ArticleNucleic acids research2026
Linker-mediated conformational coupling drives lesion recognition in MutY glycosylase.
Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- DNA Damage Recognition by Bacterial and Human Adenine-DNA Glycosylases: Insights from Non-Canonical Substrates.Biomolecules · 2026Article
- Structural Basis for Nucleobase Activation by the Adenine DNA Glycosylase MutY.Chembiochem : a European journal of chemical biology · 2026Article
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Authors and funding
3 authors.
Funding
Abstract
Maintaining genome stability requires accurate recognition of oxidative DNA damage. MutY glycosylase prevents mutagenic G:C→T:A transversions by excising adenine mispaired with 8-oxoguanine (8OG). While crystal structures have captured two endpoint states-the encounter complex (EC) and the lesion recognition complex (LRC)-the dynamic steps connecting these states have remained unresolved. Using large-scale enhanced-sampling molecular dynamics simulations, we mapped the free energy landscapes of lesion recognition and identified a dominant pathway in which adenine and 8OG undergo synchronized glycosidic rotations orchestrated by a flexible interdomain linker. This linker coordinates adenine flipping, dual base isomerization, and interdomain rearrangements into a unified, streamlined process that secures extrahelical adenine in a catalytically competent LRC state. These findings reveal a previously unrecognized mechanistic framework for MutY and related glycosylases with flexible linkers, highlighting how such linkers guide lesion interrogation and reinforce genome integrity.
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