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

Felipe Cortes Ledesma (), Sherif F. El Khamisy, Maria C. Zuma, Kay Osborn and Keith W. Caldecott ()
Additional contact information
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
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

Nature, 2009, vol. 461, issue 7264, 674-678

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.

Date: 2009
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature08444 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:461:y:2009:i:7264:d:10.1038_nature08444

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature08444

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().