Advertisement

Poly (ADP-Ribosylation) and DNA Topoisomerase I in Different Cell Lines

  • Ari M. Ferro
  • Larry H. Thompson
  • Baldomero M. Olivera
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 179)

Abstract

With his discovery that the Escherichia coli chromosome was circular, John Cairns first pointed out the need for a swivel in DNA replication (1). In eukaryotes, type I DNA topoisomerase has the enzymatic properties necessary to serve as such a swivel. DNA replication would introduce positive supertwists ahead of the replication fork; DNA topoisomerase I has the capacity to unwind such positively supertwisted DNA (2, 3). For this reason, a role for topoisomerase I in replication has been suggested by many workers (2, 3). Recent biological and phenomenological data have also led to the suggestion that type I DNA topoisomerase may be involved in catalyzing DNA strand exchange under certain conditions (4). The mechanisms by which the activity of such a potentially important enzyme may be modulated are of obvious interest.

Keywords

Yeast Extract Chinese Hamster Ovary Cell Replication Fork Sister Chromatid Exchange Strand Exchange 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Cairns, J. (1963) J. Mol. Biol. 6, 208.PubMedCrossRefGoogle Scholar
  2. 2.
    Wang, J.C. (1981) in; The Enzymes, pp. 331, Boyer, P.D., ed., Academic Press, New York.Google Scholar
  3. 3.
    Geliert, M. (1981) Annu. Rev. Biochem. 50, 879.CrossRefGoogle Scholar
  4. 4.
    Halligan, B.D., Davis, J.L., Edwards, K.A. and Liu, L.F. (1982) J. Biol. Chem. 257, 3995.PubMedGoogle Scholar
  5. 5.
    Ferro, A.M. and Olivera, B.M. (1984) J. Biol. Chem. 259, 547.PubMedGoogle Scholar
  6. 6.
    Hayaishi, O. and Ueda, K. (eds.) (1982) ADP-Ribosylation Reactions, Biology and Medicine, Academic Press, New York.Google Scholar
  7. 7.
    Mandel, P., Okazaki, H. and Niedergang, C. (1982) Prog. Nucleic Acid Res. Mol. Biol. 27, 1.PubMedCrossRefGoogle Scholar
  8. 8.
    Yamada, M., Miwa, M. and Sugimura, T. (1971) Arch, Biochem. Biophys. 146, 579.CrossRefGoogle Scholar
  9. 9.
    Yoshihara, K. (1972) Biochem. Biophys. Res. Commun. 47, 119.PubMedCrossRefGoogle Scholar
  10. 10.
    Benjamin, R.C. and Gill, D.M. (1980) J. Biol. Chem. 255, 10502.PubMedGoogle Scholar
  11. 11.
    Ferro, A.M., Higgins, N.P. and Olivera, B.M. (1983) J. Biol. Chem. 258, 6000.PubMedGoogle Scholar
  12. 12.
    Chang, L.M.S. (1971) Biochem. Biophys. Res. Commun. 44, 124.PubMedCrossRefGoogle Scholar
  13. 13.
    Bollum, F.J. (1978) Adv. Enzymol, Meister, A., ed., 47, 347.Google Scholar
  14. 14.
    Liu, L.F. and Miller, K.G. (1981) Proc. Natl. Acad. Sci. USA 78, 3487.PubMedCrossRefGoogle Scholar
  15. 15.
    Jacobson, M.K. and Bernofsky, C. (1974) Biochim. Biophys. Acta 350, 277.PubMedCrossRefGoogle Scholar
  16. 16.
    Cabib, E. (1971) Methods Enzymol. 22, 120.CrossRefGoogle Scholar
  17. 17.
    Lange, R.A. and Jacobson, M.K. (1977) Biochem. Biophys. Res. Commun. 76, 424.CrossRefGoogle Scholar
  18. 18.
    Randerath, K. and Randerath, E. (1967) Methods Enzymol. 12A, 323.CrossRefGoogle Scholar
  19. 19.
    Thompson, L.H., Rubin, J.S., Cleaver, J.E., Whitmore, G.F. and Brookman, K. (1980) Somatic Cell Gen. 6, 391.CrossRefGoogle Scholar
  20. 20.
    Miwa, M. and Sugimura, T. (1982) in: ADP-Ribosylation Reactions Biology and Medicine, pp. 263, (Hayaishi, O. and Ueda, K., eds., Academic Press, New York.Google Scholar
  21. 21.
    Yoshihara, K., Tanigawa, Y., Burzio, L. and Koide, S.S. (1975) Proc. Natl. Acad. Sci. USA 72, 289.PubMedCrossRefGoogle Scholar
  22. 22.
    Utakoji, T., Hosoda, K., Umezawa, K., Sawamura, M., Matsushima, T., Miwa, M. and Sugimura, T. (1979) Biochem. Biophys. Res. Commun. 90, 1147.PubMedCrossRefGoogle Scholar
  23. 23.
    Oikawa, A., Tonda, H., Kanai, M., Miwa, M. and Sugimura, T. (1980) Biochem. Biophys. Res. Commun. 97, 1311.PubMedCrossRefGoogle Scholar
  24. 24.
    Hori, T. (1981) Biochem. Biophys. Res. Commun. 102, 38.PubMedCrossRefGoogle Scholar
  25. 25.
    Watarajan, A.T., Csukas, I. and van Zeeland, A.A. (1981) Mutat. Res. 84, 125.CrossRefGoogle Scholar
  26. 26.
    Schwartz, J.L., Morgan, W.F., Kapp, L.N. and Wolff, S. (1983) Exp. Cell Res. 143, 377.PubMedCrossRefGoogle Scholar
  27. 27.
    Burzio, K. and Koide, S.S. (1970) FEBS Lett. 26, 181.Google Scholar
  28. 28.
    Claycomb, W.B. (1976) Biochem. J. 154, 387.PubMedGoogle Scholar
  29. 29.
    Berger, N.A., Petzold, S.J. and Berger, S.J. (1979) Biochim. Biophys. Acta 564. 90.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Ari M. Ferro
    • 1
  • Larry H. Thompson
    • 2
  • Baldomero M. Olivera
    • 1
  1. 1.Department of BiologyUniversity of UtahSalt Lake CityUSA
  2. 2.Lawrence Livermore National LaboratoryLivermoreUSA

Personalised recommendations