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Effect of DNA Glycosylases OGG1 and Neil1 on Oxidized G-Rich Motif in the KRAS Promoter.
Ferino, Annalisa; Xodo, Luigi E.
Afiliación
  • Ferino A; Laboratory of Biochemistry, Department of Medicine, P.le Kolbe 4, 33100 Udine, Italy.
  • Xodo LE; Laboratory of Biochemistry, Department of Medicine, P.le Kolbe 4, 33100 Udine, Italy.
Int J Mol Sci ; 22(3)2021 Jan 24.
Article en En | MEDLINE | ID: mdl-33498912
The promoter of the Kirsten ras (KRAS) proto-oncogene contains, upstream of the transcription start site, a quadruplex-forming motif called 32R with regulatory functions. As guanine under oxidative stress can be oxidized to 8-oxoguanine (8OG), we investigated the capacity of glycosylases 8-oxoguanine glycosylase (OGG1) and endonuclease VIII-like 1 (Neil1) to excise 8OG from 32R, either in duplex or G-quadruplex (G4) conformation. We found that OGG1 efficiently excised 8OG from oxidized 32R in duplex but not in G4 conformation. By contrast, glycosylase Neil1 showed more activity on the G4 than the duplex conformation. We also found that the excising activity of Neil1 on folded 32R depended on G4 topology. Our data suggest that Neil1, besides being involved in base excision repair pathway (BER), could play a role on KRAS transcription.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transcripción Genética / Daño del ADN / ADN Glicosilasas / Reparación del ADN / G-Cuádruplex Límite: Humans Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transcripción Genética / Daño del ADN / ADN Glicosilasas / Reparación del ADN / G-Cuádruplex Límite: Humans Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza