OGG1 glycosylase mediated recognition and binding of an 8-oxoguanine opposite to a cytosine

Stable Identifier
Reaction [binding]
Homo sapiens
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OGG1 is an N-glycosylase and DNA lyase that recognizes oxidative DNA damage in the form of 8-oxoguanine (8oxoG). 8oxoG forms at a high frequency in the DNA of aerobic organisms. As 8oxoG has a preference for mispairing with adenine, it is one of the underlying causes of G:C -> T:A transversions, the type of mutation frequently found in cancer (Aburatani et al. 1997, Rosenquist et al. 1997, Roldan-Arjona et al. 1997, Radicella et al. 1997, Bjoras et al. 1997, Bruner et al. 2000).
Literature References
PubMed ID Title Journal Year
9223306 Molecular cloning and functional expression of a human cDNA encoding the antimutator enzyme 8-hydroxyguanine-DNA glycosylase

Anselmino, C, Wei, YF, Wang, RP, Augustus, M, Lindahl, T, Carter, KC, Klungland, A, Roldán-Arjona, T

Proc. Natl. Acad. Sci. U.S.A. 1997
9321410 Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites

Luna, L, Hoff, E, Bjorâs, M, Johnsen, B, Haug, T, Rognes, T, Seeberg, E

EMBO J. 1997
9207108 Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase

Zharkov, DO, Grollman, AP, Rosenquist, TA

Proc. Natl. Acad. Sci. U.S.A. 1997
9223305 Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae

Desmaze, C, Radicella, JP, Boiteux, S, Fox, MS, Dherin, C

Proc. Natl. Acad. Sci. U.S.A. 1997
10706276 Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA

Bruner, SD, Verdine, GL, Norman, DP

Nature 2000
9187114 Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue

Yamamoto, K, Takao, M, Yasui, A, Asano, M, Ishida, T, Takashima, R, Kodama, T, Hippo, Y, Aburatani, H, Matsuba, C

Cancer Res. 1997
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