ArticleArchives of biochemistry and biophysics2012
Stabilization of the Escherichia coli DNA polymerase III ε subunit by the θ subunit favors in vivo assembly of the Pol III catalytic core.
Article in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Peptides inhibiting the assembly of monomeric human l-lactate dehydrogenase into catalytically active homotetramer decrease the synthesis of lactate in cultured cells.Protein science : a publication of the Protein Society · 2024Article
- High-yield production in Escherichia coli and convenient purification of a candidate vaccine against SARS-CoV-2.Biotechnology letters · 2022Article
- Understanding biochemical processes in the presence of sub-diffusive behavior of biomolecules in solution and living cells.Biophysical reviews · 2019Review
- The thumb domain is not essential for the catalytic action of HoLaMa DNA polymerase.The protein journal · 2017Article
- Dual role of imidazole as activator/inhibitor of sweet almond (Biochemistry and biophysics reports · 2017Article
- Single-molecule mechanochemical characterization of E. coli pol III core catalytic activity.Protein science : a publication of the Protein Society · 2017Article
- The DnaE polymerase from Deinococcus radiodurans features RecA-dependent DNA polymerase activity.Bioscience reports · 2016Article
- Polymerase manager protein UmuD directly regulates Escherichia coli DNA polymerase III α binding to ssDNA.Nucleic acids research · 2013Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Escherichia coli DNA polymerase III holoenzyme (HE) contains a core polymerase consisting of three subunits: α (polymerase), ε (3'-5' exonuclease), and θ. Genetic experiments suggested that θ subunit stabilizes the intrinsically labile ε subunit and, furthermore, that θ might affect the cellular amounts of Pol III core and HE. Here, we provide biochemical evidence supporting this model by analyzing the amounts of the relevant proteins. First, we show that a ΔholE strain (lacking θ subunit) displays reduced amounts of free ε. We also demonstrate the existence of a dimer of ε, which may be involved in the stabilization of the protein. Second, θ, when overexpressed, dissociates the ε dimer and significantly increases the amount of Pol III core. The stability of ε also depends on cellular chaperones, including DnaK. Here, we report that: (i) temperature shift-up of ΔdnaK strains leads to rapid depletion of ε, and (ii) overproduction of θ overcomes both the depletion of ε and the temperature sensitivity of the strain. Overall, our data suggest that ε is a critical factor in the assembly of Pol III core, and that this is role is strongly influenced by the θ subunit through its prevention of ε degradation.
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Registered trials
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