KAUST DepartmentDesert Agriculture Initiative
Biological and Environmental Sciences and Engineering (BESE) Division
Laboratory of DNA Replication and Recombination
Permanent link to this recordhttp://hdl.handle.net/10754/627269
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AbstractReplicative polymerases achieve highly processive DNA synthesis by binding to a clamp-like processivity factor that is topologically linked to DNA. The eukaryotic processivity clamp, proliferating cell nuclear antigen (PCNA), exists mostly as a closed ring in solution. Replication factor C (RFC), a five-subunit ATP-dependent protein complex, mediates PCNA opening in solution (assembly stage) and closing onto the primer-template (disassembly stage). In the assembly stage, RFC binding to ATP causes conformational changes that trigger RFC to form a complex with PCNA. PCNA is then cracked open at one subunit interface, and both RFC and PCNA adopt an extended spiral structure with a chamber that selects for a primer-template DNA structure. Binding of RFC/PCNA to DNA triggers the disassembly stage by stimulating ATP hydrolysis. Subsequent conformational changes in RFC and PCNA lead to the closing of PCNA onto the primer-template and the dissociation of RFC.
CitationOke M, Zaher MS, Hamdan SM (2018) PCNA Loading by RFC, Mechanism of. Molecular Life Sciences: 861–866. Available: http://dx.doi.org/10.1007/978-1-4614-1531-2_137.
PublisherSpringer New York
JournalMolecular Life Sciences