ArticleThe Journal of biological chemistry2012
Enforced presentation of an extrahelical guanine to the lesion recognition pocket of human 8-oxoguanine glycosylase, hOGG1.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 52 citations in OpenAlex.
- A unified catalytic mechanism in bifunctional DNA glycosylases with an evolutionarily conserved aspartate-lysine dyad.Nature communications · 2026Article
- Mechanisms of search for specific sites in DNA by DNA-binding proteins.Biochemistry and biophysics reports · 2026Review
- Insights into the A-C Mismatch Conformational Ensemble in Duplex DNA and its Role in Genetic Processes through a Structure-based Review.Journal of molecular biology · 2024Review
- Molecular Mechanisms Associated with Clustered Lesion-Induced Impairment of 8-oxoG Recognition by the Human Glycosylase OGG1.Molecules (Basel, Switzerland) · 2021Article
- Non-flipping DNA glycosylase AlkD scans DNA without formation of a stable interrogation complex.Communications biology · 2021Article
- 4-Hydroxy-2-nonenal attenuates 8-oxoguanine DNA glycosylase 1 activity.Journal of cellular biochemistry · 2020Article
- Lost in the Crowd: How Does Human 8-Oxoguanine DNA Glycosylase 1 (OGG1) Find 8-Oxoguanine in the Genome?International journal of molecular sciences · 2020Review
- The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase.Nature communications · 2020Article
- Construction of a self-directed replication system for label-free and real-time sensing of repair glycosylases with zero background.Chemical science · 2020Article
- Targeting Base Excision Repair Glycosylases with DNA Containing Transition State Mimics Prepared via Click Chemistry.ACS chemical biology · 2019Article
- Facilitated Diffusion Mechanisms in DNA Base Excision Repair and Transcriptional Activation.Chemical reviews · 2018Review
- Article
- The mechanism of the glycosylase reaction with hOGG1 base-excision repair enzyme: concerted effect of Lys249 and Asp268 during excision of 8-oxoguanine.Nucleic acids research · 2017Article
- DNA Deformation-Coupled Recognition of 8-Oxoguanine: Conformational Kinetic Gating in Human DNA Glycosylase.Journal of the American Chemical Society · 2017Article
- A dynamic checkpoint in oxidative lesion discrimination by formamidopyrimidine-DNA glycosylase.Nucleic acids research · 2016Article
- CUX2 protein functions as an accessory factor in the repair of oxidative DNA damage.The Journal of biological chemistry · 2015Article
- Conformational Dynamics of DNA Repair by Escherichia coli Endonuclease III.The Journal of biological chemistry · 2015Article
- The function of CUX1 in oxidative DNA damage repair is needed to prevent premature senescence of mouse embryo fibroblasts.Oncotarget · 2015Article
- Structural Features of the Interaction between Human 8-Oxoguanine DNA Glycosylase hOGG1 and DNA.Acta naturae · 2014Article
- Structures of Cas9 endonucleases reveal RNA-mediated conformational activation.Science (New York, N.Y.) · 2014Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
Abstract
A poorly understood aspect of DNA repair proteins is their ability to identify exceedingly rare sites of damage embedded in a large excess of nearly identical undamaged DNA, while catalyzing repair only at the damaged sites. Progress toward understanding this problem has been made by comparing the structures and biochemical behavior of these enzymes when they are presented with either a target lesion or a corresponding undamaged nucleobase. Trapping and analyzing such DNA-protein complexes is particularly difficult in the case of base extrusion DNA repair proteins because of the complexity of the repair reaction, which involves extrusion of the target base from DNA followed by its insertion into the active site where glycosidic bond cleavage is catalyzed. Here we report the structure of a human 8-oxoguanine (oxoG) DNA glycosylase, hOGG1, in which a normal guanine from DNA has been forcibly inserted into the enzyme active site. Although the interactions of the nucleobase with the active site are only subtly different for G versus oxoG, hOGG1 fails to catalyze excision of the normal nucleobase. This study demonstrates that even if hOGG1 mistakenly inserts a normal base into its active site, the enzyme can still reject it on the basis of catalytic incompatibility.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.