Synopsis
Replicative 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.
Introduction
Proliferating...
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Oke, M., Zaher, M.S., Hamdan, S.M. (2014). Mechanism of PCNA Loading by RFC. In: Bell, E. (eds) Molecular Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6436-5_137-1
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DOI: https://doi.org/10.1007/978-1-4614-6436-5_137-1
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