Expression and characterization of the Trypanosoma cruzi dihydrofolate reductase domain

Molecular and Biochemical Parasitology

Volumn 76, Issue 1-2, 1996, Pages 175-185

  Reche, Pedro ^a   Arrebola, Rosalia ^a   Santi, Daniel V ^b   Gonzalez Pacanowska, Dolores ^a   Ruiz Perez, Luis M ^a  

^a INSTITUTO DE PARASITOLOGÍA Y BIOMEDICINA LÓPEZ NEYRA   (Spain)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

dihydrofolate reductase; folate metabolism; heterologous expression; protozoal enzymes; Trypanosoma cruzi

Indexed keywords

DIHYDROFOLATE REDUCTASE;

ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; ENZYME ANALYSIS; FOLATE METABOLISM; GENE EXPRESSION; GENETIC ANALYSIS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; TRYPANOSOMA CRUZI;

ANIMALIA; ESCHERICHIA COLI; FELIS CATUS; TRYPANOSOMA; TRYPANOSOMA CRUZI;

EID: 0029925445     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/0166-6851(95)02557-X     Document Type: Article

References (43)

1. Blakey, R.L. (1984) Dihydrofolate reductase. In: Folates and Pteridines (Blakey, R.L. and Benkovic, S.J., eds), Vol. 1, pp. 191-253. John Wiley and Sons, New York.
2. Santi, D.V. and Danenberg, P.V. (1984) Folates in pyrimidine nucleotide biosynthesis. In: Folates and Pteridines (Blakey, R.L. and Benkovic, S.J., eds), Vol. 1, pp. 343-396. John Wiley and Sons, New York.
3. Ferone, R. and Roland, S. (1980) Dihydrofolate reductase-thymidylate synthase, a bifunctional polypeptide from Crithidia fasticulata. Proc. Natl. Acad. Sci. USA 77, 5802-5806
4. Garrett, C.E., Coderre, J.A., Meek, T.D., Garvey, E.P., Claman, D.M., Beverley, S.M. and Santi, D.V. (1984) A bifunctional thymidylate synthase-dihydrofolate reductase in protozoa. Mol. Biochem. Parasitol. 11, 257-265.
5. Ivanetich, K.M. and Santi, D.V. (1990) Bifunctional thymidylate synthase-dihydrofolate reductase in protozoa. FASEB J. 4, 1591-1597.
6. Meek, T.D., Garvey, E.P. and Santi, D.V. (1985) Purification and characterization of the bifunctional thymidylate synthase-dihydrofolate reductase from methotrexate-resistant Leishmania tropica. Biochemistry 24, 678-686
7. Knighton, D.R., Kan, C.-C., Howland, E., Janson, C.A., Hostomska, Z., Welsh, K.M. and Matthews D.A. (1994) Structure and kinetic channeling in bifunctional dihydrofolate reductase-thymidylate synthase. Struct. Biol. 1, 186-194.
8. Ferone, R. (1984) Dihydrofolate reductase inhibitors. In: Antimalarial Drugs. Vol. II. Handbook of Experimental Pharmacology, Vol. 68 (Peter, W. and Richards, W.H.G. eds.), pp. 207-221. Springer-Verlag, New York.
9. Grossman, P.L. and Regmington, J.S. (1979) The effect of trimethoprim and sulfamethoxazole on Toxoplasma gondii in vitro and in vivo. Am. J. Trop. Med. Hyg. 28, 445-445.
10. Winston, D.J., Lau, W.K., Gale, R.P. and Young, L.S. (1980) Trimethoprim-sulfamethoxazole for treatment of Pneumocystis carinii infection. Ann. Intern. Med. 92, 762-769.
11. Appleman, J.R., Howell, E.E., Kraut, J., Kühl, M. and Blakley, R.L. (1988) Role of aspartate 27 in the binding of methotrexate to dihydrofolate reductase from Eschenchia coll. J. Biol. Chem. 263, 9187-9198.
12. Appleman, J.R., Prendergast, N., Delcamp, T.J., Freisheim, J.H. and Blakley, R.L. (1988). Kinetics of the formation and isomerization of methotrexate complexes of recombinant human dihydrofolate reductase. J. Biol. Chem. 263, 10304-10313.
13. Reche, P., Arrebola, R., Olmo, A., Santi, D.V., Gonzalez-Pacanowska, D. and Ruiz-Perez, L.M. (1994) Cloning and expression of the dihydrofolate reductase-thymidylate synthase gene from T. cruzi. Mol. Biochem. Parasitol. 65, 257-258.
14. Blakey, R.L. (1960) Crystalline dihydropteroylglutamic acid. Nature 188, 231-232.
15. Bethell, G.S., Ayers, J.S. and Hancock, W.S. (1979) A novel method of activation of cross-linked agarose with 1,1′-carbonyl diimidazole which gives a matrix for affinity chromatography devoid of additional charged groups. J. Biol. Chem. 254, 2572-2574.
16. Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning; A Laboratory Manual (2nd, Edn.). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
17. Sanger, F., Nicklen, S. and Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
18. Grumont, R., Sirawaraporn, W. and Santi, D.V. (1988) Heterologous expression of the bifunctional thymidylate synthase-dihydrofolate reductase from Leishmania major. Biochemistry 27, 3776-3784.
19. Sirawaraporn, W., Sirawaraporn, R., Cowman, A.F., Yuthavong, Y. and Santi, D.V. (1990) Heterologous expression of an active thymidylate synthase-dihydrofolate reductase from Plasmodinm falciparum. Biochemistry 29, 10779-10785.
20. Read, S.M. and Northcote, D.H. (1981) Minimization of variation in the response to different proteins of the Coomassie blue G dye-binding assay for protein. Anal. Biochem. 116, 53-64.
21. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227, 680-685.
22. Hillcoat, B.L., Nixson, P.F. and Blakey, R.L. (1967) Effect of substrate decomposition on the spectrophotometric assay of dihydrofolate reductase. Anal. Biochem. 21, 1123-1128.
23. Morrison, J.F. and Walsh, C.T. (1988) The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. 61, 202-301.
24. Bolin, J.T., Filman, D.J., Matthews, D.A., Hamlin, R.C. and Kraut, J. (1982) Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J. Biol. Chem. 257, 13650-13662
25. Filman, D.J., Bolin, J.T., Matthews, D.A. and Kraut, J. (1982) Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution, II. Environment of bound NADPH and implications for catalysis. J. Biol. Chem. 257, 13663-13672.
26. Bystroff, C., Oatley, S.J. and Kraut, J. (1990) Crystal structures of Escherichia coli dihydrofolate reductase: substrate binding and a model for the transition state. Biochemistry 29, 3263-3277.
27. Gamier, J., Osguthorpe, D.J. and Robson, B. (1978) Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120, 97-120.
28. Chou, P. and. Fasman, G.D. (1978) Empirical predictions of protein conformation. Annu. Rev. Biochem. 47, 251 276.
29. Hardy, L.W., Finer-Moore, J.S., Montfort, W.R., Jones, M.O., Santi, D.V. and Stroud, R.M. (1987) Atomic structure of thymidylate synthase: target for rational drug design. Science 235, 448-455.
30. Perry, K.M., Fauman, E.B., Finer-Moore, J.S., Montfort, W.R., Maley, G.F., Maley, F. and Stroud, R.M. (1990) Plastic adaptation towards mutations in proteins: structural comparison of thymidylate synthases. Prot. Struct. Funct. Genet, 8, 315-333.
31. Sirawaraporn W., Prapunwattana, P., Sirawaraporn, R., Yuthavong, Y. and Santi, D.V. (1993) The dihydrofolate reductase domain of Plasmodium falciparum thymidylate synthase-dihydrofolate reductase. J. Biol. Chem. 29, 21637-21644.
32. Stone, S.R. and Morrison, J.F. (1984) Catalytic mechanism of the dihydrofolate reductase reaction as determined by pH studies. Biochemistry 23, 2753-2758.
33. Fierke, C.A., Johnson, K.A. and Benkovic, S.J. (1987) Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry 26, 4085-4092.
34. Andrews, J., Fierke, C.A., Birdsall, B., Ostler, G., Feeney, J., Roberts, G.C. and Benkovic, S.J. (1989) A kinetic study of wild-type and mutant dihydrofolate reductases from Lactobacillus casei. Biochemistry 28, 5743-5750.
35. Beard, W.A., Appleman, J.R., Delcamp, T.J., Freisheim, J.H. and Blakley, R.L. (1989) Hydride transfer by dihydrofolate reductase. Causes and consequences of the wide range of rates exhibited by bacterial and vertebrate enzymes. J. Biol. Chem. 264, 9391-9399.
36. Schweitzer, B.I., Srimatkandada, S., Gritsman, H., Sheridan, R., Venkataraghavan, R. and Bertino, J.R. (1989) Probing the role of two hydrophobic active site residues in the human dihydrofolate reductase by site-directed mutagenesis. J. Biol. Chem. 264, 20786-20795.
37. Thillet, J., Absil, J., Stone, S.R. and Pictet, R. (1988) Site-directed mutagenesis of mouse dihydrofolate reductase. Mutants with increased resistance to methotrexate and trimethoprim. J. Biol. Chem. 263, 12500-125008.
38. Jaffe, J.J., McCormack, Jr., J.J. and Gutteridge, W.E. Dihydrofolate reductases within the genus Trypanosoma. Exp. Parasitol. 25, 311-318.
39. Sirawaraporn, W., Sersrivanich, R., Booth, R.G., Hasch, C., Neal, R.A. and Santi, D.V. (1988) Selective inhibition of Leishmania dihydrofolate reductase and Leishmania growth by 5-benzil-2-4-diaminopyrimidines. Mol. Biochem. Parasitol. 31, 79-85.
40. Burchall, J.J. (1979) The development of the diaminopyrimidines. J. Antimicrob. Chemother. 5 (Suppl. B), 3-14.
41. Stone, S.R., Montgomery, J.A. and Morrison, J.F. (1984) Inhibition of dihydrofolate reductase from bacterial and vertebrate sources by folate, aminopterin, methotrexate and their 5-deaza analogues. Biochem. Pharmacol. 33, 175-179.
42. Stone, S.R. and Morrison, J.F. (1986) Mechanism of inhibition of dihydrofolate reductase from bacterial and vertebrate sources by various classes of folate analogues. Biochim. Biophys. Acta 869, 275-285.
43. Garvey, E.P. and Santi, D.V. (1985) Limited proteolysis of the bifunctional thymidylate synthase-dihydrofolate reductase from Leishmania tropica. Proc. Natl. Acad. Sci. USA 82, 7188-7192.