Thioredoxins articles from across Nature Portfolio

The DNA binding and H₂O₂ sensing mechanisms are revealed for RexT, a transcriptional regulator found in cyanobacteria of the Nostocales order.

Peroxiredoxin 2 (Prx2) was previously shown to transfer H₂O₂-derived oxidative equivalents to STAT3, generating disulfide-linked dimers and tetramers. Here the authors show that the interaction between Prx2 and STAT3 at the plasma membrane is mediated by the membrane chaperone annexin A2; suggesting that the redox relay complex is part of a membrane signaling domain.

Glutaredoxins play a central role in numerous biological processes including cellular redox homeostasis and Fe-S cluster biogenesis. Here the authors establish the molecular basis for glutaredoxin redox catalysis through comprehensive biochemical and structural analyses.

Thioredoxin reductase (TrxR) plays a crucial part in regulating cellular redox homeostasis. Here, the authors developed a fluorescent probe composed of a five-membered disulphide, a coumarin fluorophore and a urea linker that detects TrxR activity with fast response and high selectivity.