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Noncanonical mono(ADP-ribosyl)ation of zinc finger SZF proteins counteracts ubiquitination for protein homeostasis in plant immunity.
Kong, Liang; Feng, Baomin; Yan, Yan; Zhang, Chao; Kim, Jun Hyeok; Xu, Lahong; Rack, Johannes Gregor Matthias; Wang, Ying; Jang, Jyan-Chyun; Ahel, Ivan; Shan, Libo; He, Ping.
Affiliation
  • Kong L; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
  • Feng B; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA; State Key Laboratory of Ecological Control of Fujian-Taiwan Crop Pests, Key Laboratory of Ministry of Education for Genetics, Breeding and Multiple Utilization of Crops, Plant Immunity Center, Fujian
  • Yan Y; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
  • Zhang C; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA; Department of Plant Pathology and Microbiology, Texas A&M University, College Station, TX 77843, USA.
  • Kim JH; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
  • Xu L; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
  • Rack JGM; Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
  • Wang Y; Department of Biological Sciences, Mississippi State University, Starkville, MS 39762, USA.
  • Jang JC; Department of Horticulture and Crop Science, Department of Molecular Genetics, Center for Applied Plant Sciences, and Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
  • Ahel I; Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
  • Shan L; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
  • He P; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA. Electronic address: pinghe@tamu.edu.
Mol Cell ; 81(22): 4591-4604.e8, 2021 11 18.
Article in En | MEDLINE | ID: mdl-34592134
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Zinc Fingers / Arabidopsis / Arabidopsis Proteins / Intracellular Signaling Peptides and Proteins / DNA-Binding Proteins / Ubiquitination / Plant Immunity / ADP-Ribosylation Limits: Humans Language: En Journal: Mol Cell Year: 2021 Document type: Article
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Zinc Fingers / Arabidopsis / Arabidopsis Proteins / Intracellular Signaling Peptides and Proteins / DNA-Binding Proteins / Ubiquitination / Plant Immunity / ADP-Ribosylation Limits: Humans Language: En Journal: Mol Cell Year: 2021 Document type: Article