Research update
Nanotransducers in cellular redox signaling: modification of thiols by reactive oxygen and nitrogen species

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Abstract

The control of signal transduction involves post-translational modification of proteins at key amino acids. Cysteine residues are important in the control of ‘redox’ cell-signaling pathways, as thiol chemistry offers the possibility of modification by structurally diverse species, including those derived from oxidized lipids, peroxides or nitric oxide. An important and provocative study of the modification of thiols in the transcription factor OxyR recently extended this hypothesis. The findings offer the enticing possibility that the cell can distinguish between different degrees of oxidant and nitrosative exposure by modification at a single site on a signaling molecule.

Section snippets

Transduction of ROS and RNS signaling by protein thiols

The idea that cysteine can be specifically modified to form S-nitrosothiol species (RSNO) has long been advocated by Jonathan Stamler's group (Duke University, NC, USA) as a signaling pathway of major importance 9., 10.. In the recent paper discussed here, they extend this concept to a range of different modifications of cysteine residues [10]. The claim advanced is that this allows an individual enzyme to have a graded response to diverse effectors (signals) by differential modification of a

Summary

This work offers a new paradigm for redox cell signaling and the potential for cross talk between several molecular mechanisms of redox signaling (as detailed in Box 2). Simple on/off (digital) signals are unable to transduce a single input function into a smoothly graded response. In complex pathways this can be achieved by multi-site modulation and simultaneous activation of many steps, resulting in a graded response whether the substrates are metabolites or signaling molecules. In this case,

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    Cys, an essential amino acid, has various vital functions, from joining the structure of proteins to sustaining redox stability (Romero et al., 2014). As a result of containing thiol groups, Cys can easily react with reactive oxygen species besides bonding to metals, and can therefore inactivate them and protect plants against the exposed stress (Cooper et al., 2002; Genisel et al., 2015). In the literature, there are a limited number of studies focusing on the effect of Cys applied exogenously to plants exposed to abiotic stress.

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