NDLI: Redox Protein Characterization and Quantification Using ICAT-MS to Investigate Thiol-based Regulatory Mechanisms Induced by Oxidative Stress in Plants

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Redox Protein Characterization and Quantification Using ICAT-MS to Investigate Thiol-based Regulatory Mechanisms Induced by Oxidative Stress in Plants

Content Provider	PubMed Central
Author	Alvarez, Sophie Hicks, Leslie M. Liu, Zhenjiu
Copyright Year	2012
Abstract	Reactive oxygen species (ROS) and reactive nitrogen species (RNS) are ubiquitously found in living cells and increase during biotic or abiotic stresses. It has been shown that reversible oxidation of selective protein residues may serve as redox sensors and signal transducers for conveying cellular anti-stress responses. The thiol group on cysteine residues is particularly sensitive to oxidative species and can be oxidized into a disulfide bond to modulate protein function. Disulfide bonds can be reversibly reduced back to the free thiol group in the presence of a mild reducing agent. Isotope-coded affinity tag (ICAT) reagents specifically react with the thiol group of cysteine residues, and we are developing this approach coupled with mass spectrometry to quantify the thiol-containing redox proteins by measuring ICAT-labeled peptide intensities. The thiol-based redox regulatory mechanisms induced by oxidative stress in plants were investigated in response to exogenous oxidative species treatment. Following protein extraction from control and treated plants, the free thiol groups were first blocked, then the disulfide bonds were reduced back to free thiols. ICAT labeling of the free thiols was performed on the samples to quantify the redox sensitive cysteine-containing peptides. To confirm the specificity of the redox changes observed, relative protein abundance was also monitored using an iTRAQ labeling approach on the same samples. Methodological considerations and analysis of the redox state of proteins are presented.
Starting Page	54
File Format	PDF
ISSN	19434731
e-ISSN	19434731
Journal	Journal of Biomolecular Techniques : JBT
Issue Number	Suppl
Volume Number	23
Language	English
Publisher	Association of Biomolecular Resource Facilities
Publisher Date	2012-01-01
Access Restriction	Open
Rights Holder	Association of Biomolecular Resource Facilities
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article

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