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Gene Review

trxA  -  thioredoxin

Escherichia coli O157:H7 str. Sakai

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Disease relevance of trxA


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 [1].
  • 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 [1].
  • Both DsbA and TcpG promote disulfide bond formation in periplasmic proteins, are required for pilus biogenesis, and, like thioredoxin, are capable of reducing insulin in vitro [5].
  • E. coli C35S Trx, in which Cys(35) was replaced with Ser, formed some adducts with MST and activated MST after treatment with DTT [6].
  • Reduced Trx turns on a redox switch for the enzymatic activation of MST, which contributes to the maintenance of cellular redox homeostasis [6].

Chemical compound and disease context of trxA


Biological context of trxA

  • 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 [9].
  • 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 [10].
  • 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 [11].

Anatomical context of trxA

  • We show that the alpha domain of Escherichia coli DsbD is able to reduce the oxidized NT domain, which suggests that DsbD in Neisseria can transfer electrons from the cytoplasmic thioredoxin to the periplasm for the reduction of the MsrA/B domains [2].
  • 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 [12].

Associations of trxA with chemical compounds

  • SppA fused to thioredoxin (TRX-SppA) showed distinct heat-stable phosphatase activity toward p-nitrophenyl phosphate with optimal pH 8.0 and optimal temperature 55 degrees C. Mn2+ greatly enhanced enzyme activity, as is found with other protein Ser/Thr phosphatases [13].
  • 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 [14].
  • 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 [15].
  • 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 [16].
  • 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 [17].

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 [18].
  • 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 [14].
  • Expression, purification, crystallization and preliminary X-ray diffraction analysis of mitochondrial thioredoxin Trx3 from Saccharomyces cerevisiae [19].
  • 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 [20].


  1. Thionein can serve as a reducing agent for the methionine sulfoxide reductases. Sagher, D., Brunell, D., Hejtmancik, J.F., Kantorow, M., Brot, N., Weissbach, H. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. The Thioredoxin Domain of Neisseria gonorrhoeae PilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases. Brot, N., Collet, J.F., Johnson, L.C., J??nsson, T.J., Weissbach, H., Lowther, W.T. J. Biol. Chem. (2006) [Pubmed]
  3. Atomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter aceti. Starks, C.M., Francois, J.A., Macarthur, K.M., Heard, B.Z., Kappock, T.J. Protein Sci. (2007) [Pubmed]
  4. Tandem copies of a human rotavirus VP8 epitope can induce specific neutralizing antibodies in BALB/c mice. Kovacs-Nolan, J., Mine, Y. Biochim. Biophys. Acta (2006) [Pubmed]
  5. A periplasmic protein disulfide oxidoreductase is required for transformation of Haemophilus influenzae Rd. Tomb, J.F. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  6. Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation. Nagahara, N., Yoshii, T., Abe, Y., Matsumura, T. J. Biol. Chem. (2007) [Pubmed]
  7. Metal-protein interactions: structure information from Ni(2+)-induced pseudocontact shifts in a native nonmetalloprotein. Jensen, M.R., Led, J.J. Biochemistry (2006) [Pubmed]
  8. Cloning and functional characterisation of a cis-muuroladiene synthase from black peppermint (Menthaxpiperita) and direct evidence for a chemotype unable to synthesise farnesene. Prosser, I.M., Adams, R.J., Beale, M.H., Hawkins, N.D., Phillips, A.L., Pickett, J.A., Field, L.M. Phytochemistry (2006) [Pubmed]
  9. Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG. Yeh, S.M., Koon, N., Squire, C., Metcalf, P. Acta Crystallogr. D Biol. Crystallogr. (2007) [Pubmed]
  10. Three Distinct-Type Glutathione S-Transferases from Escherichia coli Important for Defense against Oxidative Stress. Kanai, T., Takahashi, K., Inoue, H. J. Biochem. (2006) [Pubmed]
  11. Cloning, sequencing, expression, and antigenic characterization of rMSP4 from Anaplasma marginale isolated from Paraná State, Brazil. Kawasaki, P.M., Kano, F.S., Vidotto, O., Vidotto, M.C. Genet. Mol. Res. (2007) [Pubmed]
  12. In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. O'Reilly, M.K., Zhang, G., Imperiali, B. Biochemistry (2006) [Pubmed]
  13. Genetic and biochemical characterization of a protein phosphatase with dual substrate specificity in Streptomyces coelicolor A3(2). Umeyama, T., Naruoka, A., Horinouchi, S. Gene (2000) [Pubmed]
  14. Cloning and characterization of three thioredoxin h isoforms from wheat showing differential expression in seeds. Cazalis, R., Pulido, P., Aussenac, T., Pérez-Ruiz, J.M., Cejudo, F.J. J. Exp. Bot. (2006) [Pubmed]
  15. Molecular cloning and characterization of a 2-Cys peroxiredoxin from Taenia solium. Molina-López, J., Jiménez, L., Ochoa-Sánchez, A., Landa, A. J. Parasitol. (2006) [Pubmed]
  16. Characterization of Mycobacterium tuberculosis WhiB1/Rv3219 as a protein disulfide reductase. Garg, S.K., Suhail Alam, M., Soni, V., Radha Kishan, K.V., Agrawal, P. Protein Expr. Purif. (2007) [Pubmed]
  17. High yield expression and purification of isotopically labelled human endothelin-1 for use in NMR studies. Mac, T.T., Beyermann, M., Pires, J.R., Schmieder, P., Oschkinat, H. Protein Expr. Purif. (2006) [Pubmed]
  18. Natural Selection for Kinetic Stability Is a Likely Origin of Correlations between Mutational Effects on Protein Energetics and Frequencies of Amino Acid Occurrences in Sequence Alignments. Godoy-Ruiz, R., Ariza, F., Rodriguez-Larrea, D., Perez-Jimenez, R., Ibarra-Molero, B., Sanchez-Ruiz, J.M. J. Mol. Biol. (2006) [Pubmed]
  19. Expression, purification, crystallization and preliminary X-ray diffraction analysis of mitochondrial thioredoxin Trx3 from Saccharomyces cerevisiae. Bao, R., Chen, Y.X., Zhang, Y., Zhou, C.Z. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
  20. The pH-dependence of amide chemical shift of Asp/Glu reflects its pKa in intrinsically disordered proteins with only local interactions. Pujato, M., Navarro, A., Versace, R., Mancusso, R., Ghose, R., Tasayco, M.L. Biochim. Biophys. Acta (2006) [Pubmed]
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