The sliding clamp of DNA polymerase III holoenzyme encircles DNA.

DNA polymerases that duplicate chromosomes are remarkably processive multiprotein machines. These replicative polymerases remain in continuous association with the DNA over tens to hundreds of kilobases. What is the chemical basis of their strong grip to the template? The mystery behind the high processivity of the replicative polymerase of the Escherichia coli chromosome, DNA polymerase III holoenzyme, lies in a ring-shaped protein that acts as a sliding clamp for the rest of the machinery. A ring-shaped sliding clamp is likely to be general for replicative polymerases, being formed by the PCNA protein of yeast and humans and the gene 45 protein of T4 phage. A short summary of the subunit organization of four replicative polymerases, presented below, is necessary to appreciate the similarity between the prokaryotic and eukaryotic systems. Then the detailed mechanism by which the E. coli DNA polymerase III holoenzyme achieves its high processivity will be described, followed by a consideration of whether other polymerases spanning the evolutionary spectrum utilize a common mechanism.

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