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Peroxidase-dependent apoplastic oxidative burst in Arabidopsis required for pathogen resistance

The oxidative burst is an early response to pathogen attack leading to the production of reactive oxygen species (ROS) including hydrogen peroxide. Two major mechanisms involving either NADPH oxidases or peroxidases that may exist singly or in combination in different plant species have been propose...

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Published in:The Plant journal : for cell and molecular biology 2006-09, Vol.47 (6), p.851-863
Main Authors: Bindschedler, Laurence V, Dewdney, Julia, Blee, Kris A, Stone, Julie M, Asai, Tsuneaki, Plotnikov, Julia, Denoux, Carine, Hayes, Tezni, Gerrish, Chris, Davies, Dewi R, Ausubel, Frederick M, Bolwell, G. Paul
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Language:English
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Summary:The oxidative burst is an early response to pathogen attack leading to the production of reactive oxygen species (ROS) including hydrogen peroxide. Two major mechanisms involving either NADPH oxidases or peroxidases that may exist singly or in combination in different plant species have been proposed for the generation of ROS. We identified an Arabidopsis thaliana azide-sensitive but diphenylene iodonium-insensitive apoplastic oxidative burst that generates H₂O₂ in response to a Fusarium oxysporum cell-wall preparation. Transgenic Arabidopsis plants expressing an anti-sense cDNA encoding a type III peroxidase, French bean peroxidase type 1 (FBP1) exhibited an impaired oxidative burst and were more susceptible than wild-type plants to both fungal and bacterial pathogens. Transcriptional profiling and RT-PCR analysis showed that the anti-sense (FBP1) transgenic plants had reduced levels of specific peroxidase-encoding mRNAs, including mRNAs corresponding to Arabidopsis genes At3g49120 (AtPCb) and At3g49110 (AtPCa) that encode two class III peroxidases with a high degree of homology to FBP1. These data indicate that peroxidases play a significant role in generating H₂O₂ during the Arabidopsis defense response and in conferring resistance to a wide range of pathogens.
ISSN:0960-7412
1365-313X
DOI:10.1111/j.1365-313x.2006.02837.x