Two sliding clamp units are attached to the ends of the wire and onto the ring.
Crystal structures show how the sliding clamp that facilitates processive replication is loaded onto DNA.
The sliding clamp is a key component of DNA polymerase III Pol IIII) required for genome replication.
To extend our understanding of the structure/function relationship of the sliding clamp, we solved the crystal structure of the sliding clamp from Mycobacterium tuberculosis (M. tuberculosis), a human pathogen that causes most cases of tuberculosis (TB).
The sliding clamp from M. tuberculosis forms a ring-shaped head-to-tail dimer with three domains per subunit.
Thus, the sliding clamp seems to have evolved as an efficient mechanism for ensuring proficient DNA replication.
DNA polymerase III β sliding clamp's ability to function with diverse DNA repair proteins and cell cycle-control proteins make it a potential drug target [39].
The core replication proteins in all cell types include a helicase, primase, DNA polymerases, sliding clamp, clamp loader, and single-strand binding (SSB) protein.
In eukaryotic DNA replication, replication factor-C (RFC) acts as the clamp loader, which correctly installs the sliding clamp onto DNA strands at replication forks.
The sliding clamp, PCNA, of the archaeon Sulfolobus solfataricus P2 is a heterotrimer of three distinct subunits (PCNA1, 2, and 3) that assembles in a defined manner.
