ArticleThe Journal of biological chemistry2015
Conformational Dynamics of DNA Repair by Escherichia coli Endonuclease III.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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
19 citing papers in PubMed, 44 citations in OpenAlex.
- Biochemical, structural and mutational landscapes of base excision repair enzymes and cancer: from atomic resolution to tumor signatures.International journal of radiation biology · 2026Review
- An Insight into the Mechanism of DNA Cleavage by DNA Endonuclease from the Hyperthermophilic ArchaeonInternational journal of molecular sciences · 2024Article
- Probing the Conformational Restraints of DNA Damage Recognition with β-L-Nucleotides.International journal of molecular sciences · 2024Article
- Recognition of a Clickable Abasic Site Analog by DNA Polymerases and DNA Repair Enzymes.International journal of molecular sciences · 2022Article
- Biochemical and functional characterization of an endonuclease III from Thermococcus barophilus Ch5.World journal of microbiology & biotechnology · 2022Article
- A Low-Activity Polymorphic Variant of Human NEIL2 DNA Glycosylase.International journal of molecular sciences · 2022Article
- Caught in motion: human NTHL1 undergoes interdomain rearrangement necessary for catalysis.Nucleic acids research · 2021Article
- Cytotoxic and genotoxic evaluation of cotinine using human neuroblastoma cells (SH-SY5Y).Genetics and molecular biology · 2020Article
- The Role of Active-Site Residues Phe98, His239, and Arg243 in DNA Binding and in the Catalysis of Human Uracil-DNA Glycosylase SMUG1.Molecules (Basel, Switzerland) · 2019Article
- Substrate specificity of human apurinic/apyrimidinic endonuclease APE1 in the nucleotide incision repair pathway.Nucleic acids research · 2018Article
- Article
- Hide and seek: How do DNA glycosylases locate oxidatively damaged DNA bases amidst a sea of undamaged bases?Free radical biology & medicine · 2017Review
- Fluorescent RNA cytosine analogue - an internal probe for detailed structure and dynamics investigations.Scientific reports · 2017Article
- Mutational and Kinetic Analysis of Lesion Recognition by Escherichia coli Endonuclease VIII.Genes · 2017Article
- Probing the activity of NTHL1 orthologs by targeting conserved amino acid residues.DNA repair · 2017Article
- Visualizing the Search for Radiation-damaged DNA Bases in Real Time.Radiation physics and chemistry (Oxford, England : 1993) · 2016Article
- Twist-open mechanism of DNA damage recognition by the Rad4/XPC nucleotide excision repair complex.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A dynamic checkpoint in oxidative lesion discrimination by formamidopyrimidine-DNA glycosylase.Nucleic acids research · 2016Article
- Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli endonuclease III (Endo III or Nth) is a DNA glycosylase with a broad substrate specificity for oxidized or reduced pyrimidine bases. Endo III possesses two types of activities: N-glycosylase (hydrolysis of the N-glycosidic bond) and AP lyase (elimination of the 3'-phosphate of the AP-site). We report a pre-steady-state kinetic analysis of structural rearrangements of the DNA substrates and uncleavable ligands during their interaction with Endo III. Oligonucleotide duplexes containing 5,6-dihydrouracil, a natural abasic site, its tetrahydrofuran analog, and undamaged duplexes carried fluorescent DNA base analogs 2-aminopurine and 1,3-diaza-2-oxophenoxazine as environment-sensitive reporter groups. The results suggest that Endo III induces several fast sequential conformational changes in DNA during binding, lesion recognition, and adjustment to a catalytically competent conformation. A comparison of two fluorophores allowed us to distinguish between the events occurring in the damaged and undamaged DNA strand. Combining our data with the available structures of Endo III, we conclude that this glycosylase uses a multistep mechanism of damage recognition, which likely involves Gln(41) and Leu(81) as DNA lesion sensors.
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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.