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A human 5′-tyrosyl DNA phosphodiesterase that repairs topoisomerase-mediated DNA damage

Author

Listed:
  • Felipe Cortes Ledesma

    (Genome Damage and Stability Centre, University of Sussex, Science Park Road, Falmer, Brighton, Sussex BN1 9RQ, UK)

  • Sherif F. El Khamisy

    (Genome Damage and Stability Centre, University of Sussex, Science Park Road, Falmer, Brighton, Sussex BN1 9RQ, UK
    Faculty of Pharmacy, Ain Shams University, Abbassia 11566, Cairo, Egypt)

  • Maria C. Zuma

    (Genome Damage and Stability Centre, University of Sussex, Science Park Road, Falmer, Brighton, Sussex BN1 9RQ, UK)

  • Kay Osborn

    (Genome Damage and Stability Centre, University of Sussex, Science Park Road, Falmer, Brighton, Sussex BN1 9RQ, UK)

  • Keith W. Caldecott

    (Genome Damage and Stability Centre, University of Sussex, Science Park Road, Falmer, Brighton, Sussex BN1 9RQ, UK)

Abstract

DNA repair: the role of TTRAP The mechanism of topoisomerase action involves making a transient break in DNA. If the topoisomerase makes a break near another DNA lesion, the break can persist, with the topoisomerase attached to either the 3′ or 5′ end via a phosphotyrosyl bond. If these covalent adducts are not removed efficiently, cancer and neurodegenerative disease can result. In humans, a protein, TDP1, that removes adducts using a 3′-phosphotyrosyl bond has been identified. In this work, Ledesma et al. identify a phosphodiesterase, TTRAP, as the protein that removes adducts at the 5′-phosphotyrosyl bond.

Suggested Citation

  • Felipe Cortes Ledesma & Sherif F. El Khamisy & Maria C. Zuma & Kay Osborn & Keith W. Caldecott, 2009. "A human 5′-tyrosyl DNA phosphodiesterase that repairs topoisomerase-mediated DNA damage," Nature, Nature, vol. 461(7264), pages 674-678, October.
    • Handle: RePEc:nat:nature:v:461:y:2009:i:7264:d:10.1038_nature08444
    DOI: 10.1038/nature08444
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