Publication Information
Kong et al. 2022
No external accession available
Abstract
Mol Cell. 2021 Nov 18;81(22):4591-4604.e8. doi: 10.1016/j.molcel.2021.09.006.
Epub 2021 Sep 29.
Noncanonical mono(ADP-ribosyl)ation of zinc finger SZF proteins counteracts
ubiquitination for protein homeostasis in plant immunity.
Kong L(1), Feng B(2), Yan Y(1), Zhang C(3), Kim JH(1), Xu L(1), Rack JGM(4),
Wang Y(5), Jang JC(6), Ahel I(4), Shan L(1), He P(7).
Author information:
(1)Department of Biochemistry and Biophysics, Texas A&M University, College
Station, TX 77843, USA.
(2)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
Agriculture and Forestry University, Fuzhou 350002, P.R. China.
(3)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.
(4)Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE,
UK.
(5)Department of Biological Sciences, Mississippi State University, Starkville,
MS 39762, USA.
(6)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.
(7)Department of Biochemistry and Biophysics, Texas A&M University, College
Station, TX 77843, USA. Electronic address: pinghe@tamu.edu.
Comment in
Mol Cell. 2021 Nov 18;81(22):4572-4574.
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.
Copyright © 2021 Elsevier Inc. All rights reserved.
DOI: 10.1016/j.molcel.2021.09.006
PMCID: PMC8684601
PMID: 34592134 [Indexed for MEDLINE]
Conflict of interest statement: Declaration of interests The authors declare no
competing interests.
