Stimulation of target gene transcription by human p53 is inhibited in budding yeast lacking the TRR1 gene encoding thioredoxin reductase. LexA/p53 fusion proteins were used to study the basis for thioredoxin reductase dependence. A fusion protein containing all 393 of the residues of p53 efficiently and specifically stimulated transcription of a LexOP-LacZ reporter gene in wild-type yeast but w...

Stimulation of target gene transcription by human p53 is inhibited in budding yeast lacking the TRR1 gene encoding thioredoxin reductase. LexA/p53 fusion proteins were used to study the basis for thioredoxin reductase dependence. A fusion protein containing all 393 of the residues of p53 efficiently and specifically stimulated transcription of a LexOPLacZ reporter gene in wild-type yeast but wa...

Escherichia coli B contains a cytidine diphosphate reductase system which utilizes reduced triphosphopyridine nucleotide to effect the reduction of cytidine diphosphate to deoxycytidine diphosphate (1, 2). Two components, thioredoxin and thioredoxin reductase, have been identified as oxidation-reduction carriers between TPNH and cytidine diphosphate. Thioredoxin is a low molecular weight protei...

Activity of the cysteine adducts of the cysteine proteinases papain and thaumatopain can be recovered by treatment with thioredoxin, thioredoxin reductase and NADPH. Recovery of proteinase activity did not occur if any of the components of the thioredoxin system were omitted, or if thioredoxin or thioredoxin reductase were heat-inactivated. Such an enzyme-mediated process may be of significance...

The active site sequence of T4 thioredoxin, Cys-Val-Tyr-Cys, has been modified in two positions to Cys-Gly-Pro-Cys to mimic that of Escherichia coli thioredoxin. The two point mutants Cys-Gly-Tyr-Cys and Cys-Val-Pro-Cys have also been constructed. The mutant proteins have similar reaction rates with T4 ribonucleotide reductase as has the wild-type T4 thioredoxin. Mutant T4 thioredoxins with Pro...

Thioredoxin reductase (TrxR) is a central component in the thioredoxin system by involving catalyzing reduction of thioredoxin, which critical for organism survival. Because this essential, it promising target novel antimicrobial agents. Herein, we solved 1.9 Å high‐resolution structure TrxR from Acinetobacter baumannii ( Ab TrxR), Gram‐negative, pathogenic bacterium and drug‐resistant superbug...

Understanding how pathogenic fungi adapt to host plant cells is of major concern to securing global food production. The hemibiotrophic rice blast fungus Magnaporthe oryzae, cause of the most serious disease of cultivated rice, colonizes leaf cells asymptomatically as a biotroph for 4-5 days in susceptible rice cultivars before entering its destructive necrotrophic phase. During the biotrophic ...

A thioredoxin reductase and a thioredoxin were purified to homogeneity from a cell extract of Thermotoga maritima. The thioredoxin reductase was a homodimeric flavin adenine dinucleotide (FAD)-containing protein with a subunit of 37 kDa estimated using SDS-PAGE, which was identified to be TM0869. The amino acid sequence of the enzyme showed high identities and similarities to those of typical b...

Malaria parasites adapt to the oxidative stress during their erythrocytic stages with the help of vital thioredoxin redox system and glutathione redox system. Glutathione reductase and thioredoxin reductase are important enzymes of these redox systems that help parasites to maintain an adequate intracellular redox environment. In the present study, activities of glutathione reductase and thiore...

Mitochondrial thioredoxin-glutathione reductase was purified from larval Taenia crassiceps (cysticerci). The preparation showed NADPH-dependent reductase activity with either thioredoxin or GSSG, and was able to perform thiol/disulfide exchange reactions. At 25 degrees C specific activities were 437 +/- 27 mU mg(-1) and 840 +/- 49 mU mg(-1) with thioredoxin and GSSG, respectively. Apparent K(m)...