Poly(ADP-ribose) polymerase 1 (PARP-1) binds to 8-oxoguanine-DNA glycosylase (OGG1).

Human 8-oxoguanine-DNA glycosylase (OGG1) plays a major role in the base excision repair pathway by removing 8-oxoguanine base lesions generated by reactive oxygen species. Here we report a novel interaction between OGG1 and Poly(ADP-ribose) polymerase 1 a DNA-damage sensor protein involved in DNA repair and many other cellular processes. We found that OGG1 binds directly to through the N-terminal region of OGG1, and this interaction is enhanced by oxidative stress. Furthermore, OGG1 binds to Pduanyu37-1 through its BRCA1 C-terminal (BRCT) domain. OGG1 stimulated the poly(ADP-ribosyl)ation activity of whereas decreased poly(ADP-ribose) levels were observed in OGG1(-/-) cells compared with wild-type cells in response to DNA damage. Importantly, activated Pduanyu37-1 inhibits OGG1. Although the OGG1 polymorphic variant proteins R229Q and S326C bind to Pduanyu37-1, these proteins were defective in activating Furthermore, OGG1(-/-) cells were more sensitive to inhibitors alone or in combination with a DNA-damaging agent. These findings indicate that OGG1 binding to Pduanyu37-1 plays a functional role in the repair of oxidative DNA damage.

KEYWORDS: {{ getKeywords(articleDetailText.words) }}