trust</funding><funding>NIGMS NIH HHS</funding><funding>Biotechnology and Biological Sciences Research Council</funding><funding>National Science Foundation</funding><pagination>4591-4604.e8</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8684601</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>81(22)</volume><pubmed_abstract>Protein ADP-ribosylation is a reversible post-translational modification that transfers ADP-ribose from NAD&lt;sup>+&lt;/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</pubmed_abstract><journal>Molecular cell</journal><pubmed_title>Noncanonical mono(ADP-ribosyl)ation of zinc finger SZF proteins counteracts ubiquitination for protein homeostasis in plant immunity.</pubmed_title><pmcid>PMC8684601</pmcid><funding_grant_id>MCB-1906060</funding_grant_id><funding_grant_id>R01GM092893</funding_grant_id><funding_grant_id>22284</funding_grant_id><funding_grant_id>R01 GM092893</funding_grant_id><funding_grant_id>R01 GM097247</funding_grant_id><funding_grant_id>101794</funding_grant_id><funding_grant_id>R01GM097247</funding_grant_id><funding_grant_id>IOS-1951094</funding_grant_id><funding_grant_id>210634/Z/18/Z</funding_grant_id><funding_grant_id>210634</funding_grant_id><funding_grant_id>C35050/A22284</funding_grant_id><funding_grant_id>BB/R007195/1</funding_grant_id><pubmed_authors>Xu L</pubmed_authors><pubmed_authors>Kong L</pubmed_authors><pubmed_authors>Ahel I</pubmed_authors><pubmed_authors>Rack JGM</pubmed_authors><pubmed_authors>Shan L</pubmed_authors><pubmed_authors>Jang JC</pubmed_authors><pubmed_authors>Kim JH</pubmed_authors><pubmed_authors>Feng B</pubmed_authors><pubmed_authors>Yan Y</pubmed_authors><pubmed_authors>Zhang C</pubmed_authors><pubmed_authors>Wang Y</pubmed_authors><pubmed_authors>He P</pubmed_authors></additional><is_claimable>false</is_claimable><name>Noncanonical mono(ADP-ribosyl)ation of zinc finger SZF proteins counteracts ubiquitination for protein homeostasis in plant immunity.</name><description>Protein ADP-ribosylation is a reversible post-translational modification that transfers ADP-ribose from NAD&lt;sup>+&lt;/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</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Nov</publication><modification>2026-06-01T02:12:25.585Z</modification><creation>2025-02-19T01:28:35.007Z</creation></dates><accession>S-EPMC8684601</accession><cross_references><pubmed>34592134</pubmed><doi>10.1016/j.molcel.2021.09.006</doi></cross_references></HashMap>