Photosynthetic organisms have a high diversity of proteins belonging to the thioredoxin (TRX) superfamily. It comprises more than 150 proteins distributed in different families and classes, including in particular thioredoxins, glutaredoxins, protein disulfide isomerases, thiol peroxidases or glutathione transferases, which share the TRX structural fold. Many of them have one or two redox-active cysteines and a characteristic cis-proline at specific positions, but also additional domains or secondary structures at either end or inserted into the protein core. With the aim of further describing the TRX superfamily in plants, we identified a set of 17 atypical TRX-like proteins from Arabidopsis thaliana, which have not been considered before. The in silico analyses revealed that they differ by their active-site signature and structural
features and that they are spread in eight distinct classes. To delineate the possible functions of these novel TRX-like proteins, we combined biochemical and structural analyses of recombinant proteins together with cellular approaches to determine their subcellular localizations. Recent data obtained on specific representatives will be presented.
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