ArticleProceedings of the National Academy of Sciences of the United States of America1996
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.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Review
- Concordance of hydrogen peroxide-induced 8-oxo-guanine patterns with two cancer mutation signatures of upper GI tract tumors.Science advances · 2022Article
- Functional Characterization of a Novel Oxidative Stress Protection Protein in the Pathogenic YeastFrontiers in genetics · 2020Article
- A comprehensive mechanistic model of iron metabolism in Saccharomyces cerevisiae.Metallomics : integrated biometal science · 2019Article
- The current state of eukaryotic DNA base damage and repair.Nucleic acids research · 2015Review
- Synthesis and characterization of oligonucleotides containing a nitrogen mustard formamidopyrimidine monoadduct of deoxyguanosine.Chemical research in toxicology · 2014Article
- Crosstalk between mitochondrial stress signals regulates yeast chronological lifespan.Mechanisms of ageing and development · 2014Article
- Review
- Functional genomics indicates yeast requires Golgi/ER transport, chromatin remodeling, and DNA repair for low dose DMSO tolerance.Frontiers in genetics · 2013Article
- DNA repair defects sensitize cells to anticodon nuclease yeast killer toxins.Molecular genetics and genomics : MGG · 2011Article
- Article
- Adaptation of organisms by resonance of RNA transcription with the cellular redox cycle.PloS one · 2011Article
- Characterization of the major formamidopyrimidine-DNA glycosylase homolog in Mycobacterium tuberculosis and its linkage to variable tandem repeats.FEMS immunology and medical microbiology · 2009Article
- Catalytically impaired hMYH and NEIL1 mutant proteins identified in patients with primary sclerosing cholangitis and cholangiocarcinoma.Carcinogenesis · 2009Article
- Reactive oxygen species regulate DNA copy number in isolated yeast mitochondria by triggering recombination-mediated replication.Nucleic acids research · 2009Article
- Characterization of the meningococcal DNA glycosylase Fpg involved in base excision repair.BMC microbiology · 2009Article
- Efficient removal of formamidopyrimidines by 8-oxoguanine glycosylases.Biochemistry · 2008Article
- Oxidative DNA damage repair in mammalian cells: a new perspective.DNA repair · 2007Review
- DNA recombination-initiation plays a role in the extremely biased inheritance of yeast [rho-] mitochondrial DNA that contains the replication origin ori5.Molecular and cellular biology · 2007Article
- Antimutator role of DNA glycosylase MutY in pathogenic Neisseria species.Journal of bacteriology · 2005Article
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6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One gene locus on chromosome I in Saccharomyces cerevisiae encodes a protein (YAB5_YEAST; accession no. P31378) with local sequence similarity to the DNA repair glycosylase endonuclease III from Escherichia coli. We have analyzed the function of this gene, now assigned NTG1 (endonuclease three-like glycosylase 1), by cloning, mutant analysis, and gene expression in E. coli. Targeted gene disruption of NTG1 produces a mutant that is sensitive to H2O2 and menadione, indicating that NTG1 is required for repair of oxidative DNA damage in vivo. Northern blot analysis and expression studies of a NTG1-lacZ gene fusion showed that NTG1 is induced by cell exposure to different DNA damaging agents, particularly menadione, and hence belongs to the DNA damage-inducible regulon in S. cerevisiae. When expressed in E. coli, the NTG1 gene product cleaves plasmid DNA damaged by osmium tetroxide, thus, indicating specificity for thymine glycols in DNA similarly as is the case for EndoIII. However, NTG1 also releases formamidopyrimidines from DNA with high efficiency and, hence, represents a glycosylase with a novel range of substrate recognition. Sequences similar to NTG1 from other eukaryotes, including Caenorhabditis elegans, Schizosaccharomyces pombe, and mammals, have recently been entered in the GenBank suggesting the universal presence of NTG1-like genes in higher organisms. S. cerevisiae NTG1 does not have the [4Fe-4S] cluster DNA binding domain characteristic of the other members of this family.
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