Article
Elucidation of the epsilon-theta subunit interface of Escherichia coli DNA polymerase III by NMR spectroscopy.
Biochemistry - 8 Apr 2003
DeRose Eugene F, Darden Thomas, Harvey Scott, Gabel Scott, Perrino Fred W, Schaaper Roel M, London Robert E
Abstract excerpt
The DNA polymerase III holoenzyme (HE) is the primary replicative polymerase of Escherichia coli. The epsilon (epsilon) subunit of HE provides the 3'-->5' exonucleolytic proofreading activity for this complex. Epsilon consists of two domains: an N-terminal domain containing the proofreading exonuclease activity (residues 1-186) and a C-terminal domain required for binding to the polymerase (alpha) subunit...
Topics
- Amino Acid Sequence
- Binding Sites
- Catalytic Domain
- DNA Replication
- Enzyme Stability
- Escherichia coli
- Exodeoxyribonuclease V
- Exodeoxyribonucleases
- Exonucleases
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Nuclear Magnetic Resonance, Biomolecular