Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily

Protein Science

Volumn 7, Issue 11, 1998, Pages 2465-2468

  Schröder, Ewald ^a,c   Ponting, Chris P ^b,c  

^a UNIVERSITY OF EXETER   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Cysteine sulfenic acid; Glutathione peroxidase; Oxidative stress; Reactive oxygen species; Thiol specific antioxidant

Indexed keywords

ALCOHOL; ANTIOXIDANT; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; PEROXIDE; PEROXIREDOXIN; REACTIVE OXYGEN METABOLITE; SELENOCYSTEINE; THIOREDOXIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ESCHERICHIA COLI; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING;

EID: 0037834629     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071125     Document Type: Article

References (44)

1. Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. 1997. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucl Acids Res 25:3389-3402.
2. Baier M, Dietz KJ. 1996. The 2-Cys peroxiredoxin Bas1: Insight in a new family of plant peroxidases. In: Obinger C, Burner U, Evermann R, Penel C, Greppin H, eds. Plant peroxidases: Biochemistry and physiology. Geneva: University of Geneva.
3. Bruchhaus I, Richter S, Tannich E. 1997. Removal of hydrogen peroxide by the 29 kDa protein of Entamoeba histolytica. Biochem J 326:785-789.
4. Cha M, Kim I. 1995. Thioredoxin-linked peroxidase from human red blood cell: Evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell. Biochem Biophys Res Comm 217:900-907.
5. Chae HZ, Chung SJ, Rhee SG. 1994a. Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 269:27670-27678.
6. Chae HZ, Robison K, Poole LB, Church G, Storz G, Rhee SG. 1994b. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci USA 97:7017-7021.
7. Chae HZ, Uhm TB, Rhee SG. 1994c. Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc Natl Acad Sci USA 91:7022-7026.
8. Chivers PT, Prehoda KE, Raines RT. 1997. The CXXC motif: A rheostat in the active site. Biochemistry 36:4061-4066.
9. Claiborne A, Miller H, Parsonage D, Ross RP. 1993. Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J 7:1483-1490.
10. Epp O, Ladenstein R, Wendel A. 1983. The refined structure of the seleno-enzyme glutathione peroxidase at 0.2-nM resolution. Eur J Biochem 133: 51-69.
11. Frank S, Munz B, Werner S. 1997. The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene. Oncogene 14:915-921.
12. Halliwell B, Gutteridge JMC. 1989. Free radicals in biology and medicine. New York: Clarendon Press.
13. Holm L, Sander C. 1998, Touring protein fold space with Dali/FSSP. Nucl Acids Res 26:316-319.
14. Holmgren A. 1995. Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 5:239-243
15. Hudson-Taylor DE, Dolan SA, Klotz FW, Fujioka H, Aikawa M, Koonin EV, Miller LH. 1995. Plasmodium falciparum protein associated with the invasion junction contains a conserved oxidoreductase domain. Mol Microbiol 15:463-471.
16. Jacobson FS, Morgan RW, Christman MF, Ames BN. 1989. An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties. J Biol Chem 264:1488-1496.
17. Jin D-Y, Chae H-Z, Rhee SG, Jeang K-T. 1997. Regulatory role for a novel human thioredoxin peroxidase in NF-κB activation. J Biol Chem 272:30952-30961.
18. Kang SW, Baines IC, Rhee SG. 1998a. Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J Biol Chem 273:6303-6311.
19. Kang SW, Chae HZ, Seo MS, Kim K, Baines IC, Rhee SG. 1998b. Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-α. J Biol Chem 273:6297-6302.
20. Katti SK, LeMaster DM, Eklund H. 1990. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J Mol Biol 212:167-184.
21. Katti SK, Robbins AH, Yang Y, Wells WW. 1995. Crystal structure of thioltransferase at 2.2 Å resolution. Protein Sci 4:1998-2005.
22. Kortemme T, Creighton TE. 1995. Ionisation of cysteine residues at the termini of model α-helical peptides. Relevance to unusual thiol pKα values in proteins of the thioredoxin family. J Mol Biol 253:799-812.
23. Ladenstein R, Epp O, Bartels K, Jones A, Huber R. 1979. Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 Å resolution. J Mol Biol 134:199-218.
24. Lim YS, Cha MK, Kim HK, Uhm TB, Park JW, Kim K, Kim IH. 1993. Removals of hydrogen peroxide and hydroxyl radical by thiol-specific anti-oxidant protein as a possible role in vivo. Biochem Biophys Res Comm 192:273-280.
25. Martin JL. 1995. Thioredoxin: A fold for all reasons. Structure 3:245-250.
26. Martin JL, Bardwell JC, Kuriyan J. 1993. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365:464-468.
27. Montemartini M, Nogoceke E, Singh M, Steinert P, Flohé L, Kalisz HM. 1998. Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli. J Biol Chem 273:4864-4871.
28. Munz B, Frank S, Hübner G, Olsen E, Werner S. 1997. A novel type of glutathione peroxidase: Expression and regulation during wound repair. Biochem J 326:579-585.
29. Nogoceke E, Gommel DU, Kieβ M, Kalisz HM, Flohé L. 1997. A unique cascade of oxidoreductases catalyzes trypanothione-mediated peroxide metabolism in Crithidia fasciculata. J Biol Chem 375:827-836.
30. Pahl HL, Baeuerle PA. 1994. Oxygen and the control of gene expression. Bioessays 16:497-502.
31. Pearson WR. 1991. Searching protein sequence libraries: Comparison of the sensitivity and selectivity of the Smith-Waterman and FASTA algorithms. Genomics 11:635-650.
32. Poole LB. 1996. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction. Biochemistry 35:65-75.
33. Poole LB, Ellis HR. 1996. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. Biochemistry 35:56-64.
34. Ren B, Huang W, Akesson B, Ladenstein R. 1997. The crystal structure of seleno-glutathione peroxidase from human plasma at 2.9 A resolution. J Mol Biol 265:869-885.
35. Rost B, Sander C. 1993. Prediction of protein secondary structure at better than 70% accuracy. J Mol Biol 232:584-599.
36. Saarinen M, Gleason FK, Eklund H. 1995. Crystal structure of thioredoxin-2 from Anabaena. Structure 3:1097-1108.
37. Schröder E, Willis AC, Ponting CP. 1998. Porcine natural killer enhancing factor-B: Oligomerization and identification as a calpain substrate in vitro. Biochim Biophys Acta. Forthcoming.
38. Shau H, Kim AT, Hedrick CC, Lusis AJ, Tompkins C, Finney R, Leung DW, Paglia DE. 1997. Endogenous natural killer enhancing factor-B increases cellular resistance to oxidative stress. Free Radic Biol Med 22:497-507.
39. Shichi H, Demar JC. 1990. Non-selenium glutathione peroxidase without glutathione S-transferase activity from bovine ciliary body. Exp Eye Res 50:513-520.
40. Sodano P, Xia TH, Bushweller JH, Bjornberg O, Holmgren A, Billeter M, Wuthrich K. 1991. Sequence-specific 1H N.M.R. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin. J Mol Biol 20:1311-1324.
41. Tartaglia LA, Storz G, Brodsky MH, Lai A, Ames BN. 1990. Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases. J Biol Chem 265:10535-10540.
42. Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl Acids Res 22:4673-4680.
43. Tsuji K, Copeland NG, Jenkins NA, Obinata M. 1995. Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli. Biochem J 307:377-381.
44. Ursini F, Maiorino M, Brigelius-Flohé R, Aumann KD, Roveri A, Schomburg D, Flohé L. 1995. Diversity of glutathione peroxidases. Methods Enzymol 252:38-53.