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Journal of Experimental Botany 2008 59(14):3781-3801; doi:10.1093/jxb/ern252
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© The Author [2008]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

REVIEW-ARTICLE

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

Sara Rinalducci, Leonardo Murgiano and Lello Zolla*

Department of Environmental Sciences, University of Tuscia, Largo dell'Università snc, I-01100, Viterbo, Italy

* To whom correspondence should be addressed: E-mail: zolla{at}unitus.it

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.

Key words: Oxidative damage, oxidized/nitrosated amino acids, plant redox proteomics, protein oxidation, reactive oxygen species, reactive nitrogen species, redox regulation, stress

Received 7 July 2008; Revised 12 September 2008 Accepted 16 September 2008


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