Redox proteomics: basic principles and future perspectives for the detection of protein oxidation in plants

Abstract

The production and scavenging of chemically reactive species, such as ROS/RNS, are central to a broad range of biotic and abiotic stress and physiological responses in plants. Among the techniques developed for the identification of oxidative stress-induced modifications on proteins, the so-called 'redox proteome', proteomics appears to be the best-suited approach. Oxidative or nitrosative stress leaves different footprints in the cell in the form of different oxidatively modified components and, using the redox proteome, it will be possible to decipher the potential roles played by ROS/RNS-induced modifications in stressed cells. The purpose of this review is to present an overview of the latest research endeavours in the field of plant redox proteomics to identify the role of post-translational modifications of proteins in developmental cell stress. All the strategies set up to analyse the different oxidized/nitrosated amino acids, as well as the different reactivities of ROS and RNS for different amino acids are revised and discussed. A growing body of evidence indicates that ROS/RNS-induced protein modifications may be of physiological significance, and that in some cellular stresses they may act causatively and not arise as a secondary consequence of cell damage. Thus, although previously the oxidative modification of proteins was thought to represent a detrimental process in which the modified proteins were irreversibly inactivated, it is now clear that, in plants, oxidatively/nitrosatively modified proteins can be specific and reversible, playing a key role in normal cell physiology. In this sense, redox proteomics will have a central role in the definition of redox molecular mechanisms associated with cellular stresses.

Chitooligosaccharide Prolongs Vase Life of Cut Roses by Decreasing Reactive Oxygen Species

“…With the exception of the plant organelles, other main sources of ROS were peroxidases and oxidases in plants (Rinalducci et al, 2008). In mature petals of cut rose, the chloroplast is common to be disappeared, disintegrated or transformed to other components (Rogers, 2012).…”

“…), will oxidize nearby biological macromolecules including DNA, proteins or lipids (Bokov et al, 2004;Rinalducci et al, 2008;Jing et al, 2011;Rogers, 2012) which can be damaging or even fatal for the cell (Mittler, 2002). Malondialdehyde (MDA) is formed by oxidative damage of lipids which lead to membrane lipid mobility worse.…”

Hole hopping through tyrosine/tryptophan chains protects proteins from oxidative damage

“…The side chains of select amino acids also can serve as waystations for redox hopping reactions, with Cys, Met, Trp, and Tyr being the most likely candidates (18). Hole transfer reactions are more common in Tyr and Trp, whereas Cys and Met tend to undergo two-electron bond-making/breaking transformations (4,19). Clusters of Tyr and Trp residues, therefore, could act as conduits for high-potential holes in proteins.…”

A quick incorporation of13N into the soluble high-molecular compound in rice (Oryza sativaL.) roots by application of13N-labeled nitrate/nitrite

“…Nitrite oxide may also bind to protein cysteine residues or to the transition metals (iron and copper) of metalloproteins: such reactions are known as nitrosylation (Wang et al 2006). Both the nitration and nitrosylation of proteins are post-translational, and may regulate the activity of a wide variety of proteins from iron channels to transcription factors (Wang et al 2006;Rinalducci et al 2008). Techniques to identify nitrated and nitrosylated proteins must be developed (Camerini et al 2007), and a method of identifying specific 13 N-labelled HMC(s) is essential in order to search for the protein(s) that participate in signal transduction in the nitrate/nitrite response.…”