Fluorescence energy transfer studies of human deoxycytidine kinase: Role of cysteine 185 in the conformational changes that occur upon substrate binding

Biochemistry

Volumn 45, Issue 11, 2006, Pages 3534-3541

  Mani, Rajam S ^a   Usova, Elena V ^b   Cass, Carol E ^a   Eriksson, Staffan ^b  

^a UNIVERSITY OF ALBERTA   (Canada)

^b SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ENERGY TRANSFER; FLUORESCENCE; HUMAN ENGINEERING; MUTAGENESIS; PHOSPHORESCENCE; SUBSTRATES;

FLUORESCENCE ENERGY; HUMAN DEOXYCYTIDINE KINASE (DCK); PURINE NUCLEOSIDES; PYRIMIDINE;

ENZYMES;

ALANINE; CYSTEINE; DEOXYCYTIDINE KINASE; FLUORESCENT DYE; MALEIMIDE DERIVATIVE; MUTANT PROTEIN; N (1 PYRENYL)MALEIMIDE; NUCLEOSIDE DERIVATIVE; PRODRUG; PURINE; PYRENE DERIVATIVE; PYRIMIDINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; ENERGY TRANSFER; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE RESONANCE ENERGY TRANSFER; MUTATION; PRIORITY JOURNAL; PROTEIN PURIFICATION; WILD TYPE;

ALANINE; BINDING SITES; CYSTEINE; DEOXYCYTIDINE KINASE; ENERGY TRANSFER; ENZYME ACTIVATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENT DYES; HUMANS; KINETICS; MALEIMIDES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; NUCLEOSIDES; PHOSPHATES; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; TRYPTOPHAN;

EID: 33645224930     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052652b     Document Type: Article

References (27)

1. Eriksson, S., and Wang, L. (1997) Substrate specificity, expression, and primary sequences of deoxynucleoside kinases, implications for chemotherapy, Nucleosides Nucleotides 16, 653-659.
2. Usova, E. V., and Eriksson, S. (1997) The effects of high salt concentrations on the regulation of the substrate specificity of human recombinant deoxycytidine kinase, Eur. J. Biochem. 248, 762-766.
3. Eriksson, S., Kierdaszuk, B., Munch-Petersen, B., Oberg, B., and Johansson, N. O. (1991) Comparison of the substrate specificities of human thymidine kinase 1 and 2 and deoxycytidine kinase toward antiviral and cytostatic nucleoside analogs, Biochem. Biophys. Res. Commun. 176, 586-592.
4. Chottiner, E. G., Shewach, D. S., Datta, N. S., Ashcraft, E., Gribbin, D., Ginsburg, D., Fox, I. H., and Mitchell, B. S. (1991) Cloning and expression of human deoxycytidine kinase cDNA, Proc. Natl. Acad. Sci. U.S.A. 88, 1531-1535.
5. Sabini, E., Ort, S., Monnerjahn, C., Konrad, M., and Lavie, A. (2003) Structure of human dCK suggests strategies to improve anticancer and antiviral therapy, Nat. Struct. Biol. 10, 513-519.
6. Bohman, C., and Eriksson, S. (1988) Deoxycytidine kinase from human leukemic spleen: Preparation and characteristics of homogeneous enzyme, Biochemistry 27, 4258-4265.
7. Ives, D. H., and Durham, J. P. (1970) Deoxycytidine kinase. 3. Kinetics and allosteric regulation of the calf thymus enzyme, J. Biol. Chem. 245, 2285-2294.
8. Hughes, T. L., Hahn, T. M., Reynolds, K. K., and Shewach, D. S. (1997) Kinetic analysis of human deoxycytidine kinase with the true phosphate donor uridine triphosphate, Biochemistry 36, 7540-7547.
9. Shewach, D. S., Reynolds, K. K., and Hertel, L. (1992) Nucleotide specificity of human deoxycytidine kinase, Mol. Pharmacol. 42, 518-524.
10. Kierdaszuk, B., Rigler, R., and Eriksson, S. (1993) Binding of substrates to human deoxycytidine kinase studied with ligand-dependent quenching of enzyme intrinsic fluorescence. Biochemistry 32, 699-707.
11. Mani, R. S., Usova, E. V., Eriksson, S., and Cass, C. E. (2003) Hydrodynamic and Spectroscopic Studies of Substrate Binding to Human Recombinant Deoxycytidine Kinase, Nucleosides, Nucleotides Nucleic Acids 22, 175-192.
12. Johnsamuel, J., Eriksson, S., Oliveira, M., and Tjarks, W. (2005) Docking simulation with a purine nucleoside specific homology model of deoxycytidine kinase, a target enzyme for anticancer and antiviral therapy, Bioorg. Med. Chem. 13, 4160-4167.
13. Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77, 51-59.
14. Usova, E. V., and Eriksson, S. (2002) Identification of residues involved in the substrate specificity of human and murine dCK, Biochem. Pharmacol. 64, 1559-1567.
15. Betcher-Lange, S. L., and Lehrer, S. S. (1978) Pyrene excimer fluorescence in rabbit skeletal α,α-tropomyosin labeled with N-(1-pyrene)maleimide. A probe of sulfhydryl proximity and local chain separation, J. Biol. Chem. 253, 3757-3760.
16. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
17. Parker, C. A., and Reese, W. T. (1960) Correction of fluorescence spectra and measurement of fluorescence quantum efficiency, Analyst (London) 85, 587-592.
18. Eftink, M. R., Jia, Y., and Hu, D. (1995) Fluorescence Studies with Tryptophan Analogues: Excited-State Interaction Involving the Side Chain Amino Group, J. Phys. Chem. 99, 5713-5723.
19. Förster, T. (1965) in Modern Quantum Chemistry, Istanbul Lectures, Academic Press, New York.
20. Selvin, P. R. (1995) Fluorescence resonance energy transfer, Methods Enzymol. 246, 300-334.
21. Mani, R. S., and Kay, C. M. (1985) A fluorimetry study of N-(1-pyrenyl)iodoacetamide-labeled bovine brain S-100a protein, FEBS Lett. 181, 275-280.
22. Mani, R. S., Usova, E. V., Eriksson, S., and Cass, C. E. (2004) Fluorescence studies of substrate binding to human recombinant deoxycytidine kinase, Nucleosides, Nucleotides Nucleic Acids 23, 1343-1346.
23. Lehrer, S. S., and Leavis, P. C. (1978) Solute quenching of protein fluorescence, Methods Enzymol. 49, 222-236.
24. Johansson, K., Ramaswamy, S., Ljungcrantz, C., Knecht, W., Piskur, J., Munch-Petersen, B., Eriksson, S., and Eklund, H. (2001) Structural basis for substrate specificity of cellular deoxyribonucleoside kinases, Nat. Struct. Biol. 8, 616-620.
25. Hapke, D. M., Stegmann, A. P., and Mitchell, B. S. (1996) Retroviral transfer of deoxycytidine kinase into tumor cell lines enhances nucleoside toxicity, Cancer Res. 56, 2343-2347.
26. Wu, C. W., and Stryer, L. (1972) Proximity relationships in rhodopsin, Proc. Natl. Acad. Sci. U.S.A. 69, 1104-1108.
27. Cheung, H. C., Gonsoulin, F., and Garland, F. (1983) Fluorescence energy transfer studies on the proximity of the two essential thiols of myosin subfragment-1, J. Biol. Chem. 258, 5775-5786.