A coordinated haptic mechanism ensures efficient DNA sampling by the 8-oxoguanine glycosylase OGG1

7,8-Dihydro-8-oxoguanine (8-oxoG), a frequent mutagenic base modification occurring upon oxidative stress, is handled by the DNA glycosylase OGG1 when paired with cytosine, initiating the base excision repair pathway. Since 8-oxoG neither significantly impacts the DNA structure nor blocks transcription and replication, its detection requires a careful inspection of each base pair by OGG1. By monitoring this lesion search process in vitro and in living cells, we uncover a tight coordination between several conserved amino acids encircling the DNA. More specifically, we show that the N149-151 motif, on the target strand, as well as residues R154 and R204, on the opposite strand, both regulate OGG1 engagement on the DNA to ensure fast Y203-mediated base unstacking, a prerequisite for efficient 8-oxoG detection. These findings highlight the mechanisms that enable OGG1 to maintain rapid DNA sampling kinetics while preserving specificity for 8-oxoG in the context of the chromatin architecture within the nucleus.

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Publication Details

Journal
Cell Reports
Published
2026-01-21
DOI
https://doi.org/10.1016/j.celrep.2025.116872
Primary Topic
DNA Repair Mechanisms
Type
article
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article

A coordinated haptic mechanism ensures efficient DNA sampling by the 8-oxoguanine glycosylase OGG1

Virginie Gaudon, F Coste, Catherine Chapuis, Anna Campalans et al.
Cell Reports
DNA Repair Mechanisms
article

A coordinated haptic mechanism ensures efficient DNA sampling by the 8-oxoguanine glycosylase OGG1

Virginie Gaudon, F Coste, Catherine Chapuis, Anna Campalans, B. Castaing, Ostiane D’Augustin, Jacques Hubert, Despoina Maria Chousianiti, Nicolas Bigot, Maximilien Martinez, Ana Gil Quevedo, Anne-Marie Di Guilmi, Sébastien Huet
article en

Abstract

7,8-Dihydro-8-oxoguanine (8-oxoG), a frequent mutagenic base modification occurring upon oxidative stress, is handled by the DNA glycosylase OGG1 when paired with cytosine, initiating the base excision repair pathway. Since 8-oxoG neither significantly impacts the DNA structure nor blocks transcription and replication, its detection requires a careful inspection of each base pair by OGG1. By monitoring this lesion search process in vitro and in living cells, we uncover a tight coordination between several conserved amino acids encircling the DNA. More specifically, we show that the N149-151 motif, on the target strand, as well as residues R154 and R204, on the opposite strand, both regulate OGG1 engagement on the DNA to ensure fast Y203-mediated base unstacking, a prerequisite for efficient 8-oxoG detection. These findings highlight the mechanisms that enable OGG1 to maintain rapid DNA sampling kinetics while preserving specificity for 8-oxoG in the context of the chromatin architecture within the nucleus.

Cell ReportsVol. 45(2)
Université d'Orléans (FR), Centre National de la Recherche Scientifique (FR), Université Paris Cité (FR), Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR), Université Paris-Saclay (FR), CEA Paris-Saclay - Etablissement de Fontenay-aux-roses (FR), Centre de Biophysique Moléculaire (FR), Institut de génétique et de développement de Rennes (FR), CEA Paris-Saclay (FR), Institut de Radiobiologie Cellulaire et Moléculaire (FR)
Openalex Percentile: Top 80%
DNA Repair Mechanisms
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