Journal article
Small Molecule DFPM Derivative-Activated Plant Resistance Protein Signaling in Roots Is Unaffected by EDS1 Subcellular Targeting Signal and Chemical Genetic Isolation of victr R-Protein Mutants
PloS one, Vol.11(5), pp.e0155937-e0155937
2016
Handle:
https://hdl.handle.net/2376/107247
PMCID: PMC4878808
PMID: 27219122
Abstract
The small molecule DFPM ([5-(3,4-dichlorophenyl)furan-2-yl]-piperidine-1-ylmethanethione) was recently shown to trigger signal transduction via early effector-triggered immunity signaling genes including EDS1 and PAD4 in Arabidopsis thaliana accession Col-0. Chemical genetic analyses of A. thaliana natural variants identified the plant Resistance protein-like Toll/Interleukin1 Receptor (TIR)-Nucleotide Binding (NB)-Leucine-Rich Repeat (LRR) protein VICTR as required for DFPM-mediated root growth arrest. Here a chemical genetic screen for mutants which disrupt DFPM-mediated root growth arrest in the Col-0 accession identified new mutant alleles of the TIR-NB-LRR gene VICTR. One allele, victr-6, carries a Gly216-to-Asp mutation in the Walker A domain supporting an important function of the VICTR nucleotide binding domain in DFPM responses consistent with VICTR acting as a canonical Resistance protein. The essential nucleo-cytoplasmic regulator of TIR-NB-LRR-mediated effector-triggered immunity, EDS1, was reported to have both nuclear and cytoplasmic actions in pathogen resistance. DFPM was used to investigate the requirements for subcellular EDS1 localization in DFPM-mediated root growth arrest. EDS1-YFP fusions engineered to localize mainly in the cytoplasm or the nucleus by tagging with a nuclear export signal (NES) or a nuclear localization signal (NLS), respectively, were tested. We found that wild-type EDS1-YFP and both the NES and NLS-tagged EDS1 variants were induced by DFPM treatments and fully complemented eds1 mutant plants in root responses to DFPM, suggesting that enrichment of EDS1 in either compartment could confer DFPM-mediated root growth arrest. We further found that a light and O2-dependent modification of DFPM is necessary to mediate DFPM signaling in roots. Chemical analyses including Liquid Chromatography-Mass Spectrometry and High-Resolution Atmospheric Pressure Chemical Ionization Mass Spectrometry identified a DFPM modification product that is likely responsible for bioactivity mediating root growth arrest. We propose a chemical structure of this product and a possible reaction mechanism for DFPM modification.
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Details
- Title
- Small Molecule DFPM Derivative-Activated Plant Resistance Protein Signaling in Roots Is Unaffected by EDS1 Subcellular Targeting Signal and Chemical Genetic Isolation of victr R-Protein Mutants
- Creators
- Hans-Henning Kunz - Division of Biological Sciences, Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California 92093-0116, United States of AmericaJiyoung Park - Division of Biological Sciences, Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California 92093-0116, United States of AmericaEmily Mevers - Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego, La Jolla, California, 92093-0212, United States of AmericaAna V García - Max-Planck Institute for Plant Breeding Research, Department of Plant-Microbe Interactions, D-50829 Cologne, GermanySamantha Highhouse - Division of Biological Sciences, Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California 92093-0116, United States of AmericaWilliam H Gerwick - Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, California, 92093, United States of AmericaJane E Parker - Max-Planck Institute for Plant Breeding Research, Department of Plant-Microbe Interactions, D-50829 Cologne, GermanyJulian I Schroeder - Division of Biological Sciences, Section of Cell and Developmental Biology, University of California San Diego, La Jolla, California 92093-0116, United States of America
- Publication Details
- PloS one, Vol.11(5), pp.e0155937-e0155937
- Academic Unit
- Biological Sciences, School of
- Publisher
- United States
- Grant note
- T32 CA009523 / NCI NIH HHS R01 GM060396 / NIGMS NIH HHS
- Identifiers
- 99900546758001842
- Language
- English
- Resource Type
- Journal article