ArticleNucleic acids research2013
Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, epsilon, θ and β reveals a highly flexible arrangement of the proofreading domain.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
- Diversity and distribution of bacterial DNA polymerases.Nucleic acids research · 2026Article
- Escherichia coli DNA replication: the old model organism still holds many surprises.FEMS microbiology reviews · 2024Review
- During Translesion Synthesis, Escherichia coli DinB89 (T120P) Alters Interactions of DinB (Pol IV) with Pol III Subunit Assemblies and SSB, but Not with the β Clamp.Journal of bacteriology · 2022Article
- The Mutant βJournal of bacteriology · 2021Article
- Novel Antibiotics Targeting Bacterial Replicative DNA Polymerases.Antibiotics (Basel, Switzerland) · 2020Review
- A structural view of bacterial DNA replication.Protein science : a publication of the Protein Society · 2019Review
- Reduced structural flexibility for an exonuclease deficient DNA polymerase III mutant.Physical chemistry chemical physics : PCCP · 2018Article
- Single-molecule mechanochemical characterization of E. coli pol III core catalytic activity.Protein science : a publication of the Protein Society · 2017Article
- Article
- Error-prone DnaE2 Balances the Genome Mutation Rates inFrontiers in microbiology · 2017Article
- DNA Polymerases Divide the Labor of Genome Replication.Trends in cell biology · 2016Review
- Exchange between Escherichia coli polymerases II and III on a processivity clamp.Nucleic acids research · 2016Article
- The β2 clamp in the Mycobacterium tuberculosis DNA polymerase III αβ2ε replicase promotes polymerization and reduces exonuclease activity.Scientific reports · 2016Article
- cryo-EM structures of theeLife · 2015Article
- A Genetic Selection for dinB Mutants Reveals an Interaction between DNA Polymerase IV and the Replicative Polymerase That Is Required for Translesion Synthesis.PLoS genetics · 2015Article
- DNA Polymerase α Subunit Residues and Interactions Required for Efficient Initiation Complex Formation Identified by a Genetic Selection.The Journal of biological chemistry · 2015Article
- Mutations that Separate the Functions of the Proofreading Subunit of the Escherichia coli Replicase.G3 (Bethesda, Md.) · 2015Article
- Effects of DNA3'pp5'G capping on 3' end repair reactions and of an embedded pyrophosphate-linked guanylate on ribonucleotide surveillance.Nucleic acids research · 2015Article
- DNA polymerase IV mediates efficient and quick recovery of replication forks stalled at N2-dG adducts.Nucleic acids research · 2014Article
- Polymerase exchange on single DNA molecules reveals processivity clamp control of translesion synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A complex of the three (αεθ) core subunits and the β2 sliding clamp is responsible for DNA synthesis by Pol III, the Escherichia coli chromosomal DNA replicase. The 1.7 Å crystal structure of a complex between the PHP domain of α (polymerase) and the C-terminal segment of ε (proofreading exonuclease) subunits shows that ε is attached to α at a site far from the polymerase active site. Both α and ε contain clamp-binding motifs (CBMs) that interact simultaneously with β2 in the polymerization mode of DNA replication by Pol III. Strengthening of both CBMs enables isolation of stable αεθ:β2 complexes. Nuclear magnetic resonance experiments with reconstituted αεθ:β2 demonstrate retention of high mobility of a segment of 22 residues in the linker that connects the exonuclease domain of ε with its α-binding segment. In spite of this, small-angle X-ray scattering data show that the isolated complex with strengthened CBMs has a compact, but still flexible, structure. Photo-crosslinking with p-benzoyl-L-phenylalanine incorporated at different sites in the α-PHP domain confirm the conformational variability of the tether. Structural models of the αεθ:β2 replicase complex with primer-template DNA combine all available structural data.
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