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PLoS Genet. 2015 Jan 8;11(1):e1004936. doi: 10.1371/journal.pgen.1004936. eCollection 2015 Jan.

Protein poly(ADP-ribosyl)ation regulates arabidopsis immune gene expression and defense responses.

Author information

1
Department of Biochemistry and Biophysics, and Institute for Plant Genomics & Biotechnology, Texas A&M University, College Station, Texas, United States of America.
2
Department of Plant Pathology and Microbiology, and Institute for Plant Genomics & Biotechnology, Texas A&M University, College Station, Texas, United States of America.
3
Department of Biochemistry and Biophysics, and Institute for Plant Genomics & Biotechnology, Texas A&M University, College Station, Texas, United States of America; Department of Plant Pathology and Microbiology, and Institute for Plant Genomics & Biotechnology, Texas A&M University, College Station, Texas, United States of America; Center of Biosciences and Biotechnology, Darcy Ribeiro State University of Northern of Rio de Janeiro, Brazil.
4
Department of Plant Pathology and Microbiology, and Institute for Plant Genomics & Biotechnology, Texas A&M University, College Station, Texas, United States of America; Center of Biosciences and Biotechnology, Darcy Ribeiro State University of Northern of Rio de Janeiro, Brazil.
5
Department of Biochemistry and Biophysics, and Institute for Plant Genomics & Biotechnology, Texas A&M University, College Station, Texas, United States of America; Department of Biology, University of Puerto Rico, Mayagüez Campus, Mayagüez, Puerto Rico.
6
Department of Biology, University of Puerto Rico, Mayagüez Campus, Mayagüez, Puerto Rico.

Abstract

Perception of microbe-associated molecular patterns (MAMPs) elicits transcriptional reprogramming in hosts and activates defense to pathogen attacks. The molecular mechanisms underlying plant pattern-triggered immunity remain elusive. A genetic screen identified Arabidopsis poly(ADP-ribose) glycohydrolase 1 (atparg1) mutant with elevated immune gene expression upon multiple MAMP and pathogen treatments. Poly(ADP-ribose) glycohydrolase (PARG) is predicted to remove poly(ADP-ribose) polymers on acceptor proteins modified by poly(ADP-ribose) polymerases (PARPs) with three PARPs and two PARGs in Arabidopsis genome. AtPARP1 and AtPARP2 possess poly(ADP-ribose) polymerase activity, and the activity of AtPARP2 was enhanced by MAMP treatment. AtPARG1, but not AtPARG2, carries glycohydrolase activity in vivo and in vitro. Importantly, mutation (G450R) in atparg1 blocks its activity and the corresponding residue is highly conserved and essential for human HsPARG activity. Consistently, mutant atparp1atparp2 plants exhibited compromised immune gene activation and enhanced susceptibility to pathogen infections. Our study indicates that protein poly(ADP-ribosyl)ation plays critical roles in plant immune gene expression and defense to pathogen attacks.

PMID:
25569773
PMCID:
PMC4287526
DOI:
10.1371/journal.pgen.1004936
[Indexed for MEDLINE]
Free PMC Article

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