Disease relevance of trxA

• The redox protein and thioredoxin reductase retained their full activities for over 1h at 100 degrees C. The redox potential of the redox protein was similar to that of thioredoxin from E. coli and lower than that of glutathione [1].
• Thioredoxin system in obligate anaerobe Desulfovibrio desulfuricans: Identification and characterization of a novel thioredoxin 2 [2].
• The Thioredoxin Domain of Neisseria gonorrhoeae PilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases [3].
• Atomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter aceti [4].
• As thioredoxin 1 of Rhodobacter sphaeroides, R. capsulatus thioredoxin 2 affects the oxygen-dependent expression of photosynthesis genes, albeit in an opposite way [5].

High impact information on trxA

• The results indicate that thionein (T), which is formed when the zinc is removed from Zn-MT, can function as a reducing system for the Msr proteins because of its high content of cysteine residues and that Trx can reduce oxidized T [6].
• A heat-stable protein has been detected in bovine liver that, in the presence of EDTA, can support the Msr reaction in the absence of either Trx or DTT [6].
• Thus, we provide evidence that by changing the location of thioredoxin 1 from cytoplasm to periplasm, we change its function from a reductant to an oxidant [7].
• Recombinant B. subtilis SNR is a homodimer, which is bispecific and reduces adenylylsulfate (APS) and 3'-phosphoadenylylsulfate (PAPS) alike with thioredoxin 1 or with glutaredoxin 1 as reductants [8].
• Measurements of thymidine incorporation in newly synthesized DNA suggested that mainly Grx1 and, to a lesser extent, Trx1 contribute to the reduction of ribonucleotides [9].

Chemical compound and disease context of trxA

• Using Escherichia coli thioredoxin as a model protein, we show that potential binding sites can be identified using the Cu(2+) ion, and that pseudocontact shifts induced by a Ni(2+) ion bound to one of these sites can provide valuable long-range structure information about the protein [10].
• The crystal structure of thioredoxin (AaTrx) from the acetic acid bacterium Acetobacter aceti was determined at 1 A resolution [4].
• Thioredoxin 1 from E. coli, a small multifunctional dithiol protein, served as a sulfur acceptor substrate for GlpE with an apparent K(m) of 34 microM when thiosulfate was near its K(m), suggesting that thioredoxin 1 or related dithiol proteins could be physiological substrates for sulfurtransferases [11].
• Recombinant MxpSS1 produced in Escherichia coli, after removal of an N-terminal thioredoxin fusion, had a K(m) for FPP of 1.91+/-0.1 muM and k(cat) of 0.18 s(-1), and converted farnesyl diphosphate (FPP) into four products, the major two being cis-muurola-3,5-diene (45%) and cis-muurola-4(14),5-diene (43%) [12].

Biological context of trxA

• In silico analysis of the D. desulfuricans genome revealed the presence of thioredoxin 1 (dstrx1), thioredoxin 2 (dstrx2) and thioredoxin reductase (dstrxR) genes [2].
• While the exported thioredoxin 1 itself substantially speeds up the kinetics of disulfide bond formation, a version of this protein containing the DsbA active site exhibits kinetics that are indistinguishable from those of the DsbA protein itself [13].
• Each dimeric molecule contains two separate C-terminal thioredoxin-fold domains, joined by hinged helical ;stalks' to a single N-terminal dimerization domain formed from the N-terminal 67 residues of each monomer [14].
• This seems consistent with the hypothesis that GSTs constitute a protein superfamily that has evolved from a thioredoxin-like ancestor in response to the development of oxidative stress [15].
• The msp4 gene of an A. marginale strain isolated in Paran , Brazil, was amplified by PCR and sequenced; its cloning into the pET102/D-TOPO vector produced an msp4-6xHis-V5-HP thioredoxin fusion gene construct [16].

Anatomical context of trxA

• A cell-membrane fraction isolated from Escherichia coli overexpressing thioredoxin-tagged Alg2 was used to demonstrate that this enzyme actually carries out an alpha1,3-mannosylation, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the pathway [17].

Associations of trxA with chemical compounds

• The cloning of three full-length cDNAs encoding thioredoxin h, stated Trxh1, Trxh2 and Trxh3, from wheat (Triticum aestivum cv. Soissons) seeds is described here [18].
• Using intrinsic tryptophan fluorescence as a measure of redox state, the redox potential of WhiB1 was calculated as -236+/-2mV, which corresponds to the redox potential of many cytoplasmic thioredoxin-like proteins [19].
• Employing thioredoxin as carrier protein, specific and nearly quantitative cleavage of ET-1 from the fusion was mediated by Factor Xa, and purification to homogeneity (final purity of >95%) was achieved by RP-HPLC [20].
• It presented the catalytic mechanism for a typical 2-CysPrx because the homodimeric oxidized form is reduced to a monomeric form by thioredoxin (Trx) and by dithiothreitol (DTT) and was converted to a homodimeric oxidized form by H2O2 [21].
• Pulse proteolysis was used to demonstrate that TrxS102 unfolded at lower urea concentrations than wild type thioredoxin [22].

Other interactions of trxA

• The redox protein from PH0178 had strong thioredoxin-like activity, but no glutaredoxin activity [1].

Analytical, diagnostic and therapeutic context of trxA

• Indeed, we recently reported a robust correlation between the effect of 27 conservative mutations on the thermodynamic stability (unfolding free energy) of Escherichia coli thioredoxin and the frequencies of residues occurrences in sequence alignments [23].
• Specific expression of the three thioredoxin genes was analysed by real-time RT-PCR in developing and germinating seeds and seedlings under stressed and unstressed conditions [18].
• Expression, purification, crystallization and preliminary X-ray diffraction analysis of mitochondrial thioredoxin Trx3 from Saccharomyces cerevisiae [24].
• The reassembly of E. coli Thioredoxin (Trx) by complementation of its two disordered fragments (1-37/38-108) provides a folded heterodimer in equilibrium with its unfolded state which, based on circular dichroism and NMR spectroscopy, consists of two unfolded monomers [25].

References