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Drosophila S3 ribosomal protein accelerates repair of 8‐oxoguanine performed by human and mouse cell extracts
Author(s) -
Cappelli Enrico,
D'Osualdo Andrea,
Bogliolo Massimo,
Kelley Mark R.,
Frosina Guido
Publication year - 2003
Publication title -
environmental and molecular mutagenesis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1
H-Index - 87
eISSN - 1098-2280
pISSN - 0893-6692
DOI - 10.1002/em.10166
Subject(s) - ap site , dna glycosylase , base excision repair , dna repair , biology , microbiology and biotechnology , ap endonuclease , dna , dna damage , drosophila melanogaster , dna (apurinic or apyrimidinic site) lyase , uracil dna glycosylase , biochemistry , gene
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. Environ. Mol. Mutagen. 42:50–58, 2003. © 2003 Wiley‐Liss, Inc.