Advertisement

Biochemistry (Moscow)

, 73:289 | Cite as

Isolation and physicochemical properties of tankyrase of human embryonic kidney cells of line 293

  • N. N. Sidorova
  • A. O. Fadeev
  • A. N. KuimovEmail author
Article

Abstract

We have isolated and purified endogenous cytosolic tankyrase from human embryonic kidney cells of line 293. Our data confirm a model of De Rycker and Price who consider that tankyrase is a master scaffolding protein capable of regulating assembly of large protein complexes. We have also studied kinetic characteristics of tankyrase in the complex, pH dependence of the enzyme activity, and its physicochemical properties.

Key words

tankyrase poly(ADP-ribose) PARP ADP-ribosylation kidney 

Abbreviations

PARP

poly(ADP-ribose) polymerase

References

  1. 1.
    Otto, H., Reche, P. A., Bazan, F., Dittmar, K., Haag, F., and Koch-Nolte, F. (2005) BMC Genomics, 6, 139.PubMedCrossRefGoogle Scholar
  2. 2.
    Smith, S., Giriat, I., Schmitt, A., and de Lange, T. (1998) Science, 282, 1484–1487.PubMedCrossRefGoogle Scholar
  3. 3.
    Donigian, J. R., and de Lange, T. (2007) J. Biol. Chem., 282, 22662–22667.PubMedCrossRefGoogle Scholar
  4. 4.
    Smith, S., and de Lange, T. (1999) J. Cell Sci., 112, 3649–3656.PubMedGoogle Scholar
  5. 5.
    Chi, N.-W., and Lodish, H. F. (2000) J. Biol. Chem., 275, 38437–38444.PubMedCrossRefGoogle Scholar
  6. 6.
    Lyons, R. J., Deane, R., Lynch, D. K., Ye, Z. S., Sanderson, G. M., Eyre, H. J., Sutherland, G. R., and Daly, R. J. (2001) J. Biol. Chem., 276, 17172–17180.PubMedCrossRefGoogle Scholar
  7. 7.
    Seimiya, H., and Smith, S. (2002) J. Biol. Chem., 277, 14116–14126.PubMedCrossRefGoogle Scholar
  8. 8.
    Sbodio, J. I., and Chi, N. W. (2002) J. Biol. Chem., 277, 31887–31892.PubMedCrossRefGoogle Scholar
  9. 9.
    Muramatsu, Y., Ohishi, T., Sakamoto, M., Tsuruo, T., and Seimiya, H. (2007) Cancer Sci., 98, 850–857.PubMedCrossRefGoogle Scholar
  10. 10.
    Kuimov, A. N., and Terekhov, S. M. (2003) Biochemistry (Moscow), 68, 260–268.CrossRefGoogle Scholar
  11. 11.
    Sidorova, N., Zavalishina, L., Kurchashova, S., Korsakova, N., Nazhimov, V., Frank, G., and Kuimov, A. (2006) Cell Tissue Res., 323, 137–145.PubMedCrossRefGoogle Scholar
  12. 12.
    De Rycker, M., Venkatesan, R. N., Wei, C., and Price, C. M. (2003) Biochem. J., 372, 87–96.PubMedCrossRefGoogle Scholar
  13. 13.
    De Rycker, M., and Price, C. M. (2004) Mol. Cell. Biol., 24, 9802–9812.PubMedCrossRefGoogle Scholar
  14. 14.
    Ham, R. G., and McKeehan, W. L. (1979) Meth. Enzymol., 58, 44–93.PubMedCrossRefGoogle Scholar
  15. 15.
    Bradford, M. M. (1976) Analyt. Biochem., 72, 248–254.PubMedCrossRefGoogle Scholar
  16. 16.
    Wilson, C. M. (1983) Meth. Enzymol., 91, 236–247.PubMedCrossRefGoogle Scholar
  17. 17.
    Laemmli, U. K. (1970) Nature, 227, 680–685.PubMedCrossRefGoogle Scholar
  18. 18.
    Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Analyt. Chem., 68, 850–858.CrossRefGoogle Scholar
  19. 19.
    Rippmann, J. F., Damm, K., and Schnapp, A. (2003) J. Mol. Biol., 325, 1107.CrossRefGoogle Scholar
  20. 20.
    Rippmann, J. F., Damm, K., and Schnapp, A. (2002) J. Mol. Biol., 323, 217–224.PubMedCrossRefGoogle Scholar
  21. 21.
    Simonin, F., Hofferer, L., Panzeter, P.L., Muller, S., de Murica, G., and Althaus, F. R. (1993) J. Biol. Chem., 268, 13454–13461.PubMedGoogle Scholar

Copyright information

© Pleiades Publishing, Ltd. 2008

Authors and Affiliations

  1. 1.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia
  2. 2.Faculty of Bioengineering and BioinformaticsLomonosov Moscow State UniversityMoscowRussia

Personalised recommendations