ArticleStructure (London, England : 1993)2016
Structures of DNA Polymerase Mispaired DNA Termini Transitioning to Pre-catalytic Complexes Support an Induced-Fit Fidelity Mechanism.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 36 citations in OpenAlex.
- Insights into the A-C Mismatch Conformational Ensemble in Duplex DNA and its Role in Genetic Processes through a Structure-based Review.Journal of molecular biology · 2024Review
- Biochemical and structural characterization of Fapy•dG replication by Human DNA polymerase β.Nucleic acids research · 2024Article
- Correction of non-random mutational biases along a linear bacterial chromosome by the mismatch repair endonuclease NucS.Nucleic acids research · 2024Article
- AUF1 Recognizes 8-Oxo-Guanosine Embedded in DNA and Stimulates APE1 Endoribonuclease Activity.Antioxidants & redox signaling · 2023Article
- Polβ/XRCC1 heterodimerization dictates DNA damage recognition and basal Polβ protein levels without interfering with mouse viability or fertility.DNA repair · 2023Article
- Structures of LIG1 that engage with mutagenic mismatches inserted by polβ in base excision repair.Nature communications · 2022Article
- Structural and functional insight into mismatch extension by human DNA polymerase α.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- History of DNA polymerase β X-ray crystallography.DNA repair · 2020Review
- The ligation of pol β mismatch insertion products governs the formation of promutagenic base excision DNA repair intermediates.Nucleic acids research · 2020Article
- Molecular and structural characterization of oxidized ribonucleotide insertion into DNA by human DNA polymerase β.The Journal of biological chemistry · 2020Article
- DNA polymerase β nucleotide-stabilized template misalignment fidelity depends on local sequence context.The Journal of biological chemistry · 2020Article
- A pre-catalytic non-covalent step governs DNA polymerase β fidelity.Nucleic acids research · 2019Article
- Promutagenicity of 8-Chloroguanine, A Major Inflammation-Induced Halogenated DNA Lesion.Molecules (Basel, Switzerland) · 2019Article
- Polymorphic G:G mismatches act as hotspots for inducing right-handed Z DNA by DNA intercalation.Nucleic acids research · 2019Article
- Apurinic/apyrimidinic (AP) endonuclease 1 processing of AP sites with 5' mismatches.Acta crystallographica. Section D, Structural biology · 2018Article
- Activation of the mismatch-specific endonuclease EndoMS/NucS by the replication clamp is required for high fidelity DNA replication.Nucleic acids research · 2018Article
- Structures of a DNA Polymerase Inserting Therapeutic Nucleotide Analogues.Chemical research in toxicology · 2017Article
- Modulating the DNA polymerase β reaction equilibrium to dissect the reverse reaction.Nature chemical biology · 2017Article
- Review
- Capturing a mammalian DNA polymerase extending from an oxidized nucleotide.Nucleic acids research · 2017Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
High-fidelity DNA synthesis requires that polymerases display a strong preference for right nucleotide insertion. When the wrong nucleotide is inserted, the polymerase deters extension from the mismatched DNA terminus. Twenty-three crystallographic structures of DNA polymerase β with terminal template-primer mismatches were determined as binary DNA and ternary pre-catalytic substrate complexes. These structures indicate that the mismatched termini adopt various distorted conformations that attempt to satisfy stacking and hydrogen-bonding interactions. The binary complex structures indicate an induced strain in the mismatched template nucleotide. Addition of a non-hydrolyzable incoming nucleotide stabilizes the templating nucleotide with concomitant strain in the primer terminus. Several dead-end ternary complex structures suggest that DNA synthesis might occur as the enzyme transitions from an open to a closed complex. The structures are consistent with an induced-fit mechanism where a mismatched terminus is misaligned relative to the correct incoming nucleotide to deter or delay further DNA synthesis.
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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.