Sequence, heterologous expression and functional characterization of tryparedoxin1 from Crithidia fasciculata

European Journal of Biochemistry

Volumn 259, Issue 3, 1999, Pages 789-794

  Guerrero, Sergio A ^c   Flohé, Leopold ^b   Kalisz, Henryk M ^a   Montemartini, Marisa ^c   Nogoceke, Everson ^a   Hecht, Hans Jürgen ^a   Steinert, Peter ^c   Singh, Mahavir ^a  

^a HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

^b TECHNICAL UNIVERSITY OF BRAUNSCHWEIG   (Germany)

^c NONE

Author keywords

Crithidia fasciculata; DNA sequence; Heterologous expression; Kinetics; Tryparedoxin1

Indexed keywords

ARTICLE; CONTROLLED STUDY; CRITHIDIA FASCICULATA; DNA SEQUENCE; ENZYME ISOLATION; ENZYME KINETICS; INHIBITION KINETICS; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; TRYPANOSOMIASIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; CRITHIDIA FASCICULATA; DISULFIDES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTOZOAN PROTEINS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; THIOREDOXIN;

CRITHIDIA FASCICULATA; ESCHERICHIA COLI; PROTOZOA; TRYPANOSOMATIDAE;

EID: 0000246509     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00087.x     Document Type: Article

References (31)

1. 1. Chance, B., Sies, H. & Boveris, A. (1979) Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59, 527-605.
2. 2. Flohé, L. (1989) The selenoprolein glutathione peroxidase. In Glutathione - Chemical, Biochemical and Medical Aspects (Dolphin, D., Poulson, R. & Abramovic, O. eds), pp. 643-731. John Wiley & Sons, Inc., Philadelphia, PA, USA.
3. 3. Ursini, F., Maiorino, M., Brigelius-Flohé, R., Aumann, K.D., Roveri, A., Schomburg, D. & Flohé, L. (1995) Diversity of gluthatione peroxidases. Methods Enzymol. 252, 38-53.
4. 4. Le Trant, N., Meshnick, S.R., Kitchener, K., Eaton, J.W. & Cerami, A. (1983) Iron-containing Superoxide dismutase from Crithidia fasciculata. Purification, characterization, and similarity to leishmanial and trypanosomal enzymes. J. Biol. Chem. 258, 125-130.
5. 5. Docampo, R. (1990) Sensitivity of parasites to free radical damage by antiparasitic drugs. Chem. Biol. Interact. 73, 1-27.
6. 6. Flohé, L. (1998) The Achilles' heel of trypanosomatids: trypanothione-mediated hydroperoxide metabolism. Biofactors 8, 87-91.
7. 7. Nogoceke, E., Gommel, D.U., Kiess, M., Kalisz, H.M. & Flohé, L. (1997) A unique cascade of oxidoreductases catalyses trypanothione-medialed peroxide metabolism in Crithidia fasciculata. Biol. Chem. 378, 827-836.
8. 8. Gommel, D.U., Nogoceke, E., Morr, M., Kiess, M., Kalisz, H.M. & Flohé, L. (1997) Catalytic characteristics of tryparedoxin. Eur. J. Biochem. 248, 913-918.
9. 9. Lüdemann, H., Dormeyer, M., Sticherling, C., Stallmann, D., Follmann, H. & Krauth-Siegel, R.L. (1998) T. brucei tryparedoxin, a thioredox-in-like protein in African trypanosomes. FEBS Lett. 431, 381-385.
10. 10. Montemartini, M., Kalisz, H.M., Kiess, M., Nogoceke, E., Singh, M., Steinen, P. & Flohé, L. (1998) Sequence, heterologous expression and functional characterization of a novel tryparedoxin from Crithidia fasciculata. Biol Chem. 379, 1137-1142.
11. 11. Montemartini, M., Nogoceke, E., Singh, M., Steinert, P., Flohé, L. & Kalisz, H.M. (1998) Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli. J. Biol Chem. 273, 4864-4871.
12. 12 Samtrook, J., Fritsch, E.F. & Maniatis, T. (1989) Molecular Cloning: a Laboratory Manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
13. 13. Dalziel, K. (1957) Initial steady state velocities in the evaluation of enzymecoenzyme-substrate reaction mechanisms. Acta Chem. Scand. 11, 1706-1723.
14. 14. Cazzulo, J.., Stoka, V. & Turk, V. (1997) Cruzipain, the major cysteine proteinase from the protozoan parasite Trypanosoma cruzi. Biol. Chem. 378.1-10.
15. 15. Holmgren, A., Soderberg, B.O., Eklund, H. & Branden, C.L. (1975) Three-dimensonal structure of Escherichia coli thioredoxin-S2 to 2.8 Å resolution,. Proc. Natl Acad. Sci. USA 72, 2305-2309.
16. 16. Follmann, H. & Häberlein, I. (1995) Thioredoxins: universal, yet specific thiol-disufide redox cofactors. Biofactors 5, 147-156.
17. 17. Holmgren, A. & Asund, F. (1995) Glutaredoxin. Methods Enzymol. 252, 283-292.
18. 15N NMR relaxation measurements. Biochemistry 36, 5029-5044.
19. 19. Chivers, P.T., Prehoda, K.E. & Raines, R.T. (1997) The CXXC motif: a rheostat in the active site. Biochemistry 36, 4061-4066.
20. 20. Edman, J.C., Ellis, L., Blacher, R.W, Roth, R.A. & Rutter, W.J. (1985) Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317, 267-270.
21. 21. Schirra, H.J., Renner, C., Czisch, M., Huber-Wunderlich, M., Holak, T.A. & Glockshuber, R. (1998) Structure of reduced DsbA from Escherichia coli in solution. Biochenistry 37, 6263-6276.
22. 22. Wilson, R., Ainscough, R., Anderson, K., Baynes, C, Berks, M., Bonfield, J., Burton, J., Connell, M., Copsey, T., Cooper, J., Coulson, A., Craxton, M., Dear, S., Du, Z., Durbin, R., Favello, A., Fraser, A., Fulton, L., Gardner, A., Green, P., Hawkins, T., Millier, L., Jier, M., Johnston, L., Jones, M., Kershaw, J., Kirsten, J., Laisster, N., Latreille, P., Lightning, J., Lloyd, C., Mortimore, B., O'Callaghan, M., Parsons, J., Percy, C., Rifken, L., Roopra, A., Saunders, D., Shownkeen, R., Sims, M., Smaldon, N., Smith, A., Smith, M., Sonnhammer, E., Staden, R., Sulston, J., Thierry-Mieg, J., Thomas, K., Vaudin, M., Vaughan, K., Waterston, R., Watson, A., Weinstock, L., Wilkinson-Sproat, J. & Wohldman, P. (1994) 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature 368, 32-38.
23. 23. Rivera-Madrid, R., Marinho, P., Brugidou, C., Chartier, Y. & Meyer, Y. (1993) Nucleotide sequence of a cDNA clone encoding an Arabidopsis thaliana thioredoxin h. Plant Physiol. 102, 327-328,
24. 24. Page, M.D. & Ferguson, S.J. (1997) Paracoccus denitrificans CcmG is a periplasmic protein-disulphide oxidoreductase required for c-and aa3-type cytochrome biogenesis; evidence for a reductase role in vivo. Mol Microbiol. 24, 977-990.
25. 25. Stanchev, B.S., Doughty, J., Scutt, C.P., Dickinson, H. & Croy, R.R. (1996) Cloning of PCPI, a member of a family of pollen coat protein (PCP) genes from Brassica oleracea encoding novel cysteine-rich proteins involved in pollen-stigma interactions. Plant J. 10, 303-313.
26. 26. Kurooka, H., Kalo, K., Minoguchi, S., Takahashi, Y., Ikeda, J., Habu, S., Osawa, N., Buchberg, A.M., Moriwaki, K., Shisa, H. & Honjo, T. (1997) Cloning and characterization of the nucleoredoxin gene that encodes a novel nuclear protein related to thioredoxin. Genomics 39, 331-339.
27. 27. Grauschopf, U., Winther, J.R., Korber, P., Dallinger, P. & Bardwell, J.C.A. (1995) Why is DsbA such an oxidizing disulfide catalyst? Cell 83, 947-955.
28. 28. Dyson, H.J., Holmgren, A. & Wright, P.E. (1988) Structural differences between oxidized and reduced thioredoxin monitored by two-dimensional 1H NMR spectroscopy. FEBS Lett. 228, 254-258.
29. 29. Kalisz, H.M., Nogoceke, E., Gommel, D., Hofmann, B., Flohé, L. & Hecht, H.J. (1999) Crystallisation and preliminary X-ray analysis of Tryparedoxinl from Crithidia fasciculata. Acta Cryst. D. (in press).
30. 30. Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
31. 31. Weichsel, A., Gasdaska, J.R., Powis, G. & Montfort, W.R. (1996) Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 4, 735-751.