Cysteines under ROS attack in plants: a proteomics view.

TitleCysteines under ROS attack in plants: a proteomics view.
Publication TypeJournal Article
Year of Publication2015
AuthorsAkter, S., J. Huang, C. Waszczak, S. Jacques, K. Gevaert, F. Van Breusegem, and J. Messens
JournalJ Exp Bot
Volume66
Issue10
Pagination2935-44
Date Published2015 May
ISSN1460-2431
KeywordsCysteine, Oxidation-Reduction, Plant Physiological Phenomena, Plant Proteins, Proteome, Reactive Oxygen Species, Signal Transduction
Abstract

Plants generate reactive oxygen species (ROS) as part of their metabolism and in response to various external stress factors, potentially causing significant damage to biomolecules and cell structures. During the course of evolution, plants have adapted to ROS toxicity, and use ROS as signalling messengers that activate defence responses. Cysteine (Cys) residues in proteins are one of the most sensitive targets for ROS-mediated post-translational modifications, and they have become key residues for ROS signalling studies. The reactivity of Cys residues towards ROS, and their ability to react to different oxidation states, allow them to appear at the crossroads of highly dynamic oxidative events. As such, a redox-active cysteine can be present as S-glutathionylated (-SSG), disulfide bonded (S-S), sulfenylated (-SOH), sulfinylated (-SO2H), and sulfonylated (-SO3H). The sulfenic acid (-SOH) form has been considered as part of ROS-sensing pathways, as it leads to further modifications which affect protein structure and function. Redox proteomic studies are required to understand how and why cysteines undergo oxidative post-translational modifications and to identify the ROS-sensor proteins. Here, we update current knowledge of cysteine reactivity with ROS. Further, we give an overview of proteomic techniques that have been applied to identify different redox-modified cysteines in plants. There is a particular focus on the identification of sulfenylated proteins, which have the potential to be involved in plant signal transduction.

DOI10.1093/jxb/erv044
Alternate JournalJ. Exp. Bot.
PubMed ID25750420
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