ArticleProtein science : a publication of the Protein Society2004
Application of electrospray ionization mass spectrometry to study the hydrophobic interaction between the epsilon and theta subunits of DNA polymerase III.
Article in Protein science : a publication of the Protein Society, 2004. 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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8 citing papers in PubMed, 25 citations in OpenAlex.
- Biodereplication of Antiplasmodial Extracts: Application of the Amazonian Medicinal PlantMolecules (Basel, Switzerland) · 2022Article
- Refining the Structural Model of a Heterohexameric Protein Complex: Surface Induced Dissociation and Ion Mobility Provide Key Connectivity and Topology Information.ACS central science · 2015Article
- Escherichia coli single-stranded DNA-binding protein: nanoESI-MS studies of salt-modulated subunit exchange and DNA binding transactions.Journal of the American Society for Mass Spectrometry · 2013Article
- Effect of macromolecular crowding on protein binding stability: modest stabilization and significant biological consequences.Biophysical journal · 2009Article
- Mutator and antimutator effects of the bacteriophage P1 hot gene product.Journal of bacteriology · 2006Article
- Structure of the theta subunit of Escherichia coli DNA polymerase III in complex with the epsilon subunit.Journal of bacteriology · 2006Article
- Nuclear magnetic resonance solution structure of the Escherichia coli DNA polymerase III theta subunit.Journal of bacteriology · 2005Article
- The bacteriophage P1 hot gene product can substitute for the Escherichia coli DNA polymerase III {theta} subunit.Journal of bacteriology · 2005Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interactions between the N-terminal domain of the epsilon (epsilon186) and theta subunits of DNA polymerase III of Escherichia coli were investigated using electrospray ionization mass spectrometry. The epsilon186-theta complex was stable in 9 M ammonium actetate (pH 8), suggesting that hydrophobic interactions have a predominant contribution to the stability of the complex. Addition of primary alkanols to epsilon186-theta in 0.1 M ammonium acetate (pH 8), led to dissociation of the complex, as observed in the mass spectrometer. The concentrations of methanol, ethanol, and 1-propanol required to dissociate 50% of the complex were 8.9 M, 4.8 M, and 1.7 M, respectively. Closer scrutiny of the effect of alkanols on epsilon186, theta, and epsilon186-theta showed that epsilon186 formed soluble aggregates prior to precipitation, and that the association of epsilon186 with theta stabilized epsilon186. In-source collision-induced dissociation experiments and other results suggested that the epsilon186-theta complex dissociated in the mass spectrometer, and that the stability (with respect to dissociation) of the complex in vacuo was dependent on the solution from which it was sampled.
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