Drosophila S3 ribosomal protein accelerates repair of 8-oxoguanine performed by human and mouse cell extracts

Enrico Cappelli, Andrea D'Osualdo, Massimo Bogliolo, Mark R. Kelley, Guido Frosina

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

The S3 ribosomal protein of Drosophila melanogaster possesses various DNA repair activities, including the capacity to incise at apurinic/apyrimidinic (AP) sites and 8-oxo-7,8-dihydroguanine (8-oxoG) residues. We have recently hypothesized that this multifunctional protein may improve the efficiency of DNA base excision repair (BER) in mammalian cells. We have investigated the effect of pure GST-tagged Drosophila S3 on BER of different endogenous lesions performed by human and mouse cell extracts. Drosophila S3 significantly accelerated the BER of 8-oxoG (initiated by the bifunctional glycosylase OGG1). The stimulating effect was linked to the capacity of S3 to remove the 8-oxoG lesion and cleave the resulting AP site, rather than acceleration of downstream steps of the BER pathway (e.g., removal of 3′ blocking fragments). No stimulating effect was observed on the BER of uracil, natural AP sites, and β-lyase-cleaved AP sites. Heterologous expression of Drosophila S3 may be used to enhance 8-oxoG repair in human cells.

Original languageEnglish (US)
Pages (from-to)50-58
Number of pages9
JournalEnvironmental and Molecular Mutagenesis
Volume42
Issue number1
DOIs
StatePublished - Aug 18 2003

Keywords

  • 8-oxoguonine
  • Apurinic sites
  • DNA bose excision repair
  • Drosophilo S3 protein

ASJC Scopus subject areas

  • Environmental Science(all)
  • Environmental Chemistry
  • Genetics
  • Genetics(clinical)
  • Toxicology
  • Health, Toxicology and Mutagenesis

Fingerprint Dive into the research topics of 'Drosophila S3 ribosomal protein accelerates repair of 8-oxoguanine performed by human and mouse cell extracts'. Together they form a unique fingerprint.

  • Cite this