ArticleNucleic acids research2011
Thermodynamic and kinetic basis for recognition and repair of 8-oxoguanine in DNA by human 8-oxoguanine-DNA glycosylase.
Article in Nucleic acids research, 2011. 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, 18 citations in OpenAlex.
- How Enzymes, Proteins, and Antibodies Recognize Extended DNAs; General Regularities.International journal of molecular sciences · 2021Review
- How Human H1 Histone Recognizes DNA.Molecules (Basel, Switzerland) · 2020Article
- DNA Deformation-Coupled Recognition of 8-Oxoguanine: Conformational Kinetic Gating in Human DNA Glycosylase.Journal of the American Chemical Society · 2017Article
- Modulation of base excision repair of 8-oxoguanine by the nucleotide sequence.Nucleic acids research · 2013Article
- Influence of 8-oxoguanosine on the fine structure of DNA studied with biasing-potential replica exchange simulations.Biophysical journal · 2013Article
- DNA sequence context effects on the glycosylase activity of human 8-oxoguanine DNA glycosylase.The Journal of biological chemistry · 2012Article
- Contextual DNA features significant for the DNA damage by the 193-nm ultraviolet laser beam.Doklady. Biochemistry and biophysicsArticle
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We have used a stepwise increase in ligand complexity approach to estimate the relative contributions of the nucleotide units of DNA containing 7,8-dihydro-8-oxoguanine (oxoG) to its total affinity for human 8-oxoguanine DNA glycosylase (OGG1) and construct thermodynamic models of the enzyme interaction with cognate and non-cognate DNA. Non-specific OGG1 interactions with 10-13 nt pairs within its DNA-binding cleft provides approximately 5 orders of magnitude of its affinity for DNA (ΔG° approximately -6.7 kcal/mol). The relative contribution of the oxoG unit of DNA (ΔG° approximately -3.3 kcal/mol) together with other specific interactions (ΔG° approximately -0.7 kcal/mol) provide approximately 3 orders of magnitude of the affinity. Formation of the Michaelis complex of OGG1 with the cognate DNA cannot account for the major part of the enzyme specificity, which lies in the k(cat) term instead; the rate increases by 6-7 orders of magnitude for cognate DNA as compared with non-cognate one. The k(cat) values for substrates of different sequences correlate with the DNA twist, while the K(M) values correlate with ΔG° of the DNA fragments surrounding the lesion (position from -6 to +6). The functions for predicting the K(M) and k(cat) values for different sequences containing oxoG were found.
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