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. 2020 Aug 14;295(41):14222–14235. doi: 10.1074/jbc.RA120.014228

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© 2020 Ha et al.

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Figure 7. — A working model for the regulation of APE1 endonuclease activity on ssDNA by NEIL3-ZF1&2. Base damage is recognized and removed by NEIL3. Left panel (full-length NEIL3 with Zf-GRF repeat): base damage in ssDNA is converted into the AP site via NEIL3's DNA glycosylase activity. AP site may be shielded from APE1 endonuclease activity (shielding effect). Alternatively, NEIL3 Zf-GRF motifs may interact with APE1 and inhibit its AP endonuclease activity (inhibition effect). Middle panel (NEIL3 fragment without Zf-GRF repeat): base damage in ssDNA is converted into the AP site via DNA glycosylase activity of a fragment of NEIL3 that lacks the Zf-GRF repeat. APE1 recognizes the AP site and cleaves it into SSB, leading to genome instability. Right panel (overexpression of NEIL3 Zf-GRF repeat): AP site is generated by endogenous NEIL3 or other DNA glycosylases. APE1-mediated cleavage of the AP site is impaired by excess addition of the NEIL3 Zf-GRF repeat. These different possible mechanisms of action may explain the significance of the NEIL3 Zf-GRF repeat in the maintenance of ssDNA stability from APE1-mediated ssDNA breakage and DNA shortening. See text for details.