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dc.contributor.authorLiu, Pei-Nian
dc.contributor.authorZhang, Huoming
dc.contributor.authorWang, Hai
dc.contributor.authorXia, Yiji
dc.date.accessioned2015-08-03T11:46:34Z
dc.date.available2015-08-03T11:46:34Z
dc.date.issued2014-01-28
dc.identifier.citationLiu, P., Zhang, H., Wang, H., & Xia, Y. (2014). Identification of redox-sensitive cysteines in the Arabidopsis proteome using OxiTRAQ, a quantitative redox proteomics method. PROTEOMICS, 14(6), 750–762. doi:10.1002/pmic.201300307
dc.identifier.issn16159853
dc.identifier.pmid24376095
dc.identifier.doi10.1002/pmic.201300307
dc.identifier.urihttp://hdl.handle.net/10754/563356
dc.description.abstractCellular redox status plays a key role in mediating various physiological and developmental processes often through modulating activities of redox-sensitive proteins. Various stresses trigger over-production of reactive oxygen/nitrogen species which lead to oxidative modifications of redox-sensitive proteins. Identification and characterization of redox-sensitive proteins are important steps toward understanding molecular mechanisms of stress responses. Here, we report a high-throughput quantitative proteomic approach termed OxiTRAQ for identifying proteins whose thiols undergo reversible oxidative modifications in Arabidopsis cells subjected to oxidative stress. In this approach, a biotinylated thiol-reactive reagent is used for differential labeling of reduced and oxidized thiols. The biotin-tagged peptides are affinity purified, labeled with iTRAQ reagents, and analyzed using a paralleled HCD-CID fragmentation mode in an LTQ-Orbitrap. With this approach, we identified 195 cysteine-containing peptides from 179 proteins whose thiols underwent oxidative modifications in Arabidopsis cells following the treatment with hydrogen peroxide. A majority of those redox-sensitive proteins, including several transcription factors, were not identified by previous redox proteomics studies. This approach allows identification of the specific redox-regulated cysteine residues, and offers an effective tool for elucidation of redox proteomes. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
dc.description.sponsorshipThis work was supported by Research Grants Council of Hong Kong (grant nos. HKBU1/CRF/10 and HKBU261910 to Y.X.) and by HKBU Strategic Development Fund (to Y.X.).
dc.publisherWiley
dc.subjectArabidopsis thaliana
dc.subjectITRAQ
dc.subjectOxidative stress
dc.subjectOxiTRAQ
dc.subjectPlant proteomics
dc.subjectRedox-sensitive protein
dc.subjectRedoxome
dc.titleIdentification of redox-sensitive cysteines in the arabidopsis proteome using OxiTRAQ, a quantitative redox proteomics method
dc.typeArticle
dc.contributor.departmentBioscience Core Lab
dc.identifier.journalPROTEOMICS
dc.contributor.institutionDepartment of Biology, Hong Kong Baptist University, Hong Kong, China
dc.contributor.institutionPartner State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Hong Kong, China
kaust.personZhang, Huoming
dc.date.published-online2014-01-28
dc.date.published-print2014-03


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