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An extracellular aspartic protease functions in Arabidopsis disease resistance signaling
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An extracellular aspartic protease functions in Arabidopsis disease resistance signaling
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Journal Article
An extracellular aspartic protease functions in Arabidopsis disease resistance signaling
2004
Overview
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.
Publisher
Nature Publishing Group UK,John Wiley & Sons, Ltd,Springer Nature B.V,Nature Publishing Group
