| Literature DB >> 34592134 |
Liang Kong1, Baomin Feng2, Yan Yan1, Chao Zhang3, Jun Hyeok Kim1, Lahong Xu1, Johannes Gregor Matthias Rack4, Ying Wang5, Jyan-Chyun Jang6, Ivan Ahel4, Libo Shan1, Ping He7.
Abstract
Protein ADP-ribosylation is a reversible post-translational modification that transfers ADP-ribose from NAD+ 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) from acceptor proteins. MARylation antagonizes polyubiquitination of SZF1 mediated by the SH3 domain-containing proteins SH3P1/SH3P2, thereby stabilizing SZF1 proteins. Our study uncovers a noncanonical ADP-ribosyltransferase mediating MARylation of immune regulators and underpins the molecular mechanism of maintaining protein homeostasis by the counter-regulation of ADP-ribosylation and polyubiquitination to ensure proper immune responses.Entities:
Keywords: ADP-ribosyltransferase; MARylation; PARylation; plant immunity; protein ADP-ribosylation; protein stability; ubiquitination; zinc finger proteins
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Year: 2021 PMID： 34592134 PMCID： PMC8684601 DOI： 10.1016/j.molcel.2021.09.006
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 19.328