Modulating protein function through reversible oxidation: Redox-mediated processes in plants revealed through proteomics.

Bykova, N.V. and Rampitsch, C. (2013). "Modulating protein function through reversible oxidation: Redox-mediated processes in plants revealed through proteomics.", Proteomics, 13(3-4), pp. 579-596. doi : 10.1002/pmic.201200270  Access to full text

Abstract

It has been clearly demonstrated that plants redox control can be exerted over virtually every cellular metabolic pathway affecting metabolic homeostasis and energy balance. Therefore, a tight link exists between cellular/compartmental steady-state redox level and cellular metabolism. Proteomics offers a powerful new way to characterize the response and regulation of protein oxidation in different cell types and in relation to cellular metabolism. Compelling evidence revealed in proteomics studies suggests the integration of the redox network with other cellular signaling pathways such as Ca2+ and/or protein phosphorylation, jasmonic, salicylic, abscisic acids, ethylene, and other phytohormones. Here we review progress in using the various proteomics techniques and approaches to answer biological questions arising from redox signaling and from changes in redox status of the cell. The focus is on reversible redox protein modifications and on three main processes, namely oxidative and nitrosative stress, defense against pathogens, cellular redox response and regulation, drawing on examples from plant redox proteomics studies.

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