A trojan horse approach for silencing thymidylate synthase

Biochemistry

Volumn 43, Issue 28, 2004, Pages 9177-9184

  West, Deborah K ^a   Porter, Donald C ^a   Saxl, Ruth L ^a   Maley, Frank ^a  

^a WADSWORTH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CHEMOTHERAPY; DIMERS; ESCHERICHIA COLI; TOXICITY;

MUTANTS; THYMIDYLATE SYNTHASE (TS);

PROTEINS;

ARGININE; CYSTEINE; DIMER; FLOXURIDINE PHOSPHATE; GLUTAMINE; MUTANT PROTEIN; PROTEIN SUBUNIT; THYMIDYLATE SYNTHASE; TRYPTOPHAN;

AMINO ACID SEQUENCE; ARTICLE; CELL DEATH; CELL GROWTH; DRUG TARGETING; ENZYME DENATURATION; ENZYME INHIBITION; ESCHERICHIA COLI; HUMAN; HUMAN CELL; IN VITRO STUDY; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN FOLDING;

ANTINEOPLASTIC AGENTS; CELL DEATH; CELL LINE, TUMOR; ENZYME INHIBITORS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FLUORODEOXYURIDYLATE; HUMANS; MUTATION; PROTEIN RENATURATION; PROTEIN SUBUNITS; THYMIDYLATE SYNTHASE;

EQUUS CABALLUS; ESCHERICHIA COLI;

EID: 3142704386     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049105v     Document Type: Article

References (44)

1. 2 infection of a thymine requiring mutant of Escherichia coli, J. Bacteriol. 68, 80-88.
2. Heidelberger, C., Chaudhuri, N. K., Danenberg, P., Mooren, D., Grisbach, L., Duschinsky, R., Schnitzer, R. J., Pleven, E., and Scheiner, J. (1957) Fluorinated Pyrimidines, a new class of tumour-inhibitory compounds, Nature 179, 663-666.
3. Cohen, S. S., Flaks, J. G., Barner, H. D., Loeb, M. R., and Lichtenstein, J. (1958) The mode of action of 5-fluorouracil and its derivatives, Proc. Natl. Acad. Sci. U.S.A. 44, 1004-1012.
4. Danenberg, D. V., Langenbach, R. J., and Heidelberger, C. (1974) Structures of reversible and irreversible complexes of thymidylate synthetase and fluorinated pyrimidine nucleotides, Biochemistry 13, 926-933.
5. Santi, D. V., McHenry, C. S., and Sommer, H. (1974) Mechanism of interaction of thymidylate synthetase with 5-fluorodeoxyuridylate, Biochemistry 13, 471-480.
6. Bellisario, R. L., Maley, G. F., Galivan, J. H., and Maley, F. (1976) The amino acid sequence at the FdUMP binding site of thymidylate synthetase, Proc. Natl. Acad. Sci. U.S.A. 73, 1848-1852.
7. Pogolotti, A. L., Ivanetich, K. M., Sommer, H., and Santi, D. V. (1976) Thymidylate synthetase: Studies on the peptide containing covalently bound 5-fluoro-2′-deoxyuridylate and methylene tetrahydrofolate, Biochem. Biophys. Res. Commun. 70, 972-978.
8. Friedkin, M., and Kornberg, A. (1957) The enzymatic conversion of deoxyuridylic acid to thymidylic acid and the participation of tetrahydrofolic acid, in The Chemical Basis of Heredity (McElroy, W. O., and Glass, B., Eds.) pp 609-614, The Johns Hopkins Press, Baltimore, MD.
9. Ullman, B., Lee, M., Martin, D. W., Jr., and Santi, D. V. (1978) Cytotoxicity of 5-fluoro-2′-deoxyuridine: Requirement for reduced folate cofactors and antagonism by methotrexate, Proc. Natl. Acad. Sci. U.S.A. 75, 980-983.
10. Yin, M.-B., Zakrzewski, S. F., and Hakala, M. T. (1983) Relationship of cellular folate cofactor pools to the activity of 5-fluorouracil, Mol. Pharmacol. 23, 190-197.
11. Romanine, A., Li, W. W., Colofiore, J. R., and Bertino, J. R. (1992) Leucovorin enhances cytotoxicity of trimetrexate/fluorouracil, but not methotrexate/fluorouracil, in CCRF-CEM cells, J. Natl. Cancer Inst. 84, 1033-1038.
12. Baugh, C. M., and Krumdiek, C. L. (1971) Naturally occurring folates, Ann. N.Y. Acad. Sci. 186, 7-28.
13. Brown, J. P., Davidson, G. E., and Scott, J. M. (1974) The identification of the forms of folate found in the liver, kidney, and intestine of the monkey and their biosynthesis from exogenous pteryolglutamate (folic acid), Biochim. Biophys. Acta 343, 78-88.
14. Priest, D. G., and Mangum, M. (1981) Relative affinity of 5,10-methylenetetrahydrofolyl-polyglutamates for the Lactobacillus casei thymidylate synthase-5-fluorodeoxyuridylate binary complex, Arch. Biochem. Biophys. 210, 118-123.
15. Kisliuk, R. L., Gaumont, I., Lafer, E., Baugh, C. M., and Montgomery, J. A. (1981) Polyglutamyl derivatives of tetrahydrofolate as substrates for Lactobacillus casei, Biochemistry 20, 929-934.
16. Kisliuk, R. L. (2003) Deaza analogues of folic acid as antitumor agents. Curr. Pharmaceut. Design 9, 2615-2625.
17. Maley, F., Pedersen-Lane, J., and Changchien, L.-M. (1995) Complete restoration of activity to inactive mutants of Escherichia coli thymidylate synthase: Evidence that thymidylate synthase is a half-the-sites activity enzyme, Biochemistry 34, 1469-1474.
18. Saxl, R. L., Changchien, L.-M., Hardy, L. W., and Maley, F. (2001) Parameters affecting the restoration of activity to inactive mutants of thymidylate synthase via subunit exchange: Further evidence that thymidylate synthase is a half-the-sites activity enzyme, Biochemistry, 40, 5275-5282.
19. Leary, R. P., Beaudette, N., and Kisliuk, R. L. (1975) Interaction of deoxyuridylate with thymidylate synthetase, J. Biol. Chem. 250, 4864-4868.
20. Beaudette, N. V., Langerman, N., Kisliuk, R. L., and Gaumont, Y. (1977) A calorimetric study of the binding of 2′-deoxyuridine-5′-phosphate and 5-fluoro-2′-deoxyuridine-5′-phosphate to thymidylate synthetase, Arch. Biochem. Biophys. 179, 272-278.
21. Galivan, J. H., Maley, G. F., and Maley, F. (1976) Factors affecting substrate binding in Lactobacillus casei thymidylate synthase as studied by equilibrium dialysis, Biochemistry 15, 356-363.
22. Galivan, J., Noonan, J., and Maley, F. (1977) Studies on the reactivity of the essential cysteine of thymidylate synthase, Arch. Biochem. Biophys. 184, 336-345.
23. Levitzski, A., Stallcup, W. B., and Koshland, D. E., Jr. (1971) Half-of-the-sites reactivity and the conformational states of cytidine triphosphate synthetase, Biochemistry 10, 3371-3378.
24. Spencer, H. T., Villafranca, J. E., and Appelman, J. R. (1997) Kinetic scheme for thymidylate synthase from Escherichia coli: determination from measurements of ligand binding, primary and secondary isotope effects and pre-steady-state catalysis, Biochemistry 36, 4212-4222.
25. Anderson, A. C., O'Neil, R. H., DeLano, W. L., and Stroud, R. M. (1999) The structural mechanism for half-the-sites reactivity in an enzyme. Thymidylate synthase involves a relay of changes between subunits, Biochemistry 38, 13829-13836.
26. Changchien, L.-M., Garibian, A., Frasca, V., Lobo, A., Maley, G. F., and Maley, F. (2000) High level expression of Escherichia coli and Bacillus subtilis thymidylate synthase, Protein Expression Purif. 19, 265-270.
27. Pedersen-Lane, J., Maley, G. F., Chu, E., and Maley, F. (1997) High-level expression of human thymidylate synthase, Protein Expression Purif. 10, 256-262.
28. Wahba, A. J., and Friedkin, M. (1961) Direct spectrophotometric evidence for the oxidation of tetrahydrofolate during the enzymatic synthesis of thymidylate, J. Biol. Chem. 236, PC 11-12.
29. Roberts, D. (1966) An isotopic assay for thymidylate synthetase, Biochemistry 5, 3546-3548.
30. Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4, Nature 227, 680-685.
31. Maniatis, T., Fritsch, E. G., and Sambrook, J. (1982) Molecular Cloning, A Laboratory Manual, p 468, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
32. Greene, P. J., Maley, F., Pedersen-Lane, J., and Santi, D. V. (1993) Catalytically active cross-species heterodimers of thymidylate synthase, Biochemistry 32, 10283-10288.
33. Staniforth, R. A., Giannini, S., Higgins, L. D., Conroy, M. J., Horinslow, A. M., Jerala, R., Craven, C. J., and Waltho, J. P. (2001) Three-dimensional domain swapping in the foled and molten-globule states of cystatins, an amyloid-forming structural superfamily, EMBO J. 20, 4774-4781.
34. Carreras, C. W., and Santi, D. V. (1995) The catalytic mechanism and structures of thymidylate synthase, Annu. Rev. Biochem. 64, 721-762.
35. Strop, P., Changchien, L.-M., Maley, F., and Montfort, W. R. (1997) Crystal structures of a marginally active thymidylate synthase mutant, Arg 1264→ Glu, Protein Sci. 6, 2509-2511.
36. Parker, W. B. and Cheng, Y. C. (1990) Metabolism and mechanism of action of 5-fluoro-uracil, Pharmacol. Ther. 48, 381-395.
37. Breitman, T. R., Bradford, R. M., and Cannon, W. D., Jr. (1967) Use of exogenous deoxythymidylic acid to label the deoxyribonucleic acid of growing wild type Escherichia coli, J. Bacteriol. 93, 1471-1472.
38. Hovmöller, S., and Zhou, T. (2004) Why are both ends of the polypeptide chain on the outside of proteins? Proteins: Struct., Funct., Genet. 55, 219-222.
39. Studier, F. W., Rosenberg, A. H., Dunn, J. J., and Dubendorff, J. W. (1990) Use of T7 RNA polymerase to direct expression of cloned genes, Methods Enzymol. 185, 60-89.
40. Went, S. R., and Schachman, H. K. (1987) Shared active sites in oligomeric enzymes: Model studies with defective mutants of asparatate transcarbamoylase produced by site-directed mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 84, 31-35.
41. Coleman, C. S., Stanley, B. A., Viswanath, R., and Pegg, A. (1994) Rapid exchange of subunits of mammalian ornithine decarboxylase, J. Biol. Chem. 269, 3155-3158.
42. Turner, M. A., Simpson, A., McInnes, R. R., and Howell, P. L. (1997) Human arginosuccinate lyase: A structural basis for intragenic complementation. Proc. Natl. Acad. Sci. U.S.A. 94, 9063-9068.
43. Kang, C., Kim, S., and Fromm, H. J. (1996) Subunit complementation of Escherichia coli adenylsuccinate synthetase, J. Biol. Chem. 271, 29722-29728.
44. Ozturk, D. H., Dorfman, R. H., Scapin, G., Sacchettini, J. C., and Grubmeyer, D. (1995) Structure and function of Salmonella typhimurium orotate phosphoribosyl transferase: Protein complementation reveals shared active sites, Biochemistry 34, 10764-10770.