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    Proteomic identification of early salicylate- and flg22-responsive redox-sensitive proteins in Arabidopsis

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    Type
    Article
    Authors
    Liu, Peng
    Zhang, Huoming cc
    Yu, Boying
    Xiong, Liming cc
    Xia, Yiji
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Core Lab
    Plant Science
    Plant Stress Genomics Research Lab
    Date
    2015-02-27
    Online Publication Date
    2015-02-27
    Print Publication Date
    2015-08
    Permanent link to this record
    http://hdl.handle.net/10754/346701
    
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    Abstract
    Accumulation of reactive oxygen species (ROS) is one of the early defense responses against pathogen infection in plants. The mechanism about the initial and direct regulation of the defense signaling pathway by ROS remains elusive. Perturbation of cellular redox homeostasis by ROS is believed to alter functions of redox-sensitive proteins through their oxidative modifications. Here we report an OxiTRAQ-based proteomic study in identifying proteins whose cysteines underwent oxidative modifications in Arabidopsis cells during the early response to salicylate or flg22, two defense pathway elicitors that are known to disturb cellular redox homeostasis. Among the salicylate- and/or flg22-responsive redox-sensitive proteins are those involved in transcriptional regulation, chromatin remodeling, RNA processing, post-translational modifications, and nucleocytoplasmic shuttling. The identification of the salicylate-/flg22-responsive redox-sensitive proteins provides a foundation from which further study can be conducted toward understanding biological significance of their oxidative modifications during the plant defense response.
    Citation
    Proteomic identification of early salicylate- and flg22-responsive redox-sensitive proteins in Arabidopsis 2015, 5:8625 Scientific Reports
    Publisher
    Springer Nature
    Journal
    Scientific Reports
    DOI
    10.1038/srep08625
    PubMed ID
    25720653
    PubMed Central ID
    PMC4342551
    Additional Links
    http://www.nature.com/doifinder/10.1038/srep08625
    ae974a485f413a2113503eed53cd6c53
    10.1038/srep08625
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Core Lab

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