Deoxyribophosphate Lyase Activity of Mammalian Endonuclease Viii-like Proteins.
From: SB RAS Institute of Chemical Biology and Fundamental Medicine, Novosibirsk 630090, Russia.
FEBS letters
- Publish Date: Sep 2006
- ISSN: 0014-5793
- Volume: 580
- Issue: 20
- Pages: 4916-22
- Medium: Print
- Language: English
- Citation (JAMA): Grin Inga R, Khodyreva Svetlana N, Nevinsky Georgy A, et al. Deoxyribophosphate Lyase Activity of Mammalian Endonuclease Viii-like Proteins.. FEBS Lett. Sep 2006;580:4916-22
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.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, DNA Glycosylases, DNA Polymerase beta, DNA Repair, DNA-Formamidopyrimidine Glycosylase, Deoxyribonuclease (Pyrimidine Dimer), Escherichia coli Proteins, Humans, Molecular Sequence Data, Molecular Structure, Nucleic Acid Conformation, Phosphorus-Oxygen Lyases, Sequence Alignment
Check for Full Text / PubMed Unique Identifier (PMID): 16920106
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