PCNA Loading by RFC, Mechanism of

Muse Oke, Manal Zaher, Samir Hamdan

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

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.
Original languageEnglish (US)
Title of host publicationMolecular Life Sciences
PublisherSpringer Nature
Pages861-866
Number of pages6
ISBN (Print)9781461415299
DOIs
StatePublished - Jan 30 2018

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