Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Plant Physiology Preview
Published on November 4, 2009; 10.1104/pp.109.148049

OPEN ACCESS ARTICLE
This Article
Free via Open Access: OA
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrow Supplemental Data
Right arrowOA All Versions of this Article:
pp.109.148049v2    most recent
pp.109.148049v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via CrossRef
Google Scholar
Right arrow Articles by Adams-Phillips, L.
Right arrow Articles by Bent, A. F.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Adams-Phillips, L.
Right arrow Articles by Bent, A. F.
Agricola
Right arrow Articles by Adams-Phillips, L.
Right arrow Articles by Bent, A. F.

Received September 25, 2009
Accepted October 30, 2009

Disruption of poly(ADP-ribosyl)ation mechanisms alters responses of Arabidopsis thaliana to biotic stress

Lori Adams-Phillips , Amy G. Briggs , and Andrew F. Bent *

Department of Plant Pathology; Program in Cellular and Molecular Biology, University of Wisconsin - Madison, Madison, WI 53706

* Corresponding author; email: afbent{at}wisc.edu.

Poly(ADP-ribosyl)ation is a post-translational protein modification in which ADP-ribose units derived from NAD+ are attached to proteins by poly(ADP-ribose) polymerase (PARP) enzymes. ADP-ribose groups are removed from these polymer chains by the enzyme poly(ADP-ribose) glycohydrolase (PARG). In animals, poly(ADP-ribosyl)ation is associated with DNA damage responses and programmed cell death. Previously, we hypothesized a role for poly(ADP-ribosyl)ation in plant defense responses when we detected defense-associated expression of the poly(ADP-ribosyl)ation-related genes PARG2 and NUDT7, and observed altered callose deposition in the presence of a chemical PARP inhibitor (Adams-Phillips et al., 2008). The role of poly(ADP-ribosyl)ation in plant defenses was more extensively investigated in the current study, using Arabidopsis thaliana. Pharmacological inhibition of PARP using 3-aminobenzamide (3AB) perturbs certain innate immune responses to MAMPs (flg22 and elf18), including callose deposition, lignin deposition, pigment accumulation, and phenylalanine ammonia lyase (PAL) activity, but does not disrupt other responses such as the initial oxidative burst and expression of some early defense-associated genes. Mutant parg1 seedlings exhibit an exaggerated seedling growth inhibition and pigment accumulation in response to elf18, and are hypersensitive to the DNA damaging agent mitomycin C. Both parg1 and parg2 knockout plants show accelerated onset of disease symptoms when infected with Botrytis cinerea. Cellular levels of ADP-ribose polymer increase after infection with avirulent Pseudomonas syringae pv. tomato DC3000 avrRpt2+, and pathogen-dependent changes in the poly(ADP-ribosyl)ation of discrete proteins were also observed. We conclude that poly(ADP-ribosyl)ation is a functional component in plant responses to biotic stress.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2009 by the American Society of Plant Biologists