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 0027-5107
Full text not available from this repository.Abstract
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.
| Item Type: | Article |
|---|---|
| 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 |
| ID Code: | 10161 |
| Deposited By: | Dr Sarah Allinson |
| Deposited On: | 08 Jul 2008 13:05 |
| Refereed?: | Yes |
| Published?: | Published |
| Last Modified: | 26 Jul 2012 14:44 |
| Identification Number: | |
| URI: | http://eprints.lancs.ac.uk/id/eprint/10161 |
Actions (login required)
| View Item |
