An extracellular aspartic protease functions in Arabidopsis disease resistance signaling

Yiji Xia*, Hideyuki Suzuki, Justin Borevitz, Jack Blount, Zejian Guo, Kanu Patel, Richard A Dixon, Chris Lamb

*Corresponding author for this work

Research output: Contribution to journalJournal articlepeer-review

291 Citations (Scopus)

Abstract

We have used activation tagging with T-DNA carrying cauliflower mosaic virus 35S enhancers to investigate the complex signaling networks underlying disease resistance in Arabidopsis. From a screen of ∼5000 lines, we identified constitutive disease resistance (CDR1) encoding an apoplastic aspartic protease, the overexpression of which causes dwarfing and resistance to virulent Pseudomonas syringae. These phenotypes reflect salicylic-acid-dependent activation of micro-oxidative bursts and various defense-related genes. Antisense CDR1 plants were compromised for resistance to avirulent P. syringae and more susceptible to virulent strains than wild type. CDR1 accumulates in intercellular fluid in response to pathogen attacks. Induction of CDR1 generates a small mobile signal, and CDR1 action is blocked by the protease inhibitor pepstatin and by mutations in the protease active sites. We propose that CDR1 mediates a peptide signal system involved in the activation of inducible resistance mechanisms.

Original languageEnglish
Pages (from-to)980-988
Number of pages9
JournalEMBO Journal
Volume23
Issue number4
DOIs
Publication statusPublished - 25 Feb 2004

Scopus Subject Areas

  • General Neuroscience
  • Molecular Biology
  • General Biochemistry,Genetics and Molecular Biology
  • General Immunology and Microbiology

User-Defined Keywords

  • Activation tagging
  • Arabidopsis thaliana
  • Aspartic protease
  • CDR1
  • Disease resistance

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