About this Research Topic
Owing to their lack of mobility and to the existence of a photosynthetic metabolism generating high amount of reactive oxygen species (ROS), plants imperatively have to cope with adverse conditions. Although plant redox homeostasis is mainly preserved by the cellular glutathione pool, specific strategies have been adopted by plant kingdom during evolution to manage these “extra” pro-oxidant conditions. Unlike human or yeast, plants generally possess a higher number of genes coding for antioxidant proteins, including protein families responsible of dithiol/disulfide exchange reactions.
Thiol groups of cysteinyl residues are highly sensitive to oxidation which might critically perturb cellular homeostasis. Members of the thioredoxin superfamily are key proteins involved in the regulation of cysteine/protein redox state. They share two common and well-known features: (i) the presence of an active center containing at least one catalytic cysteine residue and also, (ii) a highly conserved 3D-structure, namely the thioredoxin fold. It consists of a four-stranded anti-parallel beta sheet surrounded by three alpha helices. All members of this superfamily as Thioredoxins (TRX), Glutaredoxins (GRX), Protein Disulfide Isomerases (PDI), Thiol Peroxidases (TPX) or Glutathione-S-Transferases (GST) display at least one TRX motif in their structures. During the last decades and nowadays, major advances have shown that redox control, usually achieved through post-translational modifications of proteins, is pivotal to many if not all cellular functions. In particular, this is critically important under some situations of environmental constraints taking into account the alterations and fine adjustment of the cell redox status occurring during and after any biotic or abiotic stresses.
This Research Topic will provide an overview on the new insights about redox control, regulation or signalling in plants, focusing on glutathione and proteins of the thioredoxin superfamily. We welcome high-quality contributions that fit within this framework with all types of articles, such as original research articles, method articles, reviews, mini-reviews or perspective articles, all of them from the widest point of view (molecular, cellular, structural, …).
Thiol groups of cysteinyl residues are highly sensitive to oxidation which might critically perturb cellular homeostasis. Members of the thioredoxin superfamily are key proteins involved in the regulation of cysteine/protein redox state. They share two common and well-known features: (i) the presence of an active center containing at least one catalytic cysteine residue and also, (ii) a highly conserved 3D-structure, namely the thioredoxin fold. It consists of a four-stranded anti-parallel beta sheet surrounded by three alpha helices. All members of this superfamily as Thioredoxins (TRX), Glutaredoxins (GRX), Protein Disulfide Isomerases (PDI), Thiol Peroxidases (TPX) or Glutathione-S-Transferases (GST) display at least one TRX motif in their structures. During the last decades and nowadays, major advances have shown that redox control, usually achieved through post-translational modifications of proteins, is pivotal to many if not all cellular functions. In particular, this is critically important under some situations of environmental constraints taking into account the alterations and fine adjustment of the cell redox status occurring during and after any biotic or abiotic stresses.
This Research Topic will provide an overview on the new insights about redox control, regulation or signalling in plants, focusing on glutathione and proteins of the thioredoxin superfamily. We welcome high-quality contributions that fit within this framework with all types of articles, such as original research articles, method articles, reviews, mini-reviews or perspective articles, all of them from the widest point of view (molecular, cellular, structural, …).
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