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Gene Review

trxA  -  thioredoxin

Escherichia coli O157:H7 str. EDL933

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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].
  • The trxA gene encoding one of the different thioredoxins of the facultative heterotrophic cyanobacterium Synechocystis sp. PCC 6803 is transcribed as a single mRNA of 450 nucleotides [2].
  • The mutants were characterized using an in vivo assay based on the ability of cell (mutants in the chromosomal trxA gene) to support growth of T7 and filamentous f1 phages [3].
  • The T. ferrooxidans trxA gene was sequenced and the thioredoxin was found to be most like that of E. coli (71% identity) and Chromatium vinosum (70% identity) [4].
  • Thioredoxin system in obligate anaerobe Desulfovibrio desulfuricans: Identification and characterization of a novel thioredoxin 2 [5].

Psychiatry related information on trxA

  • The process is an exponential function of the thioredoxin concentration and reaction time and can be described by an irreversible second order reaction [6].

High impact information on trxA

  • We report here the expression of a combinatorial library of constrained 20-residue peptides displayed by the active-site loop of Escherichia coli thioredoxin, and the use of a two-hybrid system to select those that bind human Cdk2 [7].
  • However, partially overlapping critical regions for all these functions were identified at the C-terminal end of the preceding thioredoxin-like domain a'. Point mutations introduced into this region identified several residues as critical for prolyl 4-hydroxylase assembly [8].
  • In contrast to all members of the thioredoxin family known to date, TlpA was shown to be anchored to the cytoplasmic membrane by means of an N-terminal transmembrane domain, while the active site-containing part of the protein faced the periplasm [9].
  • 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 [10].
  • 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 [10].

Chemical compound and disease context of trxA

  • To this end, new Escherichia coli K-12 strains carrying delta trxA and/or grx::kan null mutations were constructed to monitor mutagenesis by selecting forward mutations to L-arabinose resistance [11].
  • Thioredoxin reductase (NADPH), as well as thioredoxin, is required for efficient filamentous phage production [12].
  • We use this relationship to obtain unfolding free energies for both the reduced and oxidized forms of Escherichia coli thioredoxin from measurements of the effective concentrations of protein thiols [13].
  • In addition, a human FAS cDNA encoding domains II and III (enoyl and beta-ketoacyl reductases, acyl carrier protein, and thioesterase) was cloned in pET-32b(+) and expressed in E. coli as a fusion protein with thioredoxin and six in-frame histidine residues [14].
  • Here we present the first successful introduction by rational design of a [Fe4S4] cuboidal cluster into the hydrophobic core of Escherichia coli thioredoxin, a protein normally devoid of metal centers [15].

Biological context of trxA

  • Gene fusion analysis with nested series of deletions of rho indicated that the transcription of rho is attenuated in a rho-dependent manner in the leader region and that neither a read-through transcription from the upstream gene, trxA, nor a modulation of transcription initiation of the rho promoter is involved in the self-control of rho [16].
  • Plasmids carrying the trxA gene restored the Fip+ phenotype to fip strains [17].
  • Electron transport controls transcription of the thioredoxin gene (trxA) in the cyanobacterium Synechocystis sp. PCC 6803 [2].
  • Primer extension analysis suggests that trxA is transcribed from two proximal promoters containing a -10 TATA box similar to the Escherichia coli consensus promoters [2].
  • Introduction of a frameshift mutation into the cloned trxA coding region abolished the ability of these recombinant plasmids to reverse the suppressive effect [18].

Anatomical context of trxA

  • The in vitro decay of two different mRNAs (trxA and lpp) is triggered by the addition of ATP only when polysomes are prepared from s strain carrying the wild-type gene for PAP I (pcnB+) [19].
  • Such a mechanism, occurring in the thylakoid lumen, is in direct contrast to regulation of enzymes in the stroma, where reduction of disulfides targeted by thioredoxin (S-S converted to SH) leads to an increase in activity in the light [20].
  • A fusion protein of the N-terminal domain and thioredoxin binds tightly to MTs at low salt, consistent with the increased affinity of motor domain constructs (which contain the N-terminal domain) being due to the additional binding of the N-terminal domain to the microtubule [21].
  • The effect of H2O2 upon thioredoxin-enriched lens epithelial cells [22].
  • 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 [23].

Associations of trxA with chemical compounds

  • The trxA genes with W31Y and W31F substitutions restored, fully and partly, the methionine sulfoxide utilization of a trxA- metE- test strain; W31A and W31H mutations resulted in no growth [24].
  • The presence of excess cystine at a concentration sufficient to repress the sulfate assimilation pathway obviates the need for an X mutation and prevents the lethality of a novel cys+ trxA grx double mutant designated strain A522 [25].
  • Photosynthetic electron transport inhibitors, as well as glucose starvation in a mutant strain lacking photosystem II, promote a strong decline in the level of trxA transcript [2].
  • Our data suggest that the inviability of a trxA grx double mutant is due to the accumulation of 3'-phosphoadenosine 5'-phosphosulfate (PAPS), an intermediate in the sulfate assimilation pathway [25].
  • Mapping and characterization of mutations conferring a DTT-sensitive phenotype also identified the dsbA, trxA, and trxB genes, whose products are involved in different oxidation-reduction pathways [26].

Other interactions of trxA


Analytical, diagnostic and therapeutic context of trxA


  1. A hyperthermostable novel protein-disulfide oxidoreductase is reduced by thioredoxin reductase from hyperthermophilic archaeon Pyrococcus horikoshii. Kashima, Y., Ishikawa, K. Arch. Biochem. Biophys. (2003) [Pubmed]
  2. Electron transport controls transcription of the thioredoxin gene (trxA) in the cyanobacterium Synechocystis sp. PCC 6803. Navarro, F., Martín-Figueroa, E., Florencio, F.J. Plant Mol. Biol. (2000) [Pubmed]
  3. Influence of the different amino acid substitutions in Escherichia coli thioredoxin on the growth of bacteriophages T7 and f1. Minárik, P., Kollárová, M., Brunovská, A. J. Basic Microbiol. (1993) [Pubmed]
  4. Molecular genetic analysis of a thioredoxin gene from Thiobacillus ferrooxidans. Powles, R.E., Deane, S.M., Rawlings, D.E. Microbiology (Reading, Engl.) (1995) [Pubmed]
  5. Thioredoxin system in obligate anaerobe Desulfovibrio desulfuricans: Identification and characterization of a novel thioredoxin 2. Sarin, R., Sharma, Y.D. Gene (2006) [Pubmed]
  6. Kinetics and thioredoxin specificity of thiol modulation of the chloroplast H+-ATPase. Schwarz, O., Schürmann, P., Strotmann, H. J. Biol. Chem. (1997) [Pubmed]
  7. Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2. Colas, P., Cohen, B., Jessen, T., Grishina, I., McCoy, J., Brent, R. Nature (1996) [Pubmed]
  8. The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide. Koivunen, P., Pirneskoski, A., Karvonen, P., Ljung, J., Helaakoski, T., Notbohm, H., Kivirikko, K.I. EMBO J. (1999) [Pubmed]
  9. Bradyrhizobium japonicum TlpA, a novel membrane-anchored thioredoxin-like protein involved in the biogenesis of cytochrome aa3 and development of symbiosis. Loferer, H., Bott, M., Hennecke, H. EMBO J. (1993) [Pubmed]
  10. 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]
  11. Null thioredoxin and glutaredoxin Escherichia coli K-12 mutants have no enhanced sensitivity to mutagens due to a new GSH-dependent hydrogen donor and high increases in ribonucleotide reductase activity. Miranda-Vizuete, A., Martinez-Galisteo, E., Aslund, F., Lopez-Barea, J., Pueyo, C., Holmgren, A. J. Biol. Chem. (1994) [Pubmed]
  12. Thioredoxin is required for filamentous phage assembly. Russel, M., Model, P. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  13. Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein. Lin, T.Y., Kim, P.S. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  14. Cloning and expression of the multifunctional human fatty acid synthase and its subdomains in Escherichia coli. Jayakumar, A., Huang, W.Y., Raetz, B., Chirala, S.S., Wakil, S.J. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  15. The rational design and construction of a cuboidal iron-sulfur protein. Coldren, C.D., Hellinga, H.W., Caradonna, J.P. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  16. Autogenous regulation of the gene for transcription termination factor rho in Escherichia coli: localization and function of its attenuators. Matsumoto, Y., Shigesada, K., Hirano, M., Imai, M. J. Bacteriol. (1986) [Pubmed]
  17. Thioredoxin is the bacterial protein encoded by fip that is required for filamentous bacteriophage f1 assembly. Lim, C.J., Haller, B., Fuchs, J.A. J. Bacteriol. (1985) [Pubmed]
  18. Suppression of the Escherichia coli dnaA46 mutation by a mutation in trxA, the gene for thioredoxin. Hupp, T.R., Kaguni, J.M. Mol. Gen. Genet. (1988) [Pubmed]
  19. Development of an in vitro mRNA decay system for Escherichia coli: poly(A) polymerase I is necessary to trigger degradation. Ingle, C.A., Kushner, S.R. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  20. Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen. Gopalan, G., He, Z., Balmer, Y., Romano, P., Gupta, R., Héroux, A., Buchanan, B.B., Swaminathan, K., Luan, S. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  21. The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. Stock, M.F., Chu, J., Hackney, D.D. J. Biol. Chem. (2003) [Pubmed]
  22. The effect of H2O2 upon thioredoxin-enriched lens epithelial cells. Spector, A., Yan, G.Z., Huang, R.R., McDermott, M.J., Gascoyne, P.R., Pigiet, V. J. Biol. Chem. (1988) [Pubmed]
  23. 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]
  24. Substitution of the conserved tryptophan 31 in Escherichia coli thioredoxin by site-directed mutagenesis and structure-function analysis. Krause, G., Holmgren, A. J. Biol. Chem. (1991) [Pubmed]
  25. Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis. Russel, M., Model, P., Holmgren, A. J. Bacteriol. (1990) [Pubmed]
  26. Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. Missiakas, D., Georgopoulos, C., Raina, S. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  27. Elongation factor Tu and DnaK are transferred from the cytoplasm to the periplasm of Escherichia coli during osmotic downshock presumably via the mechanosensitive channel mscL. Berrier, C., Garrigues, A., Richarme, G., Ghazi, A. J. Bacteriol. (2000) [Pubmed]
  28. Possible regulation of the in vitro assembly of bovine brain tubulin by the bovine thioredoxin system. Khan, I.A., Ludueña, R.F. Biochim. Biophys. Acta (1991) [Pubmed]
  29. Expression and molecular characterization of an enzymatically active recombinant human spumaretrovirus protease. Pfrepper, K.I., Löchelt, M., Schnölzer, M., Flügel, R.M. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  30. The cyanobacterial thioredoxin gene is required for both photoautotrophic and heterotrophic growth. Navarro, F., Florencio, F.J. Plant Physiol. (1996) [Pubmed]
  31. Cardioprotective effects of thioredoxin in myocardial ischemia and reperfusion: role of S-nitrosation [corrected]. Tao, L., Gao, E., Bryan, N.S., Qu, Y., Liu, H.R., Hu, A., Christopher, T.A., Lopez, B.L., Yodoi, J., Koch, W.J., Feelisch, M., Ma, X.L. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  32. Site-directed mutagenesis reveals the involvement of an additional thioredoxin-dependent regulatory site in the activation of recombinant sorghum leaf NADP-malate dehydrogenase. Issakidis, E., Miginiac-Maslow, M., Decottignies, P., Jacquot, J.P., Crétin, C., Gadal, P. J. Biol. Chem. (1992) [Pubmed]
  33. Reconstitution of Escherichia coli thioredoxin from complementing peptide fragments obtained by cleavage at methionine-37 or arginine-73. Slaby, I., Holmgren, A. J. Biol. Chem. (1975) [Pubmed]
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