Abstract
S-nitrosation has been recognized as an important mechanism of ubiquitous posttranslational modification of proteins on the basis of the attachment of the nitroso group to cysteine thiols. Reversible S-nitrosation, similarly to other redox-based modifications of protein thiols, has a profound effect on protein structure and activity and is considered as a convergence of signaling pathways of reactive nitrogen and oxygen species. This review summarizes the current knowledge on the emerging role of the thioredoxin-thioredoxin reductase (TRXR-TRX) system in protein denitrosation. Important advances have been recently achieved on plant thioredoxins (TRXs) and their properties, regulation, and functions in the control of protein S-nitrosation in plant root development, translation of photosynthetic light harvesting proteins, and immune responses. Future studies of plants with down- and upregulated TRXs together with the application of genomics and proteomics approaches will contribute to obtain new insights into plant S-nitrosothiol metabolism and its regulation.
Highlights
Protein posttranslational modifications (PTMs) evolved as a mechanism to expand the coding capacity of eukaryotic genomes to generate an enormous diversity of corresponding proteomes.PTMs comprise highly divergent forms of protein modifications, including covalent additions of small or complex chemical groups or polypeptides to protein side chains, chemical modifications of amino acids, or proteolytic cleavage
We focus on the regulatory mechanisms of protein S-nitrosation and denitrosation within Nitric oxide (NO) signaling in plants
NO and the TRX system show a complex interplay within the redox regulation of mammalian cells, where TRXs play an active role in attenuating NO signaling and responses to nitrosative stress, whereas NO reciprocally modulates the redox activity of TRX and thioredoxin reductase (TRXR)
Summary
Protein posttranslational modifications (PTMs) evolved as a mechanism to expand the coding capacity of eukaryotic genomes to generate an enormous diversity of corresponding proteomes. PTMs regulates the rates of key metabolic processes of photosynthesis, respiration, photorespiration, and glycolysis [3] Besides their role in plant development and growth, multiple PTMs regulate proteins involved in plant responses to stress conditions [4,5]. We review how other systems of redox control, including peroxiredoxins, sulfiredoxins, and S-nitrosoglutathione reductase (GSNOR) complement the specific functions of cytosolic thioredoxins (TRXs) in protein denitrosation in plants. These highly conserved enzymes regulate multiple NO-dependent signaling pathways, protect plants from nitrosative stress conditions, and play crucial roles in plant immunity to microbial pathogens
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