ArticleNucleic acids research1994
Formamidopyrimidine DNA glycosylase in the yeast Saccharomyces cerevisiae.
Article in Nucleic acids research, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 32 citations in OpenAlex.
- Artifacts associated with the measurement of oxidized DNA bases.Environmental health perspectives · 1997Review
- The Ogg1 protein of Saccharomyces cerevisiae: a 7,8-dihydro-8-oxoguanine DNA glycosylase/AP lyase whose lysine 241 is a critical residue for catalytic activity.Nucleic acids research · 1997Article
- Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- DNA glycosylases in the base excision repair of DNA.The Biochemical journal · 1997Review
- Base excision of oxidative purine and pyrimidine DNA damage in Saccharomyces cerevisiae by a DNA glycosylase with sequence similarity to endonuclease III from Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A DNA glycosylase that excises, 2,6-diamino-4-hydroxy-5N-methylformamidopyrimidine (Fapy) from double stranded DNA has been purified 28,570-fold from the yeast Saccharomyces cerevisiae. Gel filtration chromatography shows that yeast Fapy DNA glycosylase has a molecular weight of about 40 kDa. The Fapy DNA glycosylase is active in the presence of EDTA, but is completely inhibited by 0.2 M KCl. Yeast Fapy DNA glycosylase does not excise N7-methylguanine, N3-methyladenine or uracil. A repair enzyme for 7,8-dihydro-8-oxoguanine (8-OxoG) co-purifies with the Fapy DNA glycosylase. This repair activity causes strand cleavage at the site of 8-OxoG in DNA duplexes. The highest rate of incision of the 8-OxoG-containing strand was observed for duplexes where 8-OxoG was opposite guanine. The mode of incision at 8-OxoG was not established yet. The results however suggest that the Fapy- and 8-OxoG-repair activities are associated with a single protein.
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