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TRX3  -  thioredoxin H3

Arabidopsis thaliana

Synonyms: ATH3, ATTRX3, ATTRXH3, MBD2.18, MBD2_18, ...
 
 
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Disease relevance of ATTRX3

  • Cell extracts of E. coli expressing APR showed Trx-independent sulfonucleotide reductase activity with a preference for APS over PAPS as a substrate [1].
  • The structure, defined by 1637 NMR-derived distance and torsion angle constraints, displays the conserved thioredoxin fold, consisting of a five-stranded beta-sheet flanked by four helices [2].
 

High impact information on ATTRX3

  • We also created chimeric ATTRX5/ATTRX3 proteins, which identified the central portion of the protein as important for conferring specificity to ATTRX5 [3].
  • We conclude that CDSP32 is a thioredoxin with a critical role in plastid defense against oxidative damage and that this role is related to its function as a physiological electron donor to the BAS1 peroxiredoxin [4].
  • The chloroplastic drought-induced stress protein of 32 kD (CDSP32) is composed of two thioredoxin modules and is induced by environmental and oxidative stress conditions [4].
  • FKBP20-2 has a unique pair of cysteines at the C terminus and was found to be reduced by thioredoxin (Trx) (itself reduced by NADPH by means of NADP-Trx reductase) [5].
  • Results provide evidence that T6P is synthesized in the cytosol and acts on plastidial metabolism by promoting thioredoxin-mediated redox transfer to AGPase in response to cytosolic sugar levels, thereby allowing starch synthesis to be regulated independently of light [6].
 

Chemical compound and disease context of ATTRX3

  • In order to isolate thioredoxin targets related to these phenotypes, we prepared a C35S (Escherichia coli numbering) thioredoxin mutant to stabilize the intermediate disulfide bridged complex and we added a polyhistidine N-terminal extension in order to purify the complex rapidly [7].
  • This feature of MsrB1 could result from the lack of the catalytical cysteine (Cys) corresponding to Cys-63 in Escherichia coli MsrB that is involved in the regeneration of Cys-117 through the formation of an intramolecular disulfide bridge followed by thioredoxin reduction [8].
  • The steady-state reactions of A. thaliana TR with thioredoxin (TRX) and reaction product NADP+ inhibition patterns were in agreement with a proposed model of E. coli enzyme (B.W. Lennon, C.H. Williams, Jr., Biochemistry, vol. 35 (1996), pp. 4704-4712), that involved enzyme cycling between four- and two-electron reduced forms with FAD being reduced [9].
 

Biological context of ATTRX3

 

Anatomical context of ATTRX3

  • Thus, the yield of active ATP N peroxidase can be increased 50-fold by using thioredoxin reductase negative strains, which facilitate the formation of disulfide bonds in inclusion body protein [15].
 

Associations of ATTRX3 with chemical compounds

 

Other interactions of ATTRX3

  • Furthermore, we found that ATTRX5, but not ATTRX3, is highly induced in sensitive Arabidopsis following victorin treatment [3].
  • We have constructed hybrid proteins between these two thioredoxins and show that all information necessary for sulfate assimilation is present in the C-terminal part of AtTRX2, whereas some information needed for H(2)O(2) tolerance is located in the N-terminal part of AtTRX3 [10].
 

Analytical, diagnostic and therapeutic context of ATTRX3

  • Four classes are defined as peroxiredoxins and were already identified by phylogenetic sequence analysis, 1-Cys, 2-Cys, type II, and type Q peroxiredoxins, and the fifth is represented by glutathione peroxidases, which were recently shown to possess a thioredoxin-dependent activity in plants [17].
  • Identification of thioredoxin-linked proteins by fluorescence labeling combined with isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis [18].

References

  1. Sulfate reduction in higher plants: molecular evidence for a novel 5'-adenylylsulfate reductase. Setya, A., Murillo, M., Leustek, T. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  2. Solution structure of thioredoxin h1 from Arabidopsis thaliana. Peterson, F.C., Lytle, B.L., Sampath, S., Vinarov, D., Tyler, E., Shahan, M., Markley, J.L., Volkman, B.F. Protein Sci. (2005) [Pubmed]
  3. Thioredoxin h5 Is Required for Victorin Sensitivity Mediated by a CC-NBS-LRR Gene in Arabidopsis. Sweat, T.A., Wolpert, T.J. Plant Cell (2007) [Pubmed]
  4. The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage. Broin, M., Cuiné, S., Eymery, F., Rey, P. Plant Cell (2002) [Pubmed]
  5. A redox-active FKBP-type immunophilin functions in accumulation of the photosystem II supercomplex in Arabidopsis thaliana. Lima, A., Lima, S., Wong, J.H., Phillips, R.S., Buchanan, B.B., Luan, S. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  6. Trehalose 6-phosphate regulates starch synthesis via posttranslational redox activation of ADP-glucose pyrophosphorylase. Kolbe, A., Tiessen, A., Schluepmann, H., Paul, M., Ulrich, S., Geigenberger, P. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  7. In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. Verdoucq, L., Vignols, F., Jacquot, J.P., Chartier, Y., Meyer, Y. J. Biol. Chem. (1999) [Pubmed]
  8. The Arabidopsis plastidic methionine sulfoxide reductase B proteins. Sequence and activity characteristics, comparison of the expression with plastidic methionine sulfoxide reductase A, and induction by photooxidative stress. Vieira Dos Santos, C., Cuiné, S., Rouhier, N., Rey, P. Plant Physiol. (2005) [Pubmed]
  9. Interaction of quinones with Arabidopsis thaliana thioredoxin reductase. Bironaite, D., Anusevicius, Z., Jacquot, J.P., Cenas, N. Biochim. Biophys. Acta (1998) [Pubmed]
  10. Characterization of determinants for the specificity of Arabidopsis thioredoxins h in yeast complementation. Bréheĺin, C., Mouaheb, N., Verdoucq, L., Lancelin, J.M., Meyer, Y. J. Biol. Chem. (2000) [Pubmed]
  11. Comprehensive survey of proteins targeted by chloroplast thioredoxin. Motohashi, K., Kondoh, A., Stumpp, M.T., Hisabori, T. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  12. Evidence for five divergent thioredoxin h sequences in Arabidopsis thaliana. Rivera-Madrid, R., Mestres, D., Marinho, P., Jacquot, J.P., Decottignies, P., Miginiac-Maslow, M., Meyer, Y. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  13. The Arabidopsis plastidial thioredoxins: new functions and new insights into specificity. Collin, V., Issakidis-Bourguet, E., Marchand, C., Hirasawa, M., Lancelin, J.M., Knaff, D.B., Miginiac-Maslow, M. J. Biol. Chem. (2003) [Pubmed]
  14. The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative stress and its W-box-mediated response to pathogen elicitor. Laloi, C., Mestres-Ortega, D., Marco, Y., Meyer, Y., Reichheld, J.P. Plant Physiol. (2004) [Pubmed]
  15. Disulfide bond formation and folding of plant peroxidases expressed as inclusion body protein in Escherichia coli thioredoxin reductase negative strains. Teilum, K., Ostergaard, L., Welinder, K.G. Protein Expr. Purif. (1999) [Pubmed]
  16. Redox regulation of Arabidopsis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase. Entus, R., Poling, M., Herrmann, K.M. Plant Physiol. (2002) [Pubmed]
  17. The plant multigenic family of thiol peroxidases. Rouhier, N., Jacquot, J.P. Free Radic. Biol. Med. (2005) [Pubmed]
  18. Identification of thioredoxin-linked proteins by fluorescence labeling combined with isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Wong, J.H., Yano, H., Lee, Y.M., Cho, M.J., Buchanan, B.B. Meth. Enzymol. (2002) [Pubmed]
 
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