ArticleThe Journal of biological chemistry2017
Structural Basis for the Lesion-scanning Mechanism of the MutY DNA Glycosylase.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- DNA Damage Recognition by Bacterial and Human Adenine-DNA Glycosylases: Insights from Non-Canonical Substrates.Biomolecules · 2026Article
- 8oxoG:A Is Structurally Accommodated in the Nucleosome Core Particle, Yet Inaccessible to MUTYH-Initiated DNA Repair.Biomolecules · 2026Article
- Linker-mediated conformational coupling drives lesion recognition in MutY glycosylase.Nucleic acids research · 2026Article
- Direct Measurement of 8OG Syn-Anti Flips in Mutagenic 8OG·A and Long-Range Damage-Dependent Hoogsteen Breathing Dynamics UsingThe journal of physical chemistry. B · 2024Article
- Direct Measurement of 8OGbioRxiv : the preprint server for biology · 2024Article
- Mechanisms underlying the low-temperature adaptation of 17β-estradiol-degrading bacterial strainFrontiers in microbiology · 2024Article
- Noncatalytic Domains in DNA Glycosylases.International journal of molecular sciences · 2022Review
- Computational investigations on target-site searching and recognition mechanisms by thymine DNA glycosylase during DNA repair process.Acta biochimica et biophysica Sinica · 2022Review
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation.Progress in biophysics and molecular biology · 2021Article
- Structure of the mammalian adenine DNA glycosylase MUTYH: insights into the base excision repair pathway and cancer.Nucleic acids research · 2021Article
- The trajectory of intrahelical lesion recognition and extrusion by the human 8-oxoguanine DNA glycosylase.Nature communications · 2020Article
- Detection of OG:A Lesion Mispairs by MutY Relies on a Single His Residue and the 2-Amino Group of 8-Oxoguanine.Journal of the American Chemical Society · 2020Article
- Structural Basis for Finding OG Lesions and Avoiding Undamaged G by the DNA Glycosylase MutY.ACS chemical biology · 2020Article
- Single molecule glycosylase studies with engineered 8-oxoguanine DNA damage sites show functional defects of a MUTYH polyposis variant.Nucleic acids research · 2019Article
- Base-flipping dynamics from an intrahelical to an extrahelical state exerted by thymine DNA glycosylase during DNA repair process.Nucleic acids research · 2018Article
- High Free-Energy Barrier of 1D Diffusion Along DNA by Architectural DNA-Binding Proteins.Journal of molecular biology · 2018Article
- Cellular Assays for Studying the Fe-S Cluster Containing Base Excision Repair Glycosylase MUTYH and Homologs.Methods in enzymology · 2018Article
- Fe-S Clusters and MutY Base Excision Repair Glycosylases: Purification, Kinetics, and DNA Affinity Measurements.Methods in enzymology · 2018Article
- Aberrant repair initiated by the adenine-DNA glycosylase does not play a role in UV-induced mutagenesis inPeerJ · 2018Article
- Structure-Activity Relationships Reveal Key Features of 8-Oxoguanine: A Mismatch Detection by the MutY Glycosylase.ACS chemical biology · 2017Article
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3 authors.
Funding
Abstract
The highly mutagenic A:8-oxoguanine (oxoG) base pair is generated mainly by misreplication of the C:oxoG base pair, the oxidation product of the C:G base pair. The A:oxoG base pair is particularly insidious because neither base in it carries faithful information to direct the repair of the other. The bacterial MutY (MUTYH in humans) adenine DNA glycosylase is able to initiate the repair of A:oxoG by selectively cleaving the A base from the A:oxoG base pair. The difference between faithful repair and wreaking mutagenic havoc on the genome lies in the accurate discrimination between two structurally similar base pairs: A:oxoG and A:T. Here we present two crystal structures of the MutY N-terminal domain in complex with either undamaged DNA or DNA containing an intrahelical lesion. These structures have captured for the first time a DNA glycosylase scanning the genome for a damaged base in the very first stage of lesion recognition and the base extrusion pathway. The mode of interaction observed here has suggested a common lesion-scanning mechanism across the entire helix-hairpin-helix superfamily to which MutY belongs. In addition, small angle X-ray scattering studies together with accompanying biochemical assays have suggested a possible role played by the C-terminal oxoG-recognition domain of MutY in lesion scanning.
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