Abstract
Reactive oxygen species (ROS) are engaged in several processes essential for normal cell functioning, such as differentiation, anti-microbial defense, stimulus sensing and signaling. Interestingly, recent studies imply that cellular signal transduction and gene regulation are mediated not only directly by ROS but also by the molecules derived from ROS-mediated oxidation. Lipid peroxidation leads to non-enzymatic formation of oxylipins. These molecules were shown to modulate expression of signaling associated genes including genes encoding phosphatases, kinases and transcription factors. Oxidized peptides derived from protein oxidation might be engaged in organelle-specific ROS signaling. In turn, oxidation of particular mRNAs leads to decrease in the level of encoded proteins and thus, contributes to the post-transcriptional regulation of gene expression. Present mini review summarizes latest findings concerning involvement of products of lipid, protein and RNA oxidation in signal transduction and gene regulation.
Highlights
It is well established that reactive oxygen species (ROS) are engaged in the cellular signal transduction network (Neill et al, 2002; Ślesak et al, 2007; Wrzaczek et al, 2013)
It has been suggested that oxidation of cellular compounds leads to the formation of new signaling molecules: non-enzymatically formed oxylipins, peptides derived from Reactive oxygen species (ROS)-dependent protein degradation and oxidatively modified mRNAs
It has been shown that 24% of the genes in Arabidopsis up-regulated by PP are related to signal transduction, including transcription factors, phosphatases and kinases (Mueller et al, 2008)
Summary
It is well established that reactive oxygen species (ROS) are engaged in the cellular signal transduction network (Neill et al, 2002; Ślesak et al, 2007; Wrzaczek et al, 2013). Changes in ROS level affect oxidative status of redox-sensitive signal regulators such as ascorbate, glutathione and thioredoxins, leading to modulation of metabolism and gene expression. Thiol switches were shown to regulate various cellular processes including translation, transcription and signaling (Brandes et al, 2009; Dietz and Hell, 2015). Changes in cellular redox status affects disulfide bonds in proteins associated with transcription, leading to the alterations in their polymerization and DNA binding capacity (Chi et al, 2013).
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