Journal
DNA REPAIR
Volume 6, Issue 6, Pages 695-711Publisher
ELSEVIER
DOI: 10.1016/j.dnarep.2007.01.009
Keywords
base excision repair; glycosylase; endonuclease; polymerase; ligase; XRCC1; PARP; protein complexes; post-translational modification
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Funding
- NCI NIH HHS [P20 CA103730, P20 CA103730-02] Funding Source: Medline
- NCRR NIH HHS [P20 RR016457-01, P20 RR016457] Funding Source: Medline
- NIA NIH HHS [1 R01 AG24364-01, R01 AG024364, R01 AG024364-03] Funding Source: Medline
- NIGMS NIH HHS [P20 GM103430] Funding Source: Medline
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Base excision repair (BER) proteins act upon a significantly broad spectrum of DNA lesions that result from endogenous and exogenous sources. Multiple sub-pathways of BER (shortpath or long-patch) and newly designated DNA repair pathways (e.g., SSBR.and NIR) that utilize BER proteins complicate any comprehensive understanding of BER and its role in genome maintenance, chemotherapeutic response, neuro- degeneration, cancer or aging. Herein, we propose a unified model of BER, comprised of three functional processes: Lesion Recognition/Strand Scission, Gap Tailoring and DNA Synthesis/Ligation, each represented by one or more multi-protein complexes and coordinated via the XRCC1/DNA Ligase III and PARPI scaffold proteins. BER therefore may be represented by a series of repair complexes that assemble at the site of the DNA lesion and mediates repair in a coordinated fashion involving protein-protein interactions that dictate subsequent steps or sub-pathway choice. Complex formation is influenced by post-translational protein modifications that arise from the cellular state or the DNA damage response, providing an increase in specificity and efficiency to the BER pathway In this review, we have summarized the reported BER protein-protein interactions and protein post- translational modifications and discuss the impact on DNA repair capacity and complex formation. (c) 2007 Elsevier B.V. All rights reserved.
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