Advertisement

The Escherichia coli UV Endonuclease (Correndonuclease II)

  • Andrew Braun
  • Peggy Hopper
  • Lawrence Grossman
Part of the Basic Life Sciences book series

Abstract

An endonuclease from Escherichia coli which acts specifically upon UV-irradiated DNA (correndonuclease II) and is absent from the uvrA and uvrB mutants has been isolated and partially characterized. The enzyme is present in normal amounts in the uvrC mutant. It elutes from phosphocellulose at about 0.25 M potassium phosphate (pH 7.5) and passes through dialysis tubing. The enzyme binds tightly to UV-irradiated DNA but does not bind to unirradiated DNA. The enzyme incises irradiated DNA to the 5′ side of a pyrimidine dimer and leaves a 5′-phosphoryl terminus which can be resealed with polynucleotide ligase. The K m of the enzyme is about 1.5 X 10-8 M dimers. Endonucleolytic activity of the enzyme is inhibited by caffeine with a K I of about 10mM.

Keywords

Crude Extract Dialysis Tubing Micrococcus Luteus Graduate Department Filter Binding Assay 
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. Becker, A., Lyn, G., Gefter, M. and Hurwitz, J. (1967). Proc. Nat. Acad. Sci. U.S.A. 58, 1996–2003.CrossRefGoogle Scholar
  2. Braun, A. and Grossman, L. (1974). Proc. Nat. Acad. Sci. U.S.A. 71, 1838–1842.CrossRefGoogle Scholar
  3. Center, M. S. and Richardson, C. C. (1970). J. Biol. Chem. 245, 6285–6291.Google Scholar
  4. Friedberg, E. C. and King, J. J. (1969). Biochem. Biophys. Res. Commun. 37, 646–651.Google Scholar
  5. Gefter, M. L., Becker, A. and Hurwitz, J. (1967). Proc. Nat. Acad. Sci. U.S.A. 58, 240–247.CrossRefGoogle Scholar
  6. Hamilton, L., Mahler, I. and Grossman, L. (1974). Biochemistry 13, 1886–1896.PubMedCrossRefGoogle Scholar
  7. Kaplan, J. C., Kushner, S. R. and Grossman, L. (1969). Proc. Nat. Acad. Sci. U.S.A. 63, 144–151.CrossRefGoogle Scholar
  8. Riggs, A. D., Suzuki, H. and Bourgeois, S. (1970). J. Mol. Biol. 48, 67–83.PubMedCrossRefGoogle Scholar
  9. Shimada, K. and Takagi, Y. (1967). Biochim. Biophys. Acta 145, 763–770.PubMedGoogle Scholar
  10. Sideropoulous, A. S. and Shankel, D. M. (1968). J. Bacteriol. 96, 198–204.Google Scholar
  11. Takagi, Y., Sekiguchi, M., Okubo, H., Nakayama, H., Shimada, K., Yasuda, S., Michimoto, T. and Yoshihara, H. (1969). Cold Spring Harbor Symp. Quant. Biol. 33, 219–227.CrossRefGoogle Scholar
  12. Yasuda, S. and Sekiguchi, M. (1970). Proc. Nat. Acad. Sci. U.S.A. 67, 1839–1845.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1975

Authors and Affiliations

  • Andrew Braun
    • 1
  • Peggy Hopper
    • 1
  • Lawrence Grossman
    • 1
  1. 1.Graduate Department of BiochemistryBrandeis UniversityWalthamUSA

Personalised recommendations