Quantitative characterization of protein–protein complexes involved in base excision DNA repair

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Quantitative characterization of protein–protein complexes involved in base excision DNA repair

Base Excision Repair (BER) efficiently corrects the most common types of DNA damage in mammalian cells. Step-by-step coordination of BER is facilitated by multiple interactions between enzymes and accessory proteins involved. Here we characterize quantitatively a number of complexes formed by DNA polymerase β (Polβ), apurinic/apyrimidinic endonuclease 1 (APE1), poly(ADP-ribose) polymerase 1 (PA...

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Transformed cells can develop drug resistance via repair mechanisms that counteract the DNA damage from chemotherapy or radiation therapy. Disruption of DNA repair pathways can cause mis-repair that is cytotoxic [1]. Specific DNA repair inhibitors might thus be combined with DNA-damaging agents for improved therapy. In addition, some cancer cells have a reduced repertoire of DNA damage response...

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DNA glycosylases in the base excision repair of DNA.

A wide range of cytotoxic and mutagenic DNA bases are removed by different DNA glycosylases, which initiate the base excision repair pathway. DNA glycosylases cleave the N-glycosylic bond between the target base and deoxyribose, thus releasing a free base and leaving an apurinic/apyrimidinic (AP) site. In addition, several DNA glycosylases are bifunctional, since they also display a lyase activ...

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Involvement of flap endonuclease 1 in base excision DNA repair.

Base excision repair can proceed in either one of two alternative pathways: a DNA polymerase beta-dependent pathway and a proliferating cell nuclear antigen (PCNA)-dependent pathway. Excision of an apurinic/apyrimidinic (AP) site by cutting the phosphate backbone on its 3' side following incision at its 5' side by AP endonuclease is a prerequisite to completion of these repair pathways. Using a...

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ژورنال

عنوان ژورنال: Nucleic Acids Research

سال: 2015

ISSN: 0305-1048,1362-4962

DOI: 10.1093/nar/gkv569