Mycobacteriophage L5 gene 56 encodes a putative thioredoxin family protein. Phylogenetic analysis revealed that Gp56 and related proteins are distantly related to NrdH - a glutaredoxin homolog which has thioredoxin-like properties. To understand its function, the recombinant version of the protein was biochemically characterized. For the sake of comparison, a mycobacterial thioredoxin, TrxB, wa...

PPARalpha, a member of the nuclear receptor superfamily, and thioredoxin, a critical redox-regulator in cells, were found to form a negative feedback loop, which autoregulates transcriptional activity of PPARalpha. Thioredoxin was identified as a target gene of PPARalpha. Activation of PPARalpha leads to increase of thioredoxin expression as well as its translocation from cytoplasm to nucleus, ...

Mercury toxicity mediated by different forms of mercury is a major health problem, however, the molecular mechanisms underlying toxicity remains elusive. We analyzed effects of mercuric chloride (HgCl2) and monomethylmercury (MeHg) on the proteins of the mammalian thioredoxin system, thioredoxin reductase (TrxR) and thioredoxin (Trx), and of the glutaredoxin system, glutathione reductase (GR) a...

Two genes encoding thioredoxin are found on the Escherichia coli genome. Both of them are capable of reducing protein disulfide bonds in vivo and in vitro. The catalytic site contains a Cys-X(1)-X(2)-Cys motif in a so-called thioredoxin fold. Thioredoxin 2 has two additional pairs of cysteines in a non-conserved N-terminal domain. This domain does not appear to be important for the function of ...

Escherichia coli thioredoxin is a redox-active protein. A mutant protein with an aspartic acid substitution for the largely conserved glycine at position 33 (G33D) in the active site of thioredoxin has been generated to study the effects of a negatively charged residue in the active site of the protein. Despite the close proximity of the negative-charged Asp to the redox active cysteines, the e...

Thioredoxin is a small multifunctional protein which acts as a dithiol hydrogen donor for ribonucleotide reductase in DNA synthesis. Thioredoxin participates in the regulation of different metabolic processes, such as changes in the activity of different enzymes, receptors or transcription factors. The aim of the present study was to determine possible differences in the expression of thioredox...

The thioredoxin system is a key cellular antioxidant system and is highly expressed in cancer cells, especially in more aggressive and therapeutic resistant tumors. We analysed the expression of the thioredoxin system in the MDA-MB-231 breast cancer cell line under conditions mimicking the tumor oxygen microenvironment. We grew breast cancer cells in either prolonged hypoxia or hypoxia followed...