The Bacteriophage P1 hot Gene Product Can Substitute for the Escherichia coli DNA Polymerase III θ Subunit

The Bacteriophage P1 hot Gene Product Can Substitute for the Escherichia coli DNA Polymerase III Subunit

The bacteriophage P1 hot gene product can substitute for the Escherichia coli DNA polymerase III {theta} subunit.

The theta subunit (holE gene product) of Escherichia coli DNA polymerase (Pol) III holoenzyme is a tightly bound component of the polymerase core. Within the core (alpha-epsilon-theta), the alpha and epsilon subunits carry the DNA polymerase and 3' proofreading functions, respectively, while the precise function of theta is unclear. holE homologs are present in genomes of other enterobacteriae,...

The Subunit of Escherichia coli DNA Polymerase III: a Role in Stabilizing the ε Proofreading Subunit

The function of the subunit of Escherichia coli DNA polymerase III holoenzyme is not well established. is a tightly bound component of the DNA polymerase III core, which contains the subunit (polymerase), the subunit (3 35 exonuclease), and the subunit, in the linear order . Previous studies have shown that the subunit is not essential, as strains carrying a deletion of the holE gene (which enc...

Structure of the Subunit of Escherichia coli DNA Polymerase III in Complex with the ε Subunit

Structure of the Subunit of Escherichia coli DNA Polymerase III in Complex with the ε Subunit Max A. Keniry,* Ah Young Park, Elisabeth A. Owen, Samir M. Hamdan, Guido Pintacuda, Gottfried Otting, and Nicholas E. Dixon Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia, and Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 ...

DNA Polymerase III of Escherichia coli

DNA polymerase III, the core of the DNA polymerase III holoenzyme, has been purified Z&000-fold to 97% homogeneity from Escherichiu coli HMS-83. The enzyme contains three subunits: (Y, E, and 0 of 140,000, 25,000, and 10,000 daltons, respectively. The cy subunit has been previously shown to be a component of both DNA polymerase III and the more complex DNA polymerase III holoenzyme (Livingston,...