Cloning and functional characterization of a typical 2-Cys peroxiredoxin from southern bluefin tuna (Thunnus maccoyii)

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 156, Issue 2, 2010, Pages 97-106

  Sutton, Drew L ^a   Loo, Grace H ^a   Menz, R Ian ^a   Schuller, Kathryn A ^a  

^a FLINDERS UNIVERSITY   (Australia)

Author keywords

2 Cys peroxiredoxin; Antioxidant; Natural killer enhancing factor; NKEF; Southern bluefin tuna; Thunnus maccoyii

Indexed keywords

2 CYSTEINE PEROXIREDOXIN; COMPLEMENTARY DNA; CUMENE HYDROPEROXIDE; DIMER; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; PEROXIREDOXIN; PEROXIREDOXIN 1; PEROXIREDOXIN 2; TERT BUTYL HYDROPEROXIDE; TETRAMER; THIOREDOXIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AQUACULTURE; ARTICLE; AUSTRALIA; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; MAMMAL; MICHAELIS MENTEN KINETICS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MOTIF; PROTEIN PURIFICATION; SEQUENCE ANALYSIS; TUNA;

EUKARYOTA; MAMMALIA; PROTISTA; THUNNUS MACCOYII;

EID: 77952012285     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2010.02.011     Document Type: Article

References (44)

1. Akerman S.E., Müller S. 2-Cys peroxiredoxin PfTrx-Px1 is involved in the antioxidant defence of Plasmodium falciparum. Mol. Biochem. Parasitol. 2003, 130:75-81.
2. Akerman S.E., Müller S. Peroxiredoxin-linked detoxification of hydroperoxides in Toxoplasma gondii. J. Biol. Chem. 2005, 280:564-570.
3. Aran M., Ferrero D.S., Pagano E., Wolosiuk R.A. Typical 2-Cys peroxiredoxins - modulation by covalent transformations and noncovalent interactions. FEBS J. 2009, 276:2478-2493.
4. Barranco-Medina S., Lázaro J.-J., Dietz K.-J. The oligomeric conformation of peroxiredoxins links redox state to function. FEBS Lett. 2009, 583:1809-1816.
5. Boucher I.W., McMillan P.J., Gabrielsen M., Akerman S.E., Brannigan J.A., Schnick C., Brzozowski A.M., Wilkinson A.J., Müller S. Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum. Mol. Microbiol. 2006, 61:948-959.
6. Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding. Anal. Biochem. 1976, 72:248-254.
7. Chae H.Z., Chung S.J., Rhee S.G. Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 1994, 269:27670-27678.
8. Chae H.Z., Kim H.J., Kang S.W., Rhee S.G. Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Res. Clin. Pract. 1999, 45:101-112.
9. Chen Y., Zhang Y.-X., Fan T.-J., Meng L., Ren G., Chen S.-L. Molecular identification and expression analysis of the natural killer cell enhancing factor (NKEF) gene from turbot (Scophthalmus maximus). Aquaculture 2006, 261:1186-1193.
10. Chen J., Wu H.Q., Niu H., Shi Y.H., Li M.Y. Increased liver protein and mRNA expression of natural killer cell-enhancing factor B (NKEF-B) in ayu (Plecoglossus altivelis) after Aeromonas hydrophila infection. Fish Shellfish Immunol. 2009, 26:567-571.
11. Cox A.G., Pearson A.G., Pullar J.M., Jönsson T.J., Lowther W.T., Winterbourn C.C., Hampton M.B. Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins. Biochem. J. 2009, 421:51-58.
12. Dietz K.-J. Plant peroxiredoxins. Annu. Rev. Plant Biol. 2003, 54:93-107.
13. Dong W.-R., Xiang L.-X., Shao J.-Z. Cloning and characterization of two natural killer enhancing factor genes (NKEF-A and NKEF-B) in pufferfish, Tetraodon nigroviridis. Fish Shellfish Immunol. 2007, 22:1-5.
14. Glencross B.D., Clarke S.M., Buchanan J.G., Carter C.G., van Barneveld R.J. Temporal growth patterns of farmed juvenile southern bluefin tuna, Thunnus maccoyii (Castelnau) fed moist pellets. J. World Aquaculture Society 2002, 33:138-145.
15. Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl. Acids Symp. Ser. 1999, 41:95-98.
16. Hall A., Karplus P.A., Poole L.B. Typical 2-Cys peroxiredoxins - structures mechanisms and functions. FEBS J. 2009, 276:2469-2477.
17. Halliwell B., Gutteridge J.M.C. Free Radicals in Biology and Medicine 2004, Oxford Science Publications, Oxford. third ed.
18. Hofmann B., Hecht H.-J., Flohé L. Peroxiredoxins. Biol. Chem. 2002, 383:347-364.
19. Huang R., Gao L.-Y., Wang Y.-P., Hu W., Guo Q.-L. Structure, organization and expression of common carp (Cyprinus carpio L.) NKEF-B gene. Fish Shellfish Immunol. 2009, 26:220-229.
20. Kawazu S., Komaki-Yasuda K., Oku H., Kano S. Peroxiredoxins in malaria parasites: parasitologic aspects. Parasitol. Int. 2008, 57:1-7.
21. König J., Lotte K., Plessow R., Brockhinke A., Baier M., Dietz K.-J. Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure. J. Biol. Chem. 2003, 278:24409-24420.
22. Larkin M.A., Blackshields G., Brown N.P., Chenna R., McGettigan P.A., McWilliam H., Valentin F., Wallace I.M., Wilm A., Lopez R., Thompson J.D., Gibson T.J., Higgins D.G. Clustal W and Clustal X version 2.0. Bioinformatics 2007, 23:2947-2948.
23. 83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2. J. Biol. Chem. 2007, 282:22011-22022.
24. Li R.W., Waldbieser G.C. Genomic organization and expression of the natural killer cell enhancing factor (NKEF) gene in channel catfish. Ictalurus punctatus (Rafinesque). Fish Shellfish Immunol. 2006, 20:72-82.
25. Manta B., Hugo M., Ortiz C., Ferrer-Sueta G., Trujillo M., Denicola A. The peroxidase and peroxynitrite reductase activity of human erythrocyte peroxiredoxin 2. Arch. Biochem. Biophys. 2009, 484:146-154.
26. Mourente G., Bell J.G., Tocher D.R. Does dietary tocopherol level affect fatty acid metabolism in fish?. Fish Physiol. Biochem. 2007, 33:269-280.
27. 2 by yeast. J. Biol. Chem. 2004, 279:35219-35227.
28. Nicholas K.B., Nicholas H.B., Deerfield D.W. Genedoc: analysis and visualization of genetic variation. embnet.news 1997, 4(2):1.
29. Poole L.B. Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Arch. Biochem. Biophys. 2005, 433:240-254.
30. Pushpamali W.A., De Zoysa M., Kang H.-S., Oh C.H., Whang I., Kim S.J., Lee J. Comparative study of two thioredoxin peroxidases from disk abalone (Haliotis discus discus): cloning, recombinant protein purification, characterization of antioxidant activities and expression analysis. Fish Shellfish Immunol. 2008, 24:294-307.
31. Rahlfs S., Becker K. Thioredoxin peroxidases of the malarial parasite Plasmodium falciparum. Eur. J. Biochem. 2001, 268:1404-1409.
32. Rhee S.G., Chae H.Z., Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling, Free Radic. Biol. Med. 2005, 38:1543-1552.
33. Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 1987, 4:406-425.
34. Sayed A.A., Williams D.L. Biochemical characterization of 2-Cys peroxiredoxins from Schistosoma mansoni. J. Biol. Chem. 2004, 229:26159-26166.
35. Shin D., Fujiki K., Nakao M., Yano T. Organization of the NKEF gene and its expression in the common carp (Cyprinus carpio). Dev. Comp. Immunol. 2001, 25:597-606.
36. Thomas P.M., Carter C.G., Carragher J.F., Glencross B.D. Preliminary information on temporal changes in the blood chemistry of farmed southern bluefin tuna, Thunnus maccoyii (Castelnau), after feeding and repeated sampling disturbance. Aquacult. Res. 2003, 34:265-267.
37. Thompson J.L., Thomas P.M., Schuller K.A. Purification and properties of a glutathione peroxidase from southern bluefin tuna (Thunnus maccoyii) liver. Comp. Biochem. Physiol. Part B 2006, 144:86-93.
38. Tocher D.R. Metabolism and functions of lipids and fatty acids in teleost fish. Rev. Fisheries Sci. 2003, 11:107-184.
39. Valavanidis A., Vlahogianni T., Dassenakis M., Scoullos M. Molecular biomarkers of oxidative stress in aquatic organisms in relation to toxic environmental pollutants. Ecotoxicol. Environ. Saf. 2006, 64:178-189.
40. Winston G.W., Di Giulio R.T. Prooxidant and antioxidant mechanisms in aquatic organisms. Aquat. Toxicol. 1991, 19:137-161.
41. Wood Z.A., Poole L.B., Hantgan R.R., Karplus P.A. Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins. Biochemistry 2002, 41:5493-5504.
42. Wood Z.A., Poole L.B., Karplus P.A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 2003, 300:650-653.
43. Yang K.-S., Kang S.W., Woo H.A., Hwang S.C., Chae H.Z., Kim K., Rhee S.G. Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J. Biol. Chem. 2002, 277:38029-38036.
44. Zhang H., Evenhuis J.P., Thorgaard G.H., Ristow S.S. Cloning, characterization and genomic structure of the natural killer cell enhancement factor (NKEF)-like gene from homozygous clones of rainbow trout (Oncorhynchus mykiss). Dev. Comp. Immunol. 2001, 25:25-35.