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PMID: 14967139 Published · ppublish English Journal Article Review

Repair of DNA covalently linked to protein.

Molecular cell ·Vol. 13 ·No. 3 ·2004-02-13 ·Pages 307-16

Connelly JC, Leach DR

Abstract

A potentially lethal form of DNA/RNA modification, a cleavage complex, occurs when a nucleic acid-processing enzyme that acts via a transient covalent intermediate becomes trapped at its site of action. A number of overlapping pathways act to repair these lesions and many of the enzymes involved are those that catalyze recombinational-repair processes. A protein, Tdp1, has been identified that reverses cleavage-complex formation by specifically hydrolyzing a tyrosyl-DNA phosphodiester bond. The study of these pathways is both interesting and pertinent as they modulate the effectiveness of many antitumor/antibacterial drugs that act by stabilizing cleavage-complexes in vivo.

MeSH Terms
Animals Binding Sites/genetics DNA Damage/genetics DNA Repair/genetics DNA-Binding Proteins/genetics Humans Macromolecular Substances Molecular Conformation Nucleic Acids/genetics,metabolism Phosphoric Diester Hydrolases/genetics
Chemicals
DNA-Binding Proteins Macromolecular Substances Nucleic Acids Phosphoric Diester Hydrolases TDP1 protein, human tyrosyl-DNA phosphodiesterase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Connelly John C
Institute of Cell and Molecular Biology, University of Edinburgh, Kings Buildings, Edinburgh EH9 3JR, United Kingdom. [email protected]
Leach David R F
Article Info
Journal
Molecular cell
Abbr.
Mol Cell
ISSN
1097-2765
Published
2004-02-13
Pages
307-16
Language
English
Region
United States
NLM ID
9802571
Subset
IM
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