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Updated: Aug 6, 2026

Assessment of DNase Activity by Ratiometric Fluorescence Resonance Energy Transfer
Published on: July 25, 2025
Deoxyribophosphate lyase activity of mammalian endonuclease VIII-like proteins
Inga R Grin1, Svetlana N Khodyreva, Georgy A Nevinsky
1SB RAS Institute of Chemical Biology and Fundamental Medicine, Novosibirsk 630090, Russia.
Abstract:
Base excision repair (BER) protects cells from nucleobase DNA damage. In eukaryotic BER, DNA glycosylases generate abasic sites, which are then converted to deoxyribo-5'-phosphate (dRP) and excised by a dRP lyase (dRPase) activity of DNA polymerase beta (Polbeta). Here, we demonstrate that NEIL1 and NEIL2, mammalian homologs of bacterial endonuclease VIII, excise dRP by beta-elimination with the efficiency similar to Polbeta. DNA duplexes imitating BER intermediates after insertion of a single nucleotide were better substrates. NEIL1 and NEIL2 supplied dRPase activity in BER reconstituted with dRPase-null Polbeta. Our results suggest a role for NEILs as backup dRPases in mammalian cells.
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