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Apoplastic peroxidases are required for salicylic acid-mediated defense against Pseudomonas syringae.

Publication ,  Journal Article
Mammarella, ND; Cheng, Z; Fu, ZQ; Daudi, A; Bolwell, GP; Dong, X; Ausubel, FM
Published in: Phytochemistry
April 2015

Reactive oxygen species (ROS) generated by NADPH oxidases or apoplastic peroxidases play an important role in the plant defense response. Diminished expression of at least two Arabidopsis thaliana peroxidase encoding genes, PRX33 (At3g49110) and PRX34 (At3g49120), as a consequence of anti-sense expression of a heterologous French bean peroxidase gene (asFBP1.1), were previously shown to result in reduced levels of ROS following pathogen attack, enhanced susceptibility to a variety of bacterial and fungal pathogens, and reduced levels of callose production and defense-related gene expression in response to the microbe associated molecular pattern (MAMP) molecules flg22 and elf26. These data demonstrated that the peroxidase-dependent oxidative burst plays an important role in the elicitation of pattern-triggered immunity (PTI). Further work reported in this paper, however, shows that asFBP1.1 antisense plants are not impaired in all PTI-associated responses. For example, some but not all flg22-elicited genes are induced to lower levels by flg22 in asFPB1.1, and callose deposition in asFPB1.1 is similar to wild-type following infiltration with a Pseudomonas syringae hrcC mutant or with non-host P. syringae pathovars. Moreover, asFPB1.1 plants did not exhibit any apparent defect in their ability to mount a hypersensitive response (HR). On the other hand, salicylic acid (SA)-mediated activation of PR1 was dramatically impaired in asFPB1.1 plants. In addition, P. syringae-elicited expression of many genes known to be SA-dependent was significantly reduced in asFBP1.1 plants. Consistent with this latter result, in asFBP1.1 plants the key regulator of SA-mediated responses, NPR1, showed both dramatically decreased total protein abundance and a failure to monomerize, which is required for its translocation into the nucleus.

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Published In

Phytochemistry

DOI

EISSN

1873-3700

ISSN

0031-9422

Publication Date

April 2015

Volume

112

Start / End Page

110 / 121

Related Subject Headings

  • Signal Transduction
  • Salicylic Acid
  • Pseudomonas syringae
  • Plant Biology & Botany
  • Phaseolus
  • Peroxidases
  • Mutation
  • Host-Pathogen Interactions
  • Bacterial Outer Membrane Proteins
  • Arabidopsis Proteins
 

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Mammarella, N. D., Cheng, Z., Fu, Z. Q., Daudi, A., Bolwell, G. P., Dong, X., & Ausubel, F. M. (2015). Apoplastic peroxidases are required for salicylic acid-mediated defense against Pseudomonas syringae. Phytochemistry, 112, 110–121. https://doi.org/10.1016/j.phytochem.2014.07.010
Mammarella, Nicole D., Zhenyu Cheng, Zheng Qing Fu, Arsalan Daudi, G Paul Bolwell, Xinnian Dong, and Frederick M. Ausubel. “Apoplastic peroxidases are required for salicylic acid-mediated defense against Pseudomonas syringae.Phytochemistry 112 (April 2015): 110–21. https://doi.org/10.1016/j.phytochem.2014.07.010.
Mammarella ND, Cheng Z, Fu ZQ, Daudi A, Bolwell GP, Dong X, et al. Apoplastic peroxidases are required for salicylic acid-mediated defense against Pseudomonas syringae. Phytochemistry. 2015 Apr;112:110–21.
Mammarella, Nicole D., et al. “Apoplastic peroxidases are required for salicylic acid-mediated defense against Pseudomonas syringae.Phytochemistry, vol. 112, Apr. 2015, pp. 110–21. Epmc, doi:10.1016/j.phytochem.2014.07.010.
Mammarella ND, Cheng Z, Fu ZQ, Daudi A, Bolwell GP, Dong X, Ausubel FM. Apoplastic peroxidases are required for salicylic acid-mediated defense against Pseudomonas syringae. Phytochemistry. 2015 Apr;112:110–121.
Journal cover image

Published In

Phytochemistry

DOI

EISSN

1873-3700

ISSN

0031-9422

Publication Date

April 2015

Volume

112

Start / End Page

110 / 121

Related Subject Headings

  • Signal Transduction
  • Salicylic Acid
  • Pseudomonas syringae
  • Plant Biology & Botany
  • Phaseolus
  • Peroxidases
  • Mutation
  • Host-Pathogen Interactions
  • Bacterial Outer Membrane Proteins
  • Arabidopsis Proteins