Revising the roles of phytochelatin synthases and their evolutionary history in different plant species
TL;DRAbstract
The cytosolic enzyme phytochelatin synthase (PCS) is constitutively expressed and it has been studied for its role in metal(loid) detoxification in different organisms. It has been recognized that PCS enzymes detoxify Cd or other toxic heavy metals by catalysing the formation of thiol rich polymers, namely phytochelatins (PCs), from glutathione (GSH) and related thiols. PCs bind several metal(loid)s with high affinity and facilitate their sequestration into the vacuole mainly via ABC transporters.\nOther papers have reported another role played by the PCS enzyme, PCS is in fact also involved in the catabolism of glutathione-conjugates, catalysing the first reaction of degradation by the cleavage of glycine from the GS-conjugate, to generate a γ-EC-conjugate, without PC production.\nFurthermore, the transcript abundance of AtPCS1 (from the model plant Arabidopsis thaliana) increases under Fe deficiency and after treatment with a mimetic signal of a pathogen attack, a synthetic 22-amino
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The cytosolic enzyme phytochelatin synthase (PCS) is constitutively expressed and it has been studied for its role in metal(loid) detoxification in different organisms. It has been recognized that PCS enzymes detoxify Cd or other toxic heavy metals by catalysing the formation of thiol rich polymers, namely phytochelatins (PCs), from glutathione (GSH) and related thiols. PCs bind several metal(loid)s with high affinity and facilitate their sequestration into the vacuole mainly via ABC transporters.\nOther papers have reported another role played by the PCS enzyme, PCS is in fact also involved in the catabolism of glutathione-conjugates, catalysing the first reaction of degradation by the cleavage of glycine from the GS-conjugate, to generate a γ-EC-conjugate, without PC production.\nFurthermore, the transcript abundance of AtPCS1 (from the model plant Arabidopsis thaliana) increases under Fe deficiency and after treatment with a mimetic signal of a pathogen attack, a synthetic 22-amino
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