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Role of superoxide dismutases and alkyl hydroperoxidases in pathogenesis of Pseudomonas syringae (741.1)
Author(s) -
Bile Ernest,
Guo Ming,
Becker Will,
Alfano Jim
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.741.1
Subject(s) - pseudomonas syringae , mutant , mutagenesis , arabidopsis , arabidopsis thaliana , virulence , reactive oxygen species , pathogen , biology , superoxide dismutase , superoxide , microbiology and biotechnology , wild type , gene , biochemistry , oxidative stress , enzyme
Plants, such as Arabidopsis thaliana, release reactive oxygen species (ROS) such as the superoxide anion, hydroxyl radical, and hydroxyl ion as a defense mechanism when they are infected with microorganisms. The production of ROS results in restriction of the growth of pathogens like Pseudomonas syringae. In order to be a successful pathogen, P. syringae must suppress these responses when it infects plants. P. syringae has evolved redox‐related enzymes to detoxify ROS. The sods and Ahps are able to relieve oxidative stresses by detoxifying ROS into less reactive molecules using these redox‐related enzymes during infection. However, it remains unclear whether Sods and Ahp(s) also play a role in pathogenesis. In this project, we set out to1) Clone and express sodA, sodB and sodC genes in E. coli, 2) Perform pathogenicity assay with the sodC mutant, and 3) Generate deletion mutants lacking both AhpC and AhpF. We successfully cloned the sodA, sodB and sodC genes using plasmid pLN615, and verified their authenticity by immunoblot of the expression extract. Pathogenicity assays revealed that the sodC mutant did not show significant differences in virulence from the wild type strain DC3000 in Arabidopsis plants. This suggests that the sodC gene may be redundant with the sodA and sodB in DC3000. We were also successful in generating P. syringae mutant lacking both AhpC and AhpF using an unmarked mutagenesis approach. Grant Funding Source : NSF