| First Author | Lu R | Year | 1997 |
| Journal | Curr Biol | Volume | 7 |
| Issue | 6 | Pages | 397-407 |
| PubMed ID | 9197244 | Mgi Jnum | J:41160 |
| Mgi Id | MGI:893239 | Doi | 10.1016/s0960-9822(06)00187-4 |
| Citation | Lu R, et al. (1997) A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer. Curr Biol 7(6):397-407 |
| abstractText | Background: Guanine residues in the genome are vulnerable to attack by free radicals and reactive oxygen species. A major lesion thus produced, 8-oxoguanine ((O)G), causes mutations by mis-pairing with adenine during replication. In bacteria and budding yeast, (O)G is removed from the genome through the action of base-excision DNA repair (BER) enzymes, which catalyze expulsion of the aberrant base and excision of its sugar moiety from the DNA backbone. Although (O)G is known to be produced in and cleansed from mammalian genomes, the enzymes responsible for (O)G repair in these cells have remained elusive. Results: Here, we report the cloning and biochemical characterization of mammalian BER enzymes that specifically target (O)G residues in DNA. These 8- oxoguanine DNA glycosylases, hOgg1 (human) and mOgg1 (murine), are homologous to each other and to yeast Ogg1. |
