Dianov, Grigory L. and Sleeth, Kate M. and Dianova, Irina I. and Allinson, Sarah L. (2003) Repair of abasic sites in DNA. Mutation Research, 531 (1-2). pp. 157-163. ISSN 0027-5107Full text not available from this repository.
Repair of both normal and reduced AP sites is activated by AP endonuclease, which recognizes and cleaves a phosphodiester bond 5′ to the AP site. For a short period of time an incised AP site is occupied by poly(ADP-ribose) polymerase and then DNA polymerase β adds one nucleotide into the repair gap and simultaneously removes the 5′-sugar phosphate. Finally, the DNA ligase III/XRCC1 complex accomplishes repair by sealing disrupted DNA ends. However, long-patch BER pathway, which is involved in the removal of reduced abasic sites, requires further DNA synthesis resulting in strand displacement and the generation of a damage-containing flap that is later removed by the flap endonuclease. Strand-displacement DNA synthesis is accomplished by DNA polymerase δ/ and DNA ligase I restores DNA integrity. DNA synthesis by DNA polymerase δ/ is dependent on proliferating cell nuclear antigen, which also stimulates the DNA ligase I and flap endonuclease. These repair events are supported by multiple protein–protein interactions.
|Journal or Publication Title:||Mutation Research|
|Uncontrolled Keywords:||Abasic sites ; DNA ; Alkylating agents|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
|Deposited By:||Dr Sarah Allinson|
|Deposited On:||08 Jul 2008 13:05|
|Last Modified:||26 Jul 2012 14:44|
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