Abstract
The ?-clamp protein and the ? clamp loader complex are essential components of bacterial DNA replication machinery. The ?-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 ?-clamp is loaded onto DNA by the five-subunit ? clamp loader complex in a multi-step ATP-dependent process. The initial steps of this process involve the cooperative binding of the ?-clamp by the five subunits of ATP-bound clamp loader, which induces or traps an open conformation of the clamp. Remarkably, the ? subunit of the E. coli clamp loader, or even its 140 residue N-terminal domain (called mini-?), alone can shift conformational equilibrium of the ?-clamp towards the open state. Here we report nearly complete backbone and side-chain (1)H, (13)C and (15)N NMR resonance assignments of mini-? that will facilitate NMR studies of the mechanisms of ?-clamp opening and its loading on DNA by the clamp loader.
PMID: 28265855 [PubMed - as supplied by publisher]
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