Toward a mechanism-based fluorescent assay for site-specific recombinases and topoisomerases: Assay design and syntheses of fluorescent substrates

Journal of the American Chemical Society

Volumn 118, Issue 48, 1996, Pages 12004-12011

  Panigrahi, Gagan ^a   Zhao, Bao Ping ^a   Krepinsky, Jiri J ^a   Sadowski, Paul D ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

DNA TOPOISOMERASE; RECOMBINASE;

ARTICLE; ENZYME ASSAY; ENZYME BINDING; ENZYME SUBSTRATE; FLUORESCENCE; NONHUMAN; TECHNIQUE;

EID: 0030472689     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9612920     Document Type: Article

References (29)

1. Champoux, J. J. In DNA Topology and Its Biological Effects; Cozzarelli, N. R., Wang, J. C., Eds.; Cold Spring Harbor Laboratory: Cold Spring Harbor, NY, 1990; pp 217-262.
2. Sadowski, P. D. FASEB J. 1993, 7, 760.
3. Kikuchi, Y.; Nash, H. Proc. Natl. Acad. Sci. U.S.A. 1979, 76, 3760.
4. Krasnow, M. A.; Cozzarelli, N. R. Cell 1983, 32, 1313.
5. Hartley, J. L.; Donelson, J. E. Nature 1980, 286, 860.
6. Futcher, A. B. J. Theor. Biol. 1986, 119, 197.
7. Sadowski, P. D. Prog. Nucleic Acids Res. Mol Biol. 1995, 51, 53.
8. Argos, P.; Landy, A.; Abremski, K.; Egan, J. B.; Haggard-Ljundquist, E.; Hoess, R. H.; Kahn, M. L.; Kalionis, B.; Narayana, S. V. L.; Pierson, L. S.; Steraberg, N.; Leong, J. M. EMBO J. 1986, 5, 433.
9. Abremski, K.; Hoess, R. H. Protein Eng. 1992, 53, 87.
10. Pan, G.; Sadowski, P. D. J. Biol. Chem. 1992, 267, 12397.
11. Pan, G.; Luetke, K.; Juby, C. D.; Brousseau, R.; Sadowski, P. D. J. Biol. Chem. 1993, 268, 3683.
12. Sadowski, P. D.; Pan, G.; Brousseau; R. Methods Mol. Genet. 1995, 6, 186.
13. Liu, L. F. Annu. Rev. Biochem. 1989, 58, 351.
14. Pan, H.; Clary, D.; Sadowski, P. D. J. Biol. Chem. 1991, 266, 11347.
15. Zhao, B. P.; Panigrahi, G.; Sadowski, P. D.; Krepinsky, J. J. Tetrahedron Lett. 1996, 37, 3093.
16. FLP Y343F means that the tyrosine residue at position 343 has been changed to phenylalanine. This nomenclature was applied to the other mutations as well.
17. Prasad, P. V.; Young, L.-J.; Jayaram, M. Proc. Natl. Acad. Sci. U.S.A. 1987, 84, 2189.
18. Evans, B. R.; Chen, J.-W.; Parsons, R. L.; Bauer, T. K.; Teplow, D. B.; Jayaram, M. J. Biol. Chem. 1990, 265, 18504.
19. Parsons, R. L.; Prasad, P. V.; Harshey, R. M.; Jayaram, M. Mol. Cell. Biol. 1988, 8, 3303.
20. Zhu, X.-D.; Sadowski, P. D. J. Biol. Chem. 1995, 270, 23044.
21. Himel, C. M.; Chan, L.-M. In Biochemical Fluorescence: Concepts; Chen, R. F.; Edelhoch, H., Eds.; Marcel Dekker: New York, 1975; pp 607-632.
22. Bayer, E.; Bleicher, K.; Maier, M. Z Naturforsch. 1995, 50B, 1096.
23. Bayer, E; Maier, M.; Bleicher, K.; Gaus, H.-J. Z Naturforsch. 1995, 50B, 671.
24. All nucleotide conjugates with tyrosine or other carboxylic acids, e.g., 3′-tyrosyl-oligonucleotide, contain carboxamide rather than the carboxyl group. The conversion of the carboxyl group to its amide occurs during the ammonolysis step used to remove the oligonucleotide conjugate from the solid support.
25. (a) Graebe, C. Liebigs Ann. Chem. 1871, 158, 294.
26. (b) Goldschmiedt, G.; Wegscheider, R. Monatshefte Chem. 1883, 4, 238.
27. (c) Banmvarth, W. Helv. Chim. Acta 1988, 71, 1517.
28. (d) Chaikovskii, V. V.; Novikov, A. N. Zh. Org. Khim. 1984, 20, 1482.
29. (e) Radner, F. Acta Chem. Scand. 1989, 43, 481.