Disease relevance of Ogg1

• Cleavage of 8-OH-Gua.C duplex involves the formation of a reaction intermediate that is converted into a stable covalent adduct in the presence of sodium borohydre. dOgg1 complements the mutator phenotype of fpg mutY mutants of Escherichia coli [1].

High impact information on Ogg1

• Effects of ectopic expression of Drosophila DNA glycosylases dOgg1 and RpS3 in mitochondria [2].
• Arabidopsis thaliana Ogg1 protein excises 8-hydroxyguanine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine from oxidatively damaged DNA containing multiple lesions [3].
• The results unequivocally show that AtOgg1 possesses common substrates with other eukaryotic Ogg1 proteins albeit significant differences between their excision kinetics [3].
• This is in agreement with the substrate specificities of other eukaryotic Ogg1 proteins that had previously been studied under identical conditions [3].
• Repair of oxidative DNA damage in Drosophila melanogaster: identification and characterization of dOgg1, a second DNA glycosylase activity for 8-hydroxyguanine and formamidopyrimidines [1].

Biological context of Ogg1

• Here we describe a second Drosophila protein (dOgg1) with 8-OH-Gua and abasic (AP) site DNA repair activities [1].
• Another notable finding was that ectopic expression of either dOgg1 or RpS3 in mitochondria increased cell survival after exposure to the nitric oxide donor SNAP [2].
• Even in the absence of oxidative challenge, cells expressing RpS3 or dOgg1 in mitochondria exhibited increased apoptosis relative to controls, as determined by flow-cytometric analysis of Annexin V and DNA degradation measured by the Comet assay [2].

Associations of Ogg1 with chemical compounds

• Enzymatic assays using oligodeoxyribonucleotides containing a single lesion show that dOgg1 displays a marked preference for DNA duplexes containing 8-OH-Gua, 8-OH-Ade or an AP site placed opposite a cytosine [1].

Other interactions of Ogg1

• Drosophila DNA glycosylases, dOgg1 and RpS3, were ectopically expressed within the mitochondrial matrix in Drosophila S2 cells, causing a severalfold decrease in the levels of 8-oxodG in mitochondrial DNA [2].

Analytical, diagnostic and therapeutic context of Ogg1

• Whole-mount in situ hybridizations on tissues at different stages of Drosophila development reveal that the dOGG1 messenger is expressed uniformly at a low level in cells in which mitotic division occurs [1].
• The DNA glycosylase activity of purified dOgg1 was investigated using gamma-irradiated DNA and gas chromatography/isotope dilution mass spectrometry (GC/IDMS) [1].

References