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Deoxyribophosphate lyase activity of mammalian endonuclease VIII‐like proteins
Author(s) -
Grin Inga R.,
Khodyreva Svetla.,
Nevinsky Georgy A.,
Zharkov Dmitry O.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.08.011
Subject(s) - base excision repair , ap site , dna glycosylase , ap endonuclease , dna (apurinic or apyrimidinic site) lyase , dna polymerase , endonuclease , microbiology and biotechnology , dna , biology , dna repair , lyase , biochemistry , chemistry , enzyme
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 β (Polβ). Here, we demonstrate that NEIL1 and NEIL2, mammalian homologs of bacterial endonuclease VIII, excise dRP by β‐elimination with the efficiency similar to Polβ. 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 Polβ. Our results suggest a role for NEILs as backup dRPases in mammalian cells.