ArticleThe Journal of biological chemistry2010
Uracil DNA glycosylase activity on nucleosomal DNA depends on rotational orientation of targets.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 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
58 citing papers in PubMed, 97 citations in OpenAlex.
- Navigating the base excision repair pathway in chromatin-focus on oxidative DNA damage.Nucleic acids research · 2026Review
- Base excision repair in chromatin: A tug-of-war for DNA damage.DNA repair · 2025Review
- Initiation of base excision repair is modulated by nucleosome occupancy modifying sequences.DNA repair · 2025Article
- A Balancing Act: Thymine DNA Glycosylase Combines Sequence and Rotational Preferences To Define Lesion Excision in the Nucleosome Core Particle.Biochemistry · 2025Article
- Mechanisms of DNA Damage Recognition by UDG and PARP1 in the Nucleosome.Biomolecules · 2025Article
- Terminal deoxynucleotidyl transferase: Properties and applications.Engineering microbiology · 2025Review
- Ultraviolet damage and repair maps inGenome research · 2025Article
- Article
- New Discoveries on Protein Recruitment and Regulation during the Early Stages of the DNA Damage Response Pathways.International journal of molecular sciences · 2024Review
- Redox-Based Defect Detection in Packed DNA: Insights from Hybrid Quantum Mechanical/Molecular Mechanics Molecular Dynamics Simulations.Journal of chemical theory and computation · 2023Article
- Ionic strength modulates excision of uracil by SMUG1 from nucleosome core particles.DNA repair · 2023Article
- Structural basis for APE1 processing DNA damage in the nucleosome.Nature communications · 2022Article
- Histone variants H3.3 and H2A.Z/H3.3 facilitate excision of uracil from nucleosome core particles.DNA repair · 2022Article
- Obstacles and opportunities for base excision repair in chromatin.DNA repair · 2022Review
- Temporal dynamics of base excision/single-strand break repair protein complex assembly/disassembly are modulated by the PARP/NADCell reports · 2021Article
- The contribution of PARP1, PARP2 and poly(ADP-ribosyl)ation to base excision repair in the nucleosomal context.Scientific reports · 2021Article
- Comparison of the Base Excision and Direct Reversal Repair Pathways for Correcting 1,Chemical research in toxicology · 2020Article
- HECTD1 promotes base excision repair in nucleosomes through chromatin remodelling.Nucleic acids research · 2020Article
- Acetylation of the histone H3 tail domain regulates base excision repair on higher-order chromatin structures.Scientific reports · 2019Article
- Global Repair Profile of Human Alkyladenine DNA Glycosylase on Nucleosomes Reveals DNA Packaging Effects.ACS chemical biology · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The activity of uracil DNA glycosylases (UDGs), which recognize and excise uracil bases from DNA, has been well characterized on naked DNA substrates but less is known about activity in chromatin. We therefore prepared a set of model nucleosome substrates in which single thymidine residues were replaced with uracil at specific locations and a second set of nucleosomes in which uracils were randomly substituted for all thymidines. We found that UDG efficiently removes uracil from internal locations in the nucleosome where the DNA backbone is oriented away from the surface of the histone octamer, without significant disruption of histone-DNA interactions. However, uracils at sites oriented toward the histone octamer surface were excised at much slower rates, consistent with a mechanism requiring spontaneous DNA unwrapping from the nucleosome. In contrast to the nucleosome core, UDG activity on DNA outside the core DNA region was similar to that of naked DNA. Association of linker histone reduced activity of UDG at selected sites near where the globular domain of H1 is proposed to bind to the nucleosome as well as within the extra-core DNA. Our results indicate that some sites within the nucleosome core and the extra-core (linker) DNA regions represent hot spots for repair that could influence critical biological processes.
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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.