Binding of ATP to TK1-like Enzymes Is Associated with a Conformational Change in the Quaternary Structure

Journal of Molecular Biology

Volumn 369, Issue 1, 2007, Pages 129-141

  Segura Peña, Dario ^a   Lutz, Stefan ^b   Monnerjahn, Christian ^c   Konrad, Manfred ^c   Lavie, Arnon ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^b EMORY UNIVERSITY   (United States)

^c MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

hTK1; phosphoryl transfer; quaternary structure; thymidine kinase; TmTK

Indexed keywords

ADENOSINE TRIPHOSPHATE; THYMIDINE KINASE; THYMIDINE KINASE 1;

ARTICLE; CONFORMATION; CONTROLLED STUDY; ELECTRON; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STRUCTURE; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; THERMOTOGA MARITIMA;

THERMOTOGA MARITIMA;

EID: 34247365953     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.104     Document Type: Article

References (36)

1. Spyrou G., and Reichard P. Dynamics of the thymidine triphosphate pool during the cell cycle of synchronized 3T3 mouse fibroblasts. Mutat. Res. 200 (1988) 37-43
2. Eriksson S., Thelander L., and Akerman M. Allosteric regulation of calf thymus ribonucleoside diphosphate reductase. Biochemistry 18 (1979) 2948-2952
3. Boucher P.D., Im M.M., Freytag S.O., and Shewach D. S. A novel mechanism of synergistic cytotoxicity with 5-fluorocytosine and ganciclovir in double suicide gene therapy. Cancer Res. 66 (2006) 3230-3237
4. Bello L.J. Regulation of thymidine kinase synthesis in human cells. Exp. Cell Res. 89 (1974) 263-274
5. Tommasi S., and Pfeifer G.P. Constitutive protection of E2F recognition sequences in the human thymidine kinase promoter during cell cycle progression. J. Biol. Chem. 272 (1997) 30483-30490
6. Chang Z.F., Huang D.Y., and Chi L.M. Serine 13 is the site of mitotic phosphorylation of human thymidine kinase. J. Biol. Chem. 273 (1998) 12095-12100
7. Li C.L., Lu C.Y., Ke P.Y., and Chang Z.F. Perturbation of ATP-induced tetramerization of human cytosolic thymidine kinase by substitution of serine-13 with aspartic acid at the mitotic phosphorylation site. Biochem. Biophys. Res. Commun. 313 (2004) 587-593
8. Ke P.Y., and Chang Z.F. Mitotic degradation of human thymidine kinase 1 is dependent on the anaphase-promoting complex/cyclosome-CDH1-mediated pathway. Mol. Cell. Biol. 24 (2004) 514-526
9. Ke P.Y., Kuo Y.Y., Hu C.M., and Chang Z.F. Control of dTTP pool size by anaphase promoting complex/cyclosome is essential for the maintenance of genetic stability. Genes Dev. 19 (2005) 1920-1933
10. Dobrovolsky V.N., Bucci T., Heflich R.H., Desjardins J., and Richardson F.C. Mice deficient for cytosolic thymidine kinase gene develop fatal kidney disease. Mol. Genet. Metab. 78 (2003) 1-10
11. Striepen B., Pruijssers A.J., Huang J., Li C., Gubbels M.J., Umejiego N.N., et al. Gene transfer in the evolution of parasite nucleotide biosynthesis. Proc. Natl Acad. Sci. USA 101 (2004) 3154-3159
12. Welin M., Kosinska U., Mikkelsen N.E., Carnrot C., Zhu C., Wang L., et al. Structures of thymidine kinase 1 of human and mycoplasmic origin. Proc. Natl Acad. Sci. USA 101 (2004) 17970-17975
13. Kenny L.M., Vigushin D.M., AL-Nahhas A., Osman S., Luthra S.K., Shousha S., et al. Quantification of cellular proliferation in tumor and normal tissues of patients with breast cancer by [18F] fluorothymidine-positron emission tomography imaging: evaluation of analytical methods. Cancer Res. 65 (2005) 1014-1012
14. Barthel H., Perumal M., Latigo J., He Q., Brady F., Luthra S.K., et al. The uptake of 3′-deoxy-3′-[18F]fluorothymidine into L5178Y tumours in vivo is dependent on thymidine kinase 1 protein levels. Eur. J. Nucl. Med. Mol. Imaging 32 (2005) 257-263
15. Birringer M.S., Claus M.T., Folkers G., Kloer D.P., Schulz G.E., and Scapozza L. Structure of a type II thymidine kinase with bound dTTP. FEBS Letters 579 (2005) 1376-1382
16. Kosinska U., Carnrot C., Eriksson S., Wang L., and Eklund H. Structure of the substrate complex of thymidine kinase from Ureaplasma urealyticum and investigations of possible drug targets for the enzyme. FEBS J. 272 (2005) 6365-6372
17. Bone R., Cheng Y.C., and Wolfenden R. Inhibition of thymidine kinase by P1-(adenosine-5′)-P5-(thymidine-5′)-pentaphosphate. J. Biol. Chem. 261 (1986) 5731-5735
18. Birringer M.S., Perozzo R., Kut E., Stillhart C., Surber W., Scapozza L., and Folkers G. High-level expression and purification of human thymidine kinase 1: quaternary structure, stability, and kinetics. Protein Expr. Purif. 47 (2006) 506-515
19. Barion S., Franchi M., Gallori E., and Di Giulio M. The first lines of divergence in the Bacteria domain were the hyperthermophilic organisms, the Thermotogales and the Aquificales, and not the mesophilic Planctomycetales. Biosystems 81 (2007) 13-19
20. Mongodin E.F., Hance I.R., Deboy R.T., Gill S.R., Daugherty S., Huber R., et al. Gene transfer and genome plasticity in Thermotoga maritima, a model hyperthermophilic species. J. Bacteriol. 187 (2005) 4935-4944
21. Munch-Petersen B., Tyrsted G., and Cloos L. Reversible ATP-dependent transition between two forms of human cytosolic thymidine kinase with different enzymatic properties. J. Biol. Chem. 268 (1993) 15621-15625
22. Berenstein D., Christensen J.F., Kristensen T., Hofbauer R., and Munch-Petersen B. Valine, not methionine, is amino acid 106 in human cytosolic thymidine kinase (TK1). Impact on oligomerization, stability, and kinetic properties. J. Biol. Chem. 275 (2000) 32187-32192
23. Sabini E., Ort S., Monnerjahn C., Konrad M., and Lavie A. Structure of human dCK suggests strategies to improve anticancer and antiviral therapy. Nature Struct. Biol. 10 (2003) 513-519
24. Derewenda Z.S., and Vekilov P.G. Entropy and surface engineering in protein crystallization. Acta Crystallog. sect. D 62 (2006) 116-124
25. Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 24 (1993) 795-800
26. Terwilliger T.C., and Berendzen J. Automated MAD and MIR structure solution. Act. Crystallog. sect. D 55 (1999) 849-861
27. Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallog. sect. D 56 (2000) 965-972
28. Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
29. Brunger A.T., Adams P.D., Clore G.M., DeLano W. L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallog. sect. D 54 (1998) 905-921
30. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
31. Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallog. 30 (1997) 1022-1025
32. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24 (1991) 946-950
33. Esnouf R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15 (1997) 132-134
34. Merritt E.A., and Murphy M.E. Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallog. sect. D 50 (1994) 869-873
35. Schelling P., Folkers G., and Scapozza L. A spectrophotometric assay for quantitative determination of kcat of herpes simplex virus type 1 thymidine kinase substrates. Anal. Biochem. 295 (2001) 82-87
36. Agarwal K.C., Miech R.P., and Parks Jr. R.E. Guanylate kinases from human erythrocytes, hog brain, and rat liver. Methods Enzymol. 51 (1978) 483-490