title: NMR resonance assignments for the N-terminal domain of the δ subunit of the E. coli γ clamp loader complex.
abstract: The β-clamp protein and the γ clamp loader complex are essential components of bacterial DNA replication machinery. The β-clamp is a ring-shaped homodimer that encircles DNA and increases the efficiency of replication by providing a binding platform for DNA polymerases and other replication-related proteins. The β-clamp is loaded onto DNA by the five-subunit γ clamp loader complex in a multi-step ATP-dependent process. The initial steps of this process involve the cooperative binding of the β-clamp by the five subunits of ATP-bound clamp loader, which induces or traps an open conformation of the clamp. Remarkably, the δ subunit of the E. coli clamp loader, or even its 140 residue N-terminal domain (called mini-δ), alone can shift conformational equilibrium of the β-clamp towards the open state. Here we report nearly complete backbone and side-chain1H,13C and15N NMR resonance assignments of mini-δ that will facilitate NMR studies of the mechanisms of β-clamp opening and its loading on DNA by the clamp loader.
authors.affiliation: Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, 06030, USA.
authors.forename: Esmael M
authors.initials: EM
authors.lastname: Alyami
authors.affiliation: Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, 06030, USA.
authors.forename: Alessandro A
authors.initials: AA
authors.lastname: Rizzo
authors.affiliation: Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA, 02115, USA.
authors.forename: Penny J
authors.initials: PJ
authors.lastname: Beuning
authors.affiliation: Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, 06030, USA. korzhniev@uchc.edu.
authors.forename: Dmitry M
authors.initials: DM
authors.lastname: Korzhnev
mesh_terms: D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D000072417:Protein Domains; D021122:Protein Subunits / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; D021122:Protein Subunits
keywords: Bacterial DNA replication; Conformational dynamics; Pol III holoenzyme; Processivity β-clamp; Protein–protein interactions; γ clamp loader complex