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- W2561503025 abstract "Significance Zf-GRF domains are found in more than 100 eukaryotic architectures, including key proteins modulating DNA damage response and transcription. We establish the apurinic/apyrimidinic endonuclease 2 (APE2) Zf-GRF domain as a prototypical member of the Zf-GRF class of nucleic acid-binding modules, and through structural analysis reveal that the APE2 protein is composed of a compacted three-stranded β-sheet and a CHCC Zn 2+ -binding site, harboring structure-specific ssDNA-binding activity. Notably, the ssDNA-binding region of APE2 Zf-GRF is required for the 3′-5′ end resection of oxidative DNA damage and activation of the ATR-Chk1 DNA damage response pathway following oxidative stress. This distinct regulatory mechanism of APE2 exonuclease activity by ssDNA binding via Zf-GRF may extend to other Zf-GRF–containing proteins." @default.
- W2561503025 created "2017-01-06" @default.
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- W2561503025 date "2016-12-27" @default.
- W2561503025 modified "2023-10-14" @default.
- W2561503025 title "APE2 Zf-GRF facilitates 3′-5′ resection of DNA damage following oxidative stress" @default.
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- W2561503025 doi "https://doi.org/10.1073/pnas.1610011114" @default.
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