| First Author | Grin IR | Year | 2006 |
| Journal | FEBS Lett | Volume | 580 |
| Issue | 20 | Pages | 4916-22 |
| PubMed ID | 16920106 | Mgi Jnum | J:112297 |
| Mgi Id | MGI:3656086 | Doi | 10.1016/j.febslet.2006.08.011 |
| Citation | Grin IR, et al. (2006) Deoxyribophosphate lyase activity of mammalian endonuclease VIII-like proteins. FEBS Lett 580(20):4916-22 |
| abstractText | 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. |
