ArticleThe Journal of biological chemistry2013
DNA damage processing by human 8-oxoguanine-DNA glycosylase mutants with the occluded active site.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Structural and Dynamic Features of the Recognition of 8-oxoguanosine Paired with an 8-oxoG-clamp by Human 8-oxoguanine-DNA Glycosylase.Current issues in molecular biology · 2024Article
- The potential for OGG1 inhibition to be a therapeutic strategy for pulmonary diseases.Expert opinion on therapeutic targets · 2024Review
- Molecular beacons with oxidized bases report on substrate specificity of DNA oxoguanine glycosylases.Chemical science · 2022Article
- Validation of the in vitro comet assay for DNA cross-links and altered bases detection.Archives of toxicology · 2021Article
- Base excision repair of oxidative DNA damage: from mechanism to disease.Frontiers in bioscience (Landmark edition) · 2017Review
- DNA Deformation-Coupled Recognition of 8-Oxoguanine: Conformational Kinetic Gating in Human DNA Glycosylase.Journal of the American Chemical Society · 2017Article
- An active alternative splicing isoform of human mitochondrial 8-oxoguanine DNA glycosylase (OGG1).Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2015Review
- Structural Features of the Interaction between Human 8-Oxoguanine DNA Glycosylase hOGG1 and DNA.Acta naturae · 2014Article
- Molecular dynamics approach to identification of new OGG1 cancer-associated somatic variants with impaired activity.The Journal of biological chemistryArticle
- The role of cysteines in the structure and function of OGG1.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
8-Oxoguanine-DNA glycosylase (OGG1) removes premutagenic lesion 8-oxoguanine (8-oxo-G) from DNA and then nicks the nascent abasic (apurinic/apyrimidinic) site by β-elimination. Although the structure of OGG1 bound to damaged DNA is known, the dynamic aspects of 8-oxo-G recognition are not well understood. To comprehend the mechanisms of substrate recognition and processing, we have constructed OGG1 mutants with the active site occluded by replacement of Cys-253, which forms a wall of the base-binding pocket, with bulky leucine or isoleucine. The conformational dynamics of OGG1 mutants were characterized by single-turnover kinetics and stopped-flow kinetics with fluorescent detection. Additionally, the conformational mobility of wild type and the mutant OGG1 substrate complex was assessed using molecular dynamics simulations. Although pocket occlusion distorted the active site and greatly decreased the catalytic activity of OGG1, it did not fully prevent processing of 8-oxo-G and apurinic/apyrimidinic sites. Both mutants were notably stimulated in the presence of free 8-bromoguanine, indicating that this base can bind to the distorted OGG1 and facilitate β-elimination. The results agree with the concept of enzyme plasticity, suggesting that the active site of OGG1 is flexible enough to compensate partially for distortions caused by mutation.
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