Abstract
Reversible and irreversible post-translational modifications (PTMs) induced by endogenously generated reactive oxygen species (ROS) in regulatory enzymes and proteins plays an essential role in cellular signaling. Almost all cellular processes including metabolism, transcription, translation and degradation have been identified as containing redox regulated proteins. Specific redox modifications of key amino acids generated by ROS offers a dynamic and versatile means to rapidly alter the activity or functional structure of proteins in response to biochemical, environmental, genetic and pathological perturbations. How the proteome responds to these stimuli is of critical importance in oxidant physiology, as it can regulate the cell stress response by reversible and irreversible PTMs, affecting protein activity and protein-protein interactions. Due to the highly labile nature of many ROS species, applying redox proteomics can provide a signature footprint of the ROS species generated. Ideally redox proteomic approaches would allow; (1) the identification of the specific PTM, (2) identification of the amino acid residue that is modified and (3) the percentage of the protein containing the PTM. New developments in MS offer the opportunity of a more sensitive targeted proteomic approach and retrospective data analysis. Subsequent bioinformatics analysis can provide an insight into the biochemical and physiological pathways or cell signaling cascades that are affected by ROS generation. This mini-review will detail current redox proteomic approaches to identify and quantify ROS induced PTMs and the subsequent effects on cellular signaling.
Highlights
The specific reduction or oxidation of critical enzymes/proteins as a result of endogenously generated reactive oxygen or reactive nitrogen species (ROS/RNS) can alter the metabolic flux within a cell
S-nitrosylation on target proteins is considered an important mechanism for nitrogen monoxide (NO) signaling transduction and there are a large number of articles identifying specific Cysteine residues as Snitrosylation targets in a variety of cellular systems from plants to cardiovascular systems (Hess et al, 2005), as this post-translational modifications (PTMs) is reversible and highly labile PTM it has been suggested as an intermediate in the formation of disulphide bonds (Wolhuter and Eaton, 2017)
Nitration of tyrosine amino acids is considered a signature of excessive ONOO− and/or NO generation, the subset of Tyrosine residues available for nitration is generally considered to be low and the number of proteins detected to be nitrated (Tyther et al, 2011; Batthyany et al, 2017)
Summary
Reversible and irreversible post-translational modifications (PTMs) induced by endogenously generated reactive oxygen species (ROS) in regulatory enzymes and proteins plays an essential role in cellular signaling. How the proteome responds to these stimuli is of critical importance in oxidant physiology, as it can regulate the cell stress response by reversible and irreversible PTMs, affecting protein activity and protein-protein interactions. Subsequent bioinformatics analysis can provide an insight into the biochemical and physiological pathways or cell signaling cascades that are affected by ROS generation. This mini-review will detail current redox proteomic approaches to identify and quantify ROS induced PTMs and the subsequent effects on cellular signaling
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