期刊
FEBS JOURNAL
卷 272, 期 22, 页码 5753-5763出版社
WILEY
DOI: 10.1111/j.1742-4658.2005.04962.x
关键词
apurinic/apyrimidinic endonuclease 1; DNA polymerase beta; DNA repair; polynucleotide kinase; X-ray cross-complementing protein 1
Ionizing radiation, oxidative stress and endogenous DNA-damage processing can result in a variety of single-strand breaks with modified 5' and/or 3' ends. These are thought to be one of the most persistent forms of DNA damage and may threaten cell survival. This study addresses the mechanism involved in recognition and processing of DNA strand breaks containing modified 3' ends. Using a DNA-protein cross-linking assay, we followed the proteins involved in the repair of oligonucleotide duplexes containing strand breaks with a phosphate or phosphoglycolate group at the 3' end. We found that, in human whole cell extracts, end-damage-specific proteins (apurinic/apyrimidinic endonuclease 1 and polynucleotide kinase in the case of 3' ends containing phosphoglycolate and phosphate, respectively) which recognize and process 3'-end-modified DNA strand breaks are required for efficient recruitment of X-ray cross-complementing protein 1-DNA ligase III alpha heterodimer to the sites of DNA repair.
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