ArticleNucleic acids research2008
The proofreading exonuclease subunit epsilon of Escherichia coli DNA polymerase III is tethered to the polymerase subunit alpha via a flexible linker.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Subunit-specific isotope labelling of heteromeric complexes using cell-free protein expression: application to the 760 kDa ClpXP molecular machine.RSC chemical biology · 2026Article
- The β2 clamp in the Mycobacterium tuberculosis DNA polymerase III αβ2ε replicase promotes polymerization and reduces exonuclease activity.Scientific reports · 2016Article
- Mutations that Separate the Functions of the Proofreading Subunit of the Escherichia coli Replicase.G3 (Bethesda, Md.) · 2015Article
- The multifaceted benefits of protein co-expression in Escherichia coli.Journal of visualized experiments : JoVE · 2015Article
- Replicative DNA polymerases.Cold Spring Harbor perspectives in biology · 2013Review
- A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode.The EMBO journal · 2013Article
- Architecture of the Pol III-clamp-exonuclease complex reveals key roles of the exonuclease subunit in processive DNA synthesis and repair.The EMBO journal · 2013Article
- 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.Nucleic acids research · 2013Article
- SOS induction and mutagenesis by dnaQ missense alleles in wild type cells.Mutation research · 2012Article
- The DNA Exonucleases of Escherichia coli.EcoSal Plus · 2011Article
- Essential biological processes of an emerging pathogen: DNA replication, transcription, and cell division in Acinetobacter spp.Microbiology and molecular biology reviews : MMBR · 2010Review
- Glutarate and N-acetyl-L-glutamate buffers for cell-free synthesis of selectively 15N-labelled proteins.Journal of biomolecular NMR · 2009Article
- A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader.Nucleic acids research · 2009Article
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5 authors.
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Abstract
Escherichia coli DNA polymerase III holoenzyme is composed of 10 different subunits linked by noncovalent interactions. The polymerase activity resides in the alpha-subunit. The epsilon-subunit, which contains the proofreading exonuclease site within its N-terminal 185 residues, binds to alpha via a segment of 57 additional C-terminal residues, and also to theta, whose function is less well defined. The present study shows that theta greatly enhances the solubility of epsilon during cell-free synthesis. In addition, synthesis of epsilon in the presence of theta and alpha resulted in a soluble ternary complex that could readily be purified and analyzed by NMR spectroscopy. Cell-free synthesis of epsilon from PCR-amplified DNA coupled with site-directed mutagenesis and selective 15N-labeling provided site-specific assignments of NMR resonances of epsilon that were confirmed by lanthanide-induced pseudocontact shifts. The data show that the proofreading domain of epsilon is connected to alpha via a flexible linker peptide comprising over 20 residues. This distinguishes the alpha : epsilon complex from other proofreading polymerases, which have a more rigid multidomain structure.
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