ArticleNucleic acids research2007
Solution structure of Domains IVa and V of the tau subunit of Escherichia coli DNA polymerase III and interaction with the alpha subunit.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 38 citations in OpenAlex.
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- 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
- cryo-EM structures of theeLife · 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
- Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis.Nucleic acids research · 2013Article
- Structure of the PolIIIα-τc-DNA complex suggests an atomic model of the replisome.Structure (London, England : 1993) · 2013Article
- Selective disruption of the DNA polymerase III α-β complex by the umuD gene products.Nucleic acids research · 2012Article
- Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.Current drug targets · 2012Review
- Engineering [Ln(DPA)3] 3- binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions.Journal of biomolecular NMR · 2011Article
- Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O.Journal of biomolecular NMR · 2011Article
- dnaX36 Mutator of Escherichia coli: effects of the {tau} subunit of the DNA polymerase III holoenzyme on chromosomal DNA replication fidelity.Journal of bacteriology · 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
- Allosteric regulation of the primase (DnaG) activity by the clamp-loader (tau) in vitro.Molecular microbiology · 2009Article
- The proofreading exonuclease subunit epsilon of Escherichia coli DNA polymerase III is tethered to the polymerase subunit alpha via a flexible linker.Nucleic acids research · 2008Article
- Measurement of dissociation constants of high-molecular weight protein-protein complexes by transferred 15N-relaxation.Journal of biomolecular NMR · 2007Article
- The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit.Nucleic acids research · 2007Article
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5 authors at 1 institution in 1 country.
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Abstract
The solution structure of the C-terminal Domain V of the tau subunit of E. coli DNA polymerase III was determined by nuclear magnetic resonance (NMR) spectroscopy. The fold is unique to tau subunits. Amino acid sequence conservation is pronounced for hydrophobic residues that form the structural core of the protein, indicating that the fold is representative for tau subunits from a wide range of different bacteria. The interaction between the polymerase subunits tau and alpha was studied by NMR experiments where alpha was incubated with full-length C-terminal domain (tau(C)16), and domains shortened at the C-terminus by 11 and 18 residues, respectively. The only interacting residues were found in the C-terminal 30-residue segment of tau, most of which is structurally disordered in free tau(C)16. Since the N- and C-termini of the structured core of tau(C)16 are located close to each other, this limits the possible distance between alpha and the pentameric deltatau2gammadelta' clamp-loader complex and, hence, between the two alpha subunits involved in leading- and lagging-strand DNA synthesis. Analysis of an N-terminally extended construct (tau(C)22) showed that tau(C)14 presents the only part of Domains IVa and V of tau which comprises a globular fold in the absence of other interaction partners.
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