Thioredoxins are small proteins of approximately 12 kD that reduce disulfide bridges of target proteins by the reversible formation of a disulfide bridge between two neighboring Cys residues present in the active site (Try-Cys-Gly-Pro-Cys). Thioredoxins have been found to regulate a variety of biological reactions in prokaryotic and eukaryotic cells (Holmgren, 1985). In higher plants, two thior...

background: thioredoxin reductase 1 (txnrd1) and thioredoxin interacting protein (txnip) also known as thioredoxin binding protein 2 or vitamin d3-upregulated protein 1 are key players in oxidative stress control. thioredoxin (trx) is one of the major components of the thiol reducing system and plays multiple roles in cellular processes. computational analyses of txnrd1, txnip and trx expressio...

Thioredoxins (TRXs) are protein oxidoreductases that control the structure and function of cellular proteins by cleavage of a disulphide bond between the side chains of two cysteine residues. Oxidized thioredoxins are reactivated by thioredoxin reductases (TR) and a TR-dependent reduction of TRXs is called a thioredoxin system. Thiol-based redox regulation is an especially important mechanism t...

Thioredoxins are small soluble proteins that contain a redox-active disulfide (CXXC). These disulfides are tuned to oxidizing or reducing potentials depending on the function of the thioredoxin within the cell. The mechanism by which the potential is tuned has been controversial, with two main hypotheses: first, that redox potential (Em) is specifically governed by a molecular 'rheostat'-the XX...

Thioredoxins are small thiol-oxidoreductase enzymes that control cellular redox homeostasis. Paradoxically, human thioredoxin (TXN1) was first identified as the adult T cell leukemia-derived factor (ADF), a secreted protein. ADF has been implicated in a wide variety of cell-to-cell communication systems acting as a cytokine or a chemokine. TRX80 is a truncated TXN1 protein with cytokine activit...

The disruption of the two thioredoxin genes in Saccharomyces cerevisiae leads to a complex phenotype, including the inability to use methionine sulfoxide as sulfur source, modified cell cycle parameters, reduced H(2)O(2) tolerance, and inability to use sulfate as sulfur source. Expression of one of the multiple Arabidopsis thaliana thioredoxins h in this mutant complements only some aspects of ...