Structural analysis of a eukaryotic sliding DNA clamp–clamp loader complex

Gregory D. Bowman, Mike O'Donnell and John Kuriyan ()
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Gregory D. Bowman: University of California
Mike O'Donnell: The Rockefeller University
John Kuriyan: University of California

Nature, 2004, vol. 429, issue 6993, 724-730

Abstract: Abstract Sliding clamps are ring-shaped proteins that encircle DNA and confer high processivity on DNA polymerases. Here we report the crystal structure of the five-protein clamp loader complex (replication factor-C, RFC) of the yeast Saccharomyces cerevisiae, bound to the sliding clamp (proliferating cell nuclear antigen, PCNA). Tight interfacial coordination of the ATP analogue ATP-γS by RFC results in a spiral arrangement of the ATPase domains of the clamp loader above the PCNA ring. Placement of a model for primed DNA within the central hole of PCNA reveals a striking correspondence between the RFC spiral and the grooves of the DNA double helix. This model, in which the clamp loader complex locks onto primed DNA in a screw-cap-like arrangement, provides a simple explanation for the process by which the engagement of primer–template junctions by the RFC:PCNA complex results in ATP hydrolysis and release of the sliding clamp on DNA.

Date: 2004
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DOI: 10.1038/nature02585

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